Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0006886 intracellular protein transport	IBA GO_REF:0000033	ACCEPT	Summary: Intracellular protein transport is a valid broad process for ARF1-dependent Golgi/TGN and COPI-related trafficking. Reason: This IBA term captures the conserved trafficking role of ARF1. It is broader than the PN retrograde-transport candidate but biologically sound. Supporting Evidence: Reactome:R-HSA-6811434 Retrograde traffic from the cis-Golgi to the ERGIC or the ER is mediated in part by microtubule-directed COPI-coated vesicles PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
GO:0005525 GTP binding	IBA GO_REF:0000033	ACCEPT	Summary: GTP binding is the nucleotide-binding state required for ARF1 activation and membrane-effector recruitment. Reason: This is a core biochemical property of ARF1 and is directly tied to ARF1-dependent coat recruitment and vesicle budding. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
GO:0005886 plasma membrane	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Plasma membrane association/activity is reported in signaling and PLD contexts but is not the primary ARF1 compartment. Reason: ARF1 can participate in plasma-membrane-linked signaling or trafficking, but the dominant conserved role is Golgi/TGN membrane trafficking. Supporting Evidence: PMID:8529647 The results indicate that ARF proteins and their nucleotide-exchange factor are apparently involved in the signalling pathway leading from mAChR activation to PLD stimulation in human embryonic kidney cells.
GO:0000139 Golgi membrane	IEA GO_REF:0000044	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0003924 GTPase activity	IEA GO_REF:0000002	ACCEPT	Summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle. Reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
GO:0003925 G protein activity	IEA GO_REF:0000003	ACCEPT	Summary: ARF1 is an ADP-ribosylation factor family small G protein whose active GTP-bound state recruits trafficking effectors. Reason: Although broader than GTPase activity, small G protein activity is an appropriate molecular-function description for ARF1. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
GO:0005525 GTP binding	IEA GO_REF:0000120	ACCEPT	Summary: GTP binding is the nucleotide-binding state required for ARF1 activation and membrane-effector recruitment. Reason: This is a core biochemical property of ARF1 and is directly tied to ARF1-dependent coat recruitment and vesicle budding. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
GO:0014069 postsynaptic density	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: Synaptic and postsynaptic-density annotations reflect transferred neuronal ARF1/PICK1 biology rather than the core conserved Golgi trafficking function. Reason: These annotations are plausible as specialized neuronal contexts, but they are not the main ARF1 function and are supported here by similarity rather than direct human ARF1 experiments. Supporting Evidence: file:human/ARF1/ARF1-notes.md Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
GO:0045202 synapse	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: Synaptic and postsynaptic-density annotations reflect transferred neuronal ARF1/PICK1 biology rather than the core conserved Golgi trafficking function. Reason: These annotations are plausible as specialized neuronal contexts, but they are not the main ARF1 function and are supported here by similarity rather than direct human ARF1 experiments. Supporting Evidence: file:human/ARF1/ARF1-notes.md Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
GO:0005515 protein binding	IPI PMID:10198630 Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domai...	MARK AS OVER ANNOTATED	Summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function. Reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
GO:0005515 protein binding	IPI PMID:14654833 Structural snapshots of the mechanism and inhibition of a gu...	MARK AS OVER ANNOTATED	Summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function. Reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
GO:0005515 protein binding	IPI PMID:17563369 Structure-based discovery of an inhibitor of Arf activation ...	MARK AS OVER ANNOTATED	Summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function. Reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
GO:0005515 protein binding	IPI PMID:19644450 The structural basis of Arf effector specificity: the crysta...	MARK AS OVER ANNOTATED	Summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function. Reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
GO:0005515 protein binding	IPI PMID:22981988 The BAR domain protein Arfaptin-1 controls secretory granule...	MARK AS OVER ANNOTATED	Summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function. Reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
GO:0005515 protein binding	IPI PMID:31467278 Maximizing binary interactome mapping with a minimal number ...	MARK AS OVER ANNOTATED	Summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function. Reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	MARK AS OVER ANNOTATED	Summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function. Reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
GO:0005515 protein binding	IPI PMID:36396045 Targeting ARF1-IQGAP1 interaction to suppress colorectal can...	MARK AS OVER ANNOTATED	Summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function. Reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
GO:0000287 magnesium ion binding	IEA GO_REF:0000107	ACCEPT	Summary: Magnesium binding is consistent with ARF1 nucleotide binding and GTPase chemistry. Reason: Small GTPases require Mg2+-coordinated nucleotide binding/hydrolysis; this is a supporting biochemical property rather than a standalone biological role. Supporting Evidence: file:human/ARF1/ARF1-notes.md The magnesium ion binding annotation is retained as a cofactor-level biochemical property of the nucleotide/GTPase mechanism, not as an independent biological role.
GO:0005794 Golgi apparatus	IEA GO_REF:0000120	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0005829 cytosol	IEA GO_REF:0000107	ACCEPT	Summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles. Reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state. Supporting Evidence: file:human/ARF1/ARF1-notes.md Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
GO:0012505 endomembrane system	IEA GO_REF:0000107	ACCEPT	Summary: Endomembrane localization is broad but consistent with ARF1 function at Golgi/TGN and related trafficking membranes. Reason: ARF1 acts on Golgi, TGN, and related endomembrane trafficking intermediates; this term is less specific than Golgi membrane but accurate. Supporting Evidence: file:human/ARF1/ARF1-notes.md Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation. Reactome:R-HSA-6811434 Retrograde traffic from the cis-Golgi to the ERGIC or the ER is mediated in part by microtubule-directed COPI-coated vesicles
GO:0030017 sarcomere	IEA GO_REF:0000107	REMOVE	Summary: Sarcomere localization is not supported by the reviewed ARF1 functional literature and is not part of the ARF1 trafficking model. Reason: This automatic transfer appears disconnected from ARF1 core Golgi/TGN trafficking and should not be retained without stronger direct evidence. Supporting Evidence: file:human/ARF1/ARF1-notes.md Sarcomere localization and mitotic cleavage furrow ingression are not supported as core ARF1 biology in this review; the curated evidence supports Golgi/TGN endomembrane trafficking instead.
GO:0032991 protein-containing complex	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: ARF1 forms transient regulatory complexes with effectors and regulators, but a generic protein-containing complex annotation is not informative. Reason: This term loses the biology of an active small GTPase recruiting coat/adaptor machinery. It should not be treated as a core complex-membership assertion. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein-containing complex annotations are treated as over-annotated because ARF1 forms transient regulatory complexes with coat, adaptor, GEF, and GAP machinery rather than acting as a stable structural complex subunit. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
GO:1990386 mitotic cleavage furrow ingression	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Mitotic cleavage furrow ingression is a possible specialized small-GTPase trafficking context but is not supported here by direct ARF1 evidence. Reason: The annotation is too specific for the available electronically transferred evidence and should not be considered core ARF1 biology. Supporting Evidence: file:human/ARF1/ARF1-notes.md Sarcomere localization and mitotic cleavage furrow ingression are not supported as core ARF1 biology in this review; the curated evidence supports Golgi/TGN endomembrane trafficking instead.
GO:0003925 G protein activity	IDA PMID:17687330 Glycosphingolipid synthesis requires FAPP2 transfer of gluco...	ACCEPT	Summary: ARF1 is an ADP-ribosylation factor family small G protein whose active GTP-bound state recruits trafficking effectors. Reason: Although broader than GTPase activity, small G protein activity is an appropriate molecular-function description for ARF1. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
GO:0046836 glycolipid transport	IDA PMID:17687330 Glycosphingolipid synthesis requires FAPP2 transfer of gluco...	KEEP AS NON CORE	Summary: ARF1 regulates FAPP2-dependent glucosylceramide transfer and glycosphingolipid synthesis/export. Reason: The process is experimentally supported, but it is a specialized lipid-trafficking context downstream of ARF1 effector recruitment rather than the broad conserved core role. Supporting Evidence: PMID:17687330 the whole glycosphingolipid synthetic pathway sensitive to regulation by phosphatidylinositol 4-phosphate and ARF1.
GO:1903292 protein localization to Golgi membrane	IDA PMID:17687330 Glycosphingolipid synthesis requires FAPP2 transfer of gluco...	ACCEPT	Summary: ARF1 promotes Golgi/TGN localization of PH-domain effectors such as FAPP proteins by cooperating with phosphatidylinositol 4-phosphate. Reason: Effector recruitment to Golgi/TGN membranes is a central consequence of ARF1 activation and is directly supported by the FAPP studies. Supporting Evidence: PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery. PMID:17687330 the whole glycosphingolipid synthetic pathway sensitive to regulation by phosphatidylinositol 4-phosphate and ARF1.
GO:0005765 lysosomal membrane	IDA PMID:41293316 Loss of ARF5 impairs recovery after lysosomal damage.	KEEP AS NON CORE	Summary: ARF1 can relocalize to damaged lysosomal membranes in LLOME-treated cells. Reason: The localization is experimentally observed, but the same study identifies ARF5, not ARF1, as the isoform required for lysosomal recovery, so this should not be treated as a core ARF1 function. Supporting Evidence: PMID:41293316 we found that ARF1, ARF5, and ARF6 localize to lysosomal membranes following L-leucyl-L-leucine methyl ester (LLOME)-induced permeabilization.
GO:0160281 cytoplasmic side of trans-Golgi network membrane	IDA PMID:17687330 Glycosphingolipid synthesis requires FAPP2 transfer of gluco...	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	EXP PMID:17555535 Specificity, promiscuity and localization of ARF protein int...	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0003924 GTPase activity	EXP PMID:10022920 Identification of a new Pyk2 target protein with Arf-GAP act...	ACCEPT	Summary: This paper identifies a Golgi/plasma-membrane ARF-GAP with activity toward ARF1, supporting ARF1 as a regulated GTPase. Reason: GTPase activity is the core ARF1 molecular function; the paper supports regulation of ARF1 GTPase cycling by ARF-GAPs. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
GO:0003924 GTPase activity	EXP PMID:10102276 Structural and functional analysis of the ARF1-ARFGAP comple...	ACCEPT	Summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle. Reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
GO:0003924 GTPase activity	EXP PMID:15107860 FAPPs control Golgi-to-cell-surface membrane traffic by bind...	ACCEPT	Summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle. Reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
GO:0003924 GTPase activity	EXP PMID:8253837 Hydrolysis of bound GTP by ARF protein triggers uncoating of...	ACCEPT	Summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle. Reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
GO:0014069 postsynaptic density	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Synaptic and postsynaptic-density annotations reflect transferred neuronal ARF1/PICK1 biology rather than the core conserved Golgi trafficking function. Reason: These annotations are plausible as specialized neuronal contexts, but they are not the main ARF1 function and are supported here by similarity rather than direct human ARF1 experiments. Supporting Evidence: file:human/ARF1/ARF1-notes.md Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
GO:0003924 GTPase activity	TAS Reactome:R-HSA-8847883	ACCEPT	Summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle. Reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
GO:0005515 protein binding	IPI PMID:12668765 Structure of the GAT domain of human GGA1: a syntaxin amino-...	MARK AS OVER ANNOTATED	Summary: ARF-dependent GGA localization is supported, but generic protein binding is too vague. Reason: The GGA GAT-domain interaction is biologically real, but ARF1 should not be curated mainly as protein binding; its informative role is active small-GTPase recruitment of trafficking adaptors. Supporting Evidence: PMID:12668765 The ARF binding site is located in the N-terminal extension and is separate from the core three-helix bundle.
GO:0019904 protein domain specific binding	IMP PMID:12668765 Structure of the GAT domain of human GGA1: a syntaxin amino-...	KEEP AS NON CORE	Summary: ARF1 binding to the GGA1 GAT domain is a characterized adaptor-recruitment interaction, but it is not the core ARF1 molecular function. Reason: The IMP-supported GGA1-GAT interaction is real and relevant to ARF-dependent adaptor recruitment, but GTPase activity and trafficking-process annotations better capture ARF1 core function. Supporting Evidence: PMID:12668765 The ARF binding site is located in the N-terminal extension and is separate from the core three-helix bundle.
GO:0003924 GTPase activity	IDA PMID:12771146 The tyrosine kinase Pyk2 regulates Arf1 activity by phosphor...	ACCEPT	Summary: ASAP1 phosphorylation modulates GAP activity and hence ARF1 activity. Reason: This directly supports ARF1 as a regulated GTPase in signaling/trafficking pathways. Supporting Evidence: PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
GO:0098586 cellular response to virus	IMP PMID:28389568 Hepatitis C virus triggers Golgi fragmentation and autophagy...	KEEP AS NON CORE	Summary: The viral-response annotation reflects HCV-induced Golgi remodeling through IRGM/GBF1/ARF-GTPase circuitry. Reason: This is a real infection-specific context but not the conserved core function of ARF1. Supporting Evidence: PMID:28389568 which normally operates in Golgi membrane dynamics and vesicle coating in resting cells.
GO:0032991 protein-containing complex	IMP PMID:12668765 Structure of the GAT domain of human GGA1: a syntaxin amino-...	MARK AS OVER ANNOTATED	Summary: ARF1 forms transient regulatory complexes with effectors and regulators, but a generic protein-containing complex annotation is not informative. Reason: This term loses the biology of an active small GTPase recruiting coat/adaptor machinery. It should not be treated as a core complex-membership assertion. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein-containing complex annotations are treated as over-annotated because ARF1 forms transient regulatory complexes with coat, adaptor, GEF, and GAP machinery rather than acting as a stable structural complex subunit. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
GO:0005515 protein binding	IPI PMID:17956946 Dissecting the role of the ARF guanine nucleotide exchange f...	MARK AS OVER ANNOTATED	Summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function. Reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms. Supporting Evidence: file:human/ARF1/ARF1-notes.md Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
GO:0031252 cell leading edge	IDA PMID:22573891 GBF1 bears a novel phosphatidylinositol-phosphate binding mo...	KEEP AS NON CORE	Summary: Cell-leading-edge localization is plausible in chemotactic signaling contexts involving PI3K/GBF1/ARF1 activation. Reason: This is a specialized signaling/localization context, not the central Golgi/TGN ARF1 role. Supporting Evidence: PMID:22573891 is primarily responsible for Arf1 activation upon GPCR stimulation and is important for neutrophil chemotaxis and superoxide production.
GO:0005925 focal adhesion	HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome...	MARK AS OVER ANNOTATED	Summary: This high-throughput localization is compatible with broad trafficking biology but does not define ARF1 core function. Reason: High-throughput compartment detections should not outweigh the well-supported Golgi/TGN trafficking model for ARF1. Supporting Evidence: file:human/ARF1/ARF1-notes.md High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
GO:0070062 extracellular exosome	HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres...	MARK AS OVER ANNOTATED	Summary: This high-throughput localization is compatible with broad trafficking biology but does not define ARF1 core function. Reason: High-throughput compartment detections should not outweigh the well-supported Golgi/TGN trafficking model for ARF1. Supporting Evidence: file:human/ARF1/ARF1-notes.md High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
GO:0003723 RNA binding	HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ...	MARK AS OVER ANNOTATED	Summary: RNA binding is from a high-throughput mRNA-bound proteome study and is not a known ARF1 biochemical function. Reason: The canonical ARF1 function is guanine nucleotide binding/hydrolysis and membrane trafficking; RNA binding should not be promoted without targeted validation. Supporting Evidence: file:human/ARF1/ARF1-notes.md High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
GO:0002090 regulation of receptor internalization	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: regulation of receptor internalization reflects transferred neuronal PICK1/AMPAR-related ARF1 biology. Reason: These neuronal terms are plausible specialized contexts but are not the conserved core function of ARF1 and are supported by similarity transfer in this GOA set. Supporting Evidence: file:human/ARF1/ARF1-notes.md Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
GO:0034315 regulation of Arp2/3 complex-mediated actin nucleation	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: regulation of Arp2/3 complex-mediated actin nucleation reflects transferred neuronal PICK1/AMPAR-related ARF1 biology. Reason: These neuronal terms are plausible specialized contexts but are not the conserved core function of ARF1 and are supported by similarity transfer in this GOA set. Supporting Evidence: file:human/ARF1/ARF1-notes.md Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
GO:0060292 long-term synaptic depression	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: long-term synaptic depression reflects transferred neuronal PICK1/AMPAR-related ARF1 biology. Reason: These neuronal terms are plausible specialized contexts but are not the conserved core function of ARF1 and are supported by similarity transfer in this GOA set. Supporting Evidence: file:human/ARF1/ARF1-notes.md Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
GO:0097061 dendritic spine organization	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: dendritic spine organization reflects transferred neuronal PICK1/AMPAR-related ARF1 biology. Reason: These neuronal terms are plausible specialized contexts but are not the conserved core function of ARF1 and are supported by similarity transfer in this GOA set. Supporting Evidence: file:human/ARF1/ARF1-notes.md Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
GO:0070062 extracellular exosome	HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid...	MARK AS OVER ANNOTATED	Summary: This high-throughput localization is compatible with broad trafficking biology but does not define ARF1 core function. Reason: High-throughput compartment detections should not outweigh the well-supported Golgi/TGN trafficking model for ARF1. Supporting Evidence: file:human/ARF1/ARF1-notes.md High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
GO:0070062 extracellular exosome	HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote...	MARK AS OVER ANNOTATED	Summary: This high-throughput localization is compatible with broad trafficking biology but does not define ARF1 core function. Reason: High-throughput compartment detections should not outweigh the well-supported Golgi/TGN trafficking model for ARF1. Supporting Evidence: file:human/ARF1/ARF1-notes.md High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-1675883	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-1676152	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-2130619	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-350769	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-421831	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-421833	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-432706	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-432712	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-8847875	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-8847880	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-8847883	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-8870499	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-8951498	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0000139 Golgi membrane	TAS Reactome:R-HSA-9845055	ACCEPT	Summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking. Reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors. Supporting Evidence: PMID:17555535 ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis. PMID:15107860 FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
GO:0005829 cytosol	TAS Reactome:R-HSA-200879	ACCEPT	Summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles. Reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state. Supporting Evidence: file:human/ARF1/ARF1-notes.md Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
GO:0005829 cytosol	TAS Reactome:R-HSA-350769	ACCEPT	Summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles. Reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state. Supporting Evidence: file:human/ARF1/ARF1-notes.md Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
GO:0005829 cytosol	TAS Reactome:R-HSA-421831	ACCEPT	Summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles. Reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state. Supporting Evidence: file:human/ARF1/ARF1-notes.md Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
GO:0005829 cytosol	TAS Reactome:R-HSA-432706	ACCEPT	Summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles. Reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state. Supporting Evidence: file:human/ARF1/ARF1-notes.md Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
GO:0005829 cytosol	TAS Reactome:R-HSA-8950173	ACCEPT	Summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles. Reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state. Supporting Evidence: file:human/ARF1/ARF1-notes.md Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
GO:0005829 cytosol	TAS Reactome:R-HSA-8951498	ACCEPT	Summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles. Reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state. Supporting Evidence: file:human/ARF1/ARF1-notes.md Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
GO:0006878 intracellular copper ion homeostasis	IMP PMID:21034850 The ADP-ribosylation factor 1 (Arf1) is involved in regulati...	KEEP AS NON CORE	Summary: ARF1-dependent trafficking affects copper uptake and CTR1 distribution. Reason: This is experimentally supported but appears to be a cargo/trafficking consequence rather than ARF1's primary molecular role. Supporting Evidence: PMID:21034850 Arf1-dependent trafficking pathways are therefore required for optimal copper uptake efficiency.
GO:0005886 plasma membrane	TAS PMID:8529647 Evidence for ADP-ribosylation-factor-mediated activation of ...	KEEP AS NON CORE	Summary: Plasma membrane association/activity is reported in signaling and PLD contexts but is not the primary ARF1 compartment. Reason: ARF1 can participate in plasma-membrane-linked signaling or trafficking, but the dominant conserved role is Golgi/TGN membrane trafficking. Supporting Evidence: PMID:8529647 The results indicate that ARF proteins and their nucleotide-exchange factor are apparently involved in the signalling pathway leading from mAChR activation to PLD stimulation in human embryonic kidney cells.
GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum	TAS Reactome:R-HSA-6811434	NEW	Summary: PN projection and Reactome support adding the specific Golgi-to-ER retrograde transport process for ARF1. Reason: ARF1 is the regulatory small GTPase that promotes coat recruitment and controls COPI coat cycling. This supports a process-level retrograde transport annotation, while the projected COPI vesicle coat component term should not be added because ARF1 is not a coatomer subunit. Supporting Evidence: Reactome:R-HSA-6811434 Retrograde traffic from the cis-Golgi to the ERGIC or the ER is mediated in part by microtubule-directed COPI-coated vesicles PMID:8253837 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport. PMID:10102276 a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats. file:human/ARF1/ARF1-notes.md The projected `GO:0030126 COPI vesicle coat` should not be added for ARF1.

Core Functions

ARF1 functions as a guanine-nucleotide-regulated membrane-trafficking switch at Golgi and TGN membranes. In its GTP-bound state it recruits coat/adaptor and lipid-metabolism effectors, including machinery for COPI-dependent Golgi-to-ER and intra-Golgi trafficking; GTP hydrolysis stimulated by ARFGAPs and coatomer promotes coat disassembly and recycling of the trafficking machinery. ARF1 is therefore best represented as a regulatory small GTPase in vesicle-mediated intracellular transport, not as a structural COPI coat subunit.

Molecular Function:

GTPase activity

Directly Involved In:

intracellular protein transport retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum protein localization to Golgi membrane

Cellular Locations:

Golgi membrane cytoplasmic side of trans-Golgi network membrane cytosol

Supporting Evidence:

PMID:8253837
The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
PMID:10102276
a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
Reactome:R-HSA-6811434
Retrograde traffic from the cis-Golgi to the ERGIC or the ER is mediated in part by microtubule-directed COPI-coated vesicles
PMID:15107860
FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.

References

GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000003

Gene Ontology annotation based on Enzyme Commission mapping

GO_REF:0000024

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:10022920

Identification of a new Pyk2 target protein with Arf-GAP activity.

PMID:10102276

Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis.

PMID:10198630

Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain.

PMID:12668765

Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor.

PMID:12771146

The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1.

PMID:14654833

Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor.

PMID:15107860

FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P.

PMID:17555535

Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta.

PMID:17563369

Structure-based discovery of an inhibitor of Arf activation by Sec7 domains through targeting of protein-protein complexes.

PMID:17687330

Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide.

PMID:17956946

Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking.

PMID:19199708

Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).

PMID:19644450

The structural basis of Arf effector specificity: the crystal structure of ARF6 in a complex with JIP4.

PMID:20458337

MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis.

PMID:21034850

The ADP-ribosylation factor 1 (Arf1) is involved in regulating copper uptake.

PMID:21423176

Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation.

PMID:22573891

GBF1 bears a novel phosphatidylinositol-phosphate binding module, BP3K, to link PI3Kγ activity with Arf1 activation involved in GPCR-mediated neutrophil chemotaxis and superoxide production.

PMID:22681889

The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.

PMID:22981988

The BAR domain protein Arfaptin-1 controls secretory granule biogenesis at the trans-Golgi network.

PMID:23533145

In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.

PMID:28389568

Hepatitis C virus triggers Golgi fragmentation and autophagy through the immunity-related GTPase M.

PMID:31467278

Maximizing binary interactome mapping with a minimal number of assays.

PMID:35271311

OpenCell: Endogenous tagging for the cartography of human cellular organization.

PMID:36396045

Targeting ARF1-IQGAP1 interaction to suppress colorectal cancer metastasis and vemurafenib resistance.

PMID:41293316

Loss of ARF5 impairs recovery after lysosomal damage.

PMID:8253837

Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles.

PMID:8529647

Evidence for ADP-ribosylation-factor-mediated activation of phospholipase D by m3 muscarinic acetylcholine receptor.

PMID:37914730

ARF1 prevents aberrant type I interferon induction by regulating STING activation and recycling.

ARF1 is a negative regulator of cGAS-STING type I interferon signaling; GTPase-defective heterozygous ARF1 missense mutations (e.g. R99C/R99H) cause a type I interferonopathy, with mutant ARF1 perturbing mitochondrial integrity (driving mtDNA release and cGAS activation) and causing accumulation of active STING at the Golgi/ERGIC due to defective retrograde transport.

PMID:37400497

Arf1 coordinates fatty acid metabolism and mitochondrial homeostasis.

Arf1 integrates cellular metabolism with energy production by regulating fatty-acid storage and utilization; a hyperactive Arf1 mutant causes fatty-acid accumulation in lipid droplets, mitochondrial fragmentation, and decreased ATP synthesis, with the role in fatty-acid metabolism conserved in mammals and proposed to act via organelle contact sites.

PMID:36269825

Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat.

Myristoylated GTP-bound Arf1 recruits AP-1 and stabilizes it in an active conformation, and AP-1:Arf1 self-assembles into a clathrin-independent tubular membrane coat via Arf1 dimer interfaces; HIV-1 Nef hijacks this AP-1:Arf1 coat to sequester MHC-I, and coat-contact residues are conserved across Arf isoforms and AP-1/AP-3/AP-4.

Reactome:R-HSA-1675883

PI is phosphorylated to PI4P by PI4KB at the Golgi membrane

Reactome:R-HSA-1676152

PI4KB binds to ARF1/3:GTP at the Golgi membrane

Reactome:R-HSA-200879

Formation of a Nef:ARF1:CD4 complex

Reactome:R-HSA-2130619

TGN-lysosomal vesicle coat assembly

Reactome:R-HSA-350769

trans-Golgi Network Coat Activation

Reactome:R-HSA-421831

trans-Golgi Network Coat Assembly

Reactome:R-HSA-421833

Vamp And trans-Golgi Network AP-1 Binding Coupled With Cargo Capture

Reactome:R-HSA-432706

trans-Golgi Network Lysosome Vesicle Destined Membrane Coat Assembly

Reactome:R-HSA-432712

Vamp And trans-Golgi Network AP-1 Binding Coupled With Cargo Capture On Lysosome Vesicle Destined Golgi Membrane

Reactome:R-HSA-8847875

ARF1:GTP binds Golgin TRIP11

Reactome:R-HSA-8847880

CYTH proteins bind ARF1:GTP

Reactome:R-HSA-8847883

CYTH proteins stimulate ARF1 GTPase activity

Reactome:R-HSA-8870499

PLEKHA3,8 bind PI4P, ARF1

Reactome:R-HSA-8950173

Expression of ADP-ribosylation factor 1

Reactome:R-HSA-8951498

Dissociation of Arf1:GDP, AP-1 Clathrin coated nonameric complex

Reactome:R-HSA-9845055

PLEKHA8 catalyzes transport of GlcCer to plasma membrane

file:human/ARF1/ARF1-notes.md

ARF1 PN review notes

ARF1 is a regulatory ARF-family GTPase for Golgi/TGN trafficking; PN retrograde transport propagation is supported, but COPI vesicle coat component propagation is rejected.

Reactome:R-HSA-6811434

COPI-dependent Golgi-to-ER retrograde traffic

Reactome pathway supporting ARF1 participation in COPI-dependent Golgi-to-ER retrograde traffic.

Reactome:R-HSA-6807878

COPI-mediated anterograde transport

Reactome:R-HSA-6811438

Intra-Golgi traffic

Reactome:R-HSA-432720

Lysosome Vesicle Biogenesis

Reactome:R-HSA-432722

Golgi Associated Vesicle Biogenesis

Reactome:R-HSA-9845576

Glycosphingolipid transport

Suggested Experiments

Experiment: Use acute endogenous ARF1 depletion or rapid ARF1 inactivation together with rescue by GTPase-cycle mutants, then quantify KDEL receptor/chaperone retrieval from Golgi to ER and COPI coat recruitment/uncoating kinetics.

Hypothesis: ARF1 GTPase cycling is required for efficient Golgi-to-ER retrieval of escaped ER proteins, supporting the retrograde-transport annotation without implying ARF1 is a structural COPI coat component.

Type: cell biology

Experiment: Perform proximity labeling of endogenous ARF1 during synchronized COPI budding/uncoating and compare enrichment of coatomer subunits, ARFGAPs, KDEL receptors, and cargo proteins across GTP-locked and GDP-locked ARF1 states.

Hypothesis: ARF1 associates transiently with COPI coat-cycle machinery as a regulatory GTPase rather than as a stable COPI coat constituent.

Type: proteomics

Experiment: Express disease-associated GTPase-defective ARF1 variants (e.g. R99C/R99H) in ARF1-edited cells and quantify STING retrograde Golgi-to-ER recycling, mitochondrial morphology and mtDNA release, and interferon-stimulated gene induction relative to wild-type ARF1 rescue.

Hypothesis: Loss of ARF1 GTPase cycling impairs STING retrograde transport and mitochondrial integrity, causing cGAS-STING-dependent type I interferon hyperactivation, distinct from ARF1's bulk Golgi/TGN coat-recruitment role.

Type: cell biology

Deep Research

Falcon

(ARF1-deep-research-falcon.md)

this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 32 citations 1 artifacts 2026-06-07T04:49:06.334748

## Context ID: pqac-00000015 The requested information about the Arf1/AP-1 tubular membrane coat and the UniProt ID P84077 can be found in the following figures (image/png)

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Research report: Human ARF1 (UniProt P84077) — functional annotation

0) Target verification (gene/protein identity)

Human ARF1 encodes ADP-ribosylation factor 1, a Class I ARF-family small GTPase that is N‑myristoylated and undergoes GDP↔GTP cycling to control membrane association and effector recruitment central to membrane trafficking. (li2023thearffamily pages 1-3, jackson2023anevolutionaryperspective pages 1-5, dejgaard2025arfsonthe pages 1-2)

The specific UniProt accession P84077 is explicitly referenced as the human Arf1 sequence used for structural modeling (AlphaFold2 model) in a high-quality primary structural study. (hooy2022selfassemblyandstructure media 42a5c13d)

1) Key concepts and definitions (current understanding)

1.1 ARF1 as a membrane-coupled GTPase cycle (enzymology)

ARF1 is a GTPase (EC 3.6.5.2) that catalyzes GTP hydrolysis in its active state; like many small GTPases, its intrinsic hydrolysis is low and is accelerated by ARF GTPase-activating proteins (ARF GAPs), while activation requires guanine nucleotide exchange factors (ARF GEFs) that promote GDP release and GTP loading. (dejgaard2025arfsonthe pages 1-2, nikolatou2023thearfgtpase pages 1-3)

A defining ARF-family feature is an N-terminal amphipathic helix with N‑myristoylation that is sequestered in a hydrophobic pocket in the GDP state and becomes exposed upon GTP binding, allowing stable membrane insertion/association; ARF1 is therefore comparatively soluble in the GDP state and membrane-bound in the GTP state. (li2023thearffamily pages 1-3, jackson2023anevolutionaryperspective pages 1-5)

Functionally, ARF•GTP–dependent coat recruitment is not simply “switch on/off”; productive trafficking requires GTP hydrolysis, and blocking hydrolysis causes trafficking defects (highlighting the importance of cycling). (turn2025arfthemost pages 6-7)

1.2 Domain architecture and family context

ARF-family proteins (including ARF1) share a conserved small GTPase fold with switch regions (effector/regulator interfaces) and an N-terminal membrane-binding module (myristoylated helix). (nikolatou2023thearfgtpase pages 1-3, hirschenberger2023arf1preventsaberranta pages 1-2)

2) ARF1 primary cellular functions (what ARF1 does)

2.1 Core role: vesicle biogenesis and coat/adaptor recruitment

ARF1’s canonical role is to initiate vesicle formation by recruiting coats and adaptors to membranes when in its GTP-bound, membrane-associated state. (li2023thearffamily pages 1-3, dejgaard2025arfsonthe pages 1-2)

COPI / early secretory pathway. A widely supported model is that ARF1-GTP at the Golgi recruits COPI to drive retrograde trafficking (Golgi→ER) and related early secretory steps. (li2023thearffamily pages 3-5, torii2024myelinationbysignaling pages 2-2)

AP-1 / TGN–endosome sorting (and clathrin-independent coats). ARF1-GTP recruits and activates AP complexes, notably AP‑1 at TGN/endosomal membranes. A structural reconstitution study shows myristoylated, GTP-bound Arf1 recruits AP‑1 to membranes and stabilizes AP‑1 in an active conformation, and that AP‑1:Arf1 can form a tubular coat without clathrin (a mechanistic basis for a class of tubulovesicular coats). (hooy2022selfassemblyandstructure pages 1-2)

A recent review emphasizing ArfGEF compartmentalization states that BIG1-mediated ARF1 activation drives clathrin/AP‑1–positive vesicle budding from the trans-Golgi toward endosomes and/or plasma membrane, while GBF-family GEFs activate ARF1 at the cis-Golgi to regulate COPI-positive budding. (torii2024myelinationbysignaling pages 3-3)

2.2 Lipid microdomain control and membrane identity (substrate specificity in context)

ARF1 modulates membrane identity partly by controlling lipid enzymes. In a 2023 review, human ARF1 is described as directly activating PI4KB, stimulating PI4P production, and more broadly ARF-family proteins regulate lipid-metabolic enzymes and phosphoinositide landscapes that support coat recruitment and membrane curvature. (li2023thearffamily pages 5-6, li2023thearffamily pages 3-5)

2.3 Beyond trafficking: nutrient signaling and organelle homeostasis

A 2023 review summarizes evidence that ARF1 contributes to amino-acid–dependent mTORC1 signaling, affecting lysosomal localization/activation of mTORC1; in that framework Brefeldin A (an ARF GEF inhibitor) disrupts amino-acid–induced lysosomal localization of mTORC1, and ArfGAP1 binds mTORC1 to inhibit its lysosomal localization/activation. (li2023thearffamily pages 5-6)

3) Subcellular localization (where ARF1 acts)

3.1 Golgi/ERGIC axis

Recent synthesis highlights that ARF1 is found at ER–Golgi interface compartments (cis-Golgi/ERGIC) and also on TGN and TGN-derived tubules, with localization/function linked to specific ARFGEFs. (torii2024myelinationbysignaling pages 2-2)

GBF1 is described as a preferential ARF1 GEF localized to ER exit sites and regulating the COPI complex involved in ER–Golgi and Golgi-to-ER transport. (torii2024myelinationbysignaling pages 2-2)

3.2 TGN/endosomes and trafficking intermediates

ARF1 localizes to and functions at the TGN/endosomal interface where it recruits AP complexes (AP‑1 emphasized). (hooy2022selfassemblyandstructure pages 1-2, torii2024myelinationbysignaling pages 3-3)

A cancer/metastasis-focused review further notes ARF1 functions beyond the Golgi in early endocytic compartments, recycling endosomes (including retrograde transport back to the TGN), and ER–TGN steps. (nikolatou2023thearfgtpase pages 1-3)

The same 2023 review reports ARF1 at mitochondria–ER contact sites and links ARF1 to broader organelle dynamics. (nikolatou2023thearfgtpase pages 1-3)

4) Recent developments (prioritizing 2023–2024)

4.1 ARF1 in innate immunity: controlling cGAS–STING signaling (2023)

A 2023 Nature Communications study identifies ARF1 as a negative regulator of cGAS–STING type I interferon signaling and reports that heterozygous, GTPase-defective ARF1 missense mutations (e.g., R99C/R99H) cause a type I interferonopathy with elevated interferon-stimulated gene expression. Mechanistically, mutant ARF1 perturbs mitochondrial morphology (promoting mitochondrial DNA release and cGAS activation) and causes accumulation of active STING at Golgi/ERGIC due to defective retrograde transport, indicating a dual role for ARF1 in mitochondrial integrity and STING recycling. (hirschenberger2023arf1preventsaberranta pages 1-2)

4.2 Metabolism/mitochondria: ARF1 integrates fatty-acid metabolism with mitochondrial homeostasis (2023)

A 2023 Nature Cell Biology study links Arf1 activity to fatty-acid storage/utilization and mitochondrial morphology/ATP synthesis. In yeast, a hyperactive Arf1 mutant caused fatty-acid accumulation in lipid droplets, mitochondrial fragmentation, and decreased ATP synthesis, and the authors report that Arf1’s role in fatty-acid metabolism is conserved in mammals, implicating Arf1 in metabolic–organelle coupling (potentially via contact sites). (enkler2023arf1coordinatesfatty pages 1-2)

4.3 Compartment-specific ARF1 activation via GEFs in physiology (2024)

A 2024 Journal of Neurochemistry review emphasizes ArfGEF-defined spatial control: GBF activates Arf1 at cis-Golgi for COPI-positive budding, whereas BIG1 activates Arf1 at trans-Golgi/TGN for clathrin/AP‑1–positive budding toward endosomes/plasma membrane, and notes distinct Arf distributions resolved by advanced imaging. (torii2024myelinationbysignaling pages 3-3, torii2024myelinationbysignaling pages 2-2)

5) Applications and real-world implementations

5.1 Pathogen exploitation of ARF1-dependent trafficking

HIV-1 immune evasion: A structural/mechanistic study shows HIV-1 Nef hijacks AP‑1 with Arf1 to sequester MHC-I, with AP‑1:Arf1:Nef:MHC-I forming a continuous tubular coat on membranes without clathrin—providing a concrete mechanism for immune evasion rooted in ARF1-dependent sorting machinery. (hooy2022selfassemblyandstructure pages 1-2)

5.2 Chemical biology and therapeutic exploration targeting the ARF pathway

NAV-2729 as an ARF-pathway probe (2023): A 2023 Journal of Biological Chemistry study concludes NAV‑2729 has a complex target profile, inhibiting multiple ARF GEFs and ARF GAPs (often via PH-domain interactions) rather than binding ARFs directly in their assays. Reported quantitative data include: NAV‑2729 cytotoxicity EC50 ~8–11 μM, inhibition of specific regulators (e.g., Brag2Sec7-PH IC50 ~7.1 μM, AGAP1 ~2.7 μM, ASAP1PZA ~4.6 μM, ASAP3PZA ~9.1 μM, among others), and a thermal shift proteomics result of 45 proteins with significant shifts (20 increased stability, 25 decreased). (rosenberg2023thesmallmolecule pages 3-4, rosenberg2023thesmallmolecule pages 13-14)

Brefeldin A (BFA) and GBF1/BIG inhibition: The same 2023 JBC paper notes BFA inhibits ARF1 GEFs GBF1 and BIG1/2, and reports BFA was broadly toxic with an approximately 10-fold higher potency in human vs mouse cells in their referenced comparisons. (rosenberg2023thesmallmolecule pages 1-3)

Computational/repurposing pipeline suggesting ARF1 as a drug target (2023): A 2023 Nature Communications paper proposes ARF1 as a target of the proton pump inhibitor rabeprazole, supported by multiple orthogonal assays (thermal shift, nucleotide exchange assays with ARNO, and cellular ARF1 activity assays), and reports ARF1 knockdown abolishes several rabeprazole-linked phenotypes (lipid droplet accumulation, tumor growth suppression, immune effects), consistent with ARF1-dependent pharmacology in that model. (chen2023sequencebaseddrugdesign pages 8-9)

6) Disease associations and expert consensus views

A contemporary perspective argues ARFs are often oversimplified as binary “molecular switches,” and emphasizes that cycling itself (including GAP-stimulated hydrolysis) is integral to ARF function, particularly in membrane traffic. (turn2025arfthemost pages 6-7)

Database-level disease/trait associations from Open Targets link ARF1 to multiple disease areas (e.g., HIV infection and neurodegenerative disease categories, and periventricular nodular heterotopia phenotypes), providing a structured map of reported associations and supporting literature pointers. (OpenTargets Search: -ARF1)

7) Evidence figure (structural/functional context)

A representative figure set from the AP‑1:Arf1 tubular coat study provides visual support for ARF1’s role in coat assembly at membranes and confirms use of the human Arf1 (UniProt P84077) structural model in analysis. (hooy2022selfassemblyandstructure media 42a5c13d)

8) Summary: functional annotation of ARF1 (P84077)

ARF1 (P84077) is a myristoylated ARF-family small GTPase that couples a GTPase cycle to membrane recruitment and effector assembly. Its primary, best-supported function is to orchestrate vesicle biogenesis and sorting through recruitment of COPI (cis-Golgi/ERGIC; GBF1-defined) and AP complexes such as AP‑1 (TGN/endosomes; BIG1-defined), while shaping lipid environments via enzymes such as PI4KB. Recent work expands ARF1 biology into innate immune control (cGAS–STING) and metabolic/mitochondrial homeostasis, and chemical-biology studies highlight both the tractability and the complexity of pharmacologically perturbing the ARF system. (li2023thearffamily pages 3-5, torii2024myelinationbysignaling pages 3-3, hooy2022selfassemblyandstructure pages 1-2, hirschenberger2023arf1preventsaberranta pages 1-2, enkler2023arf1coordinatesfatty pages 1-2)

9) Key cited sources (URLs; publication dates)

Hooy RM et al. Science Advances (2022-10). https://doi.org/10.1126/sciadv.add3914 (hooy2022selfassemblyandstructure pages 1-2)
Li F-L, Guan K-L. BioEssays (2023-03). https://doi.org/10.1002/bies.202200214 (li2023thearffamily pages 1-3)
Nikolatou K et al. Biochem Soc Trans (2023-08). https://doi.org/10.1042/bst20221355 (nikolatou2023thearfgtpase pages 1-3)
Hirschenberger M et al. Nature Communications (2023-11). https://doi.org/10.1038/s41467-023-42150-4 (hirschenberger2023arf1preventsaberranta pages 1-2)
Enkler L et al. Nature Cell Biology (2023-07). https://doi.org/10.1038/s41556-023-01180-2 (enkler2023arf1coordinatesfatty pages 1-2)
Rosenberg EM et al. J Biol Chem (2023-03). https://doi.org/10.1016/j.jbc.2023.102992 (rosenberg2023thesmallmolecule pages 3-4)
Torii T et al. Journal of Neurochemistry (2024-06). https://doi.org/10.1111/jnc.16141 (torii2024myelinationbysignaling pages 3-3)

References

(li2023thearffamily pages 1-3): Fu‐Long Li and Kun‐Liang Guan. The arf family gtpases: regulation of vesicle biogenesis and beyond. BioEssays, Mar 2023. URL: https://doi.org/10.1002/bies.202200214, doi:10.1002/bies.202200214. This article has 18 citations and is from a peer-reviewed journal.
(jackson2023anevolutionaryperspective pages 1-5): Catherine L. Jackson, Julie Ménétrey, Mandeep Sivia, Joel B. Dacks, and Marek Eliáš. An evolutionary perspective on arf family gtpases. Current Opinion in Cell Biology, 85:102268, Dec 2023. URL: https://doi.org/10.1016/j.ceb.2023.102268, doi:10.1016/j.ceb.2023.102268. This article has 14 citations and is from a peer-reviewed journal.
(dejgaard2025arfsonthe pages 1-2): Selma Yilmaz Dejgaard and John F. Presley. Arfs on the golgi: four conductors, one orchestra. Frontiers in Molecular Biosciences, Jul 2025. URL: https://doi.org/10.3389/fmolb.2025.1612531, doi:10.3389/fmolb.2025.1612531. This article has 6 citations.
(hooy2022selfassemblyandstructure media 42a5c13d): Richard M. Hooy, Yuichiro Iwamoto, Dan A. Tudorica, Xuefeng Ren, and James H. Hurley. Self-assembly and structure of a clathrin-independent ap-1:arf1 tubular membrane coat. Science Advances, Oct 2022. URL: https://doi.org/10.1126/sciadv.add3914, doi:10.1126/sciadv.add3914. This article has 29 citations and is from a highest quality peer-reviewed journal.
(nikolatou2023thearfgtpase pages 1-3): Konstantina Nikolatou, David M. Bryant, and Emma Sandilands. The arf gtpase regulatory network in collective invasion and metastasis. Biochemical Society Transactions, 51:1559-1569, Aug 2023. URL: https://doi.org/10.1042/bst20221355, doi:10.1042/bst20221355. This article has 3 citations and is from a peer-reviewed journal.
(turn2025arfthemost pages 6-7): Rachel E. Turn, Joel Bryan Dacks, Eric M. Rosenberg, Olivier Soubias, John K. Northup, and Paul A. Randazzo. Arf: the most misunderstood gtpase i ever knew - why study arf gaps. Frontiers in Molecular Biosciences, Oct 2025. URL: https://doi.org/10.3389/fmolb.2025.1668286, doi:10.3389/fmolb.2025.1668286. This article has 0 citations.
(hirschenberger2023arf1preventsaberranta pages 1-2): Maximilian Hirschenberger, Alice Lepelley, Ulrich Rupp, Susanne Klute, Victoria Hunszinger, Lennart Koepke, Veronika Merold, Blaise Didry-Barca, Fanny Wondany, Tim Bergner, Tatiana Moreau, Mathieu P. Rodero, Reinhild Rösler, Sebastian Wiese, Stefano Volpi, Marco Gattorno, Riccardo Papa, Sally-Ann Lynch, Marte G. Haug, Gunnar Houge, Kristen M. Wigby, Jessica Sprague, Jerica Lenberg, Clarissa Read, Paul Walther, Jens Michaelis, Frank Kirchhoff, Carina C. de Oliveira Mann, Yanick J. Crow, and Konstantin M. J. Sparrer. Arf1 prevents aberrant type i interferon induction by regulating sting activation and recycling. Nature Communications, Nov 2023. URL: https://doi.org/10.1038/s41467-023-42150-4, doi:10.1038/s41467-023-42150-4. This article has 54 citations and is from a highest quality peer-reviewed journal.
(li2023thearffamily pages 3-5): Fu‐Long Li and Kun‐Liang Guan. The arf family gtpases: regulation of vesicle biogenesis and beyond. BioEssays, Mar 2023. URL: https://doi.org/10.1002/bies.202200214, doi:10.1002/bies.202200214. This article has 18 citations and is from a peer-reviewed journal.
(torii2024myelinationbysignaling pages 2-2): Tomohiro Torii, Yuki Miyamoto, and Junji Yamauchi. Myelination by signaling through arf guanine nucleotide exchange factor. Journal of Neurochemistry, 168:2201-2213, Jun 2024. URL: https://doi.org/10.1111/jnc.16141, doi:10.1111/jnc.16141. This article has 8 citations and is from a domain leading peer-reviewed journal.
(hooy2022selfassemblyandstructure pages 1-2): Richard M. Hooy, Yuichiro Iwamoto, Dan A. Tudorica, Xuefeng Ren, and James H. Hurley. Self-assembly and structure of a clathrin-independent ap-1:arf1 tubular membrane coat. Science Advances, Oct 2022. URL: https://doi.org/10.1126/sciadv.add3914, doi:10.1126/sciadv.add3914. This article has 29 citations and is from a highest quality peer-reviewed journal.
(torii2024myelinationbysignaling pages 3-3): Tomohiro Torii, Yuki Miyamoto, and Junji Yamauchi. Myelination by signaling through arf guanine nucleotide exchange factor. Journal of Neurochemistry, 168:2201-2213, Jun 2024. URL: https://doi.org/10.1111/jnc.16141, doi:10.1111/jnc.16141. This article has 8 citations and is from a domain leading peer-reviewed journal.
(li2023thearffamily pages 5-6): Fu‐Long Li and Kun‐Liang Guan. The arf family gtpases: regulation of vesicle biogenesis and beyond. BioEssays, Mar 2023. URL: https://doi.org/10.1002/bies.202200214, doi:10.1002/bies.202200214. This article has 18 citations and is from a peer-reviewed journal.
(enkler2023arf1coordinatesfatty pages 1-2): Ludovic Enkler, Viktoria Szentgyörgyi, Mirjam Pennauer, Cristina Prescianotto-Baschong, Isabelle Riezman, Aneta Wiesyk, Reut Ester Avraham, Martin Spiess, Einat Zalckvar, Roza Kucharczyk, Howard Riezman, and Anne Spang. Arf1 coordinates fatty acid metabolism and mitochondrial homeostasis. Nature Cell Biology, 25:1157-1172, Jul 2023. URL: https://doi.org/10.1038/s41556-023-01180-2, doi:10.1038/s41556-023-01180-2. This article has 84 citations and is from a highest quality peer-reviewed journal.
(rosenberg2023thesmallmolecule pages 3-4): Eric M. Rosenberg, Xiaoying Jian, Olivier Soubias, Hye-Young Yoon, Mukesh P. Yadav, Sarah Hammoudeh, Sandeep Pallikkuth, Itoro Akpan, Pei-Wen Chen, Tapan K. Maity, Lisa M. Jenkins, Marielle E. Yohe, R. Andrew Byrd, and Paul A. Randazzo. The small molecule inhibitor nav-2729 has a complex target profile including multiple adp-ribosylation factor regulatory proteins. Mar 2023. URL: https://doi.org/10.1016/j.jbc.2023.102992, doi:10.1016/j.jbc.2023.102992. This article has 24 citations and is from a domain leading peer-reviewed journal.
(rosenberg2023thesmallmolecule pages 13-14): Eric M. Rosenberg, Xiaoying Jian, Olivier Soubias, Hye-Young Yoon, Mukesh P. Yadav, Sarah Hammoudeh, Sandeep Pallikkuth, Itoro Akpan, Pei-Wen Chen, Tapan K. Maity, Lisa M. Jenkins, Marielle E. Yohe, R. Andrew Byrd, and Paul A. Randazzo. The small molecule inhibitor nav-2729 has a complex target profile including multiple adp-ribosylation factor regulatory proteins. Mar 2023. URL: https://doi.org/10.1016/j.jbc.2023.102992, doi:10.1016/j.jbc.2023.102992. This article has 24 citations and is from a domain leading peer-reviewed journal.
(rosenberg2023thesmallmolecule pages 1-3): Eric M. Rosenberg, Xiaoying Jian, Olivier Soubias, Hye-Young Yoon, Mukesh P. Yadav, Sarah Hammoudeh, Sandeep Pallikkuth, Itoro Akpan, Pei-Wen Chen, Tapan K. Maity, Lisa M. Jenkins, Marielle E. Yohe, R. Andrew Byrd, and Paul A. Randazzo. The small molecule inhibitor nav-2729 has a complex target profile including multiple adp-ribosylation factor regulatory proteins. Mar 2023. URL: https://doi.org/10.1016/j.jbc.2023.102992, doi:10.1016/j.jbc.2023.102992. This article has 24 citations and is from a domain leading peer-reviewed journal.
(chen2023sequencebaseddrugdesign pages 8-9): Lifan Chen, Zi-sheng Fan, Jie Chang, Rui-rui Yang, Hui Hou, Hao Guo, Ying-hui Zhang, Tianbiao Yang, Chenmao Zhou, Qibang Sui, Zhengyang Chen, Chenni Zheng, Xinyue Hao, Keke Zhang, Rongrong Cui, Zehong Zhang, Hudson Ma, Yiluan Ding, Naixia Zhang, Xiaojie Lu, Xiaomin Luo, Hualiang Jiang, Sulin Zhang, and M. Zheng. Sequence-based drug design as a concept in computational drug design. Nature Communications, Jul 2023. URL: https://doi.org/10.1038/s41467-023-39856-w, doi:10.1038/s41467-023-39856-w. This article has 143 citations and is from a highest quality peer-reviewed journal.
(OpenTargets Search: -ARF1): Open Targets Query (-ARF1, 11 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.

Artifacts

## Context ID: pqac-00000015 The requested information about the Arf1/AP-1 tubular membrane coat and the UniProt ID P84077 can be found in the following figures

Citations

turn2025arfthemost pages 6-7
hooy2022selfassemblyandstructure pages 1-2
torii2024myelinationbysignaling pages 3-3
li2023thearffamily pages 5-6
torii2024myelinationbysignaling pages 2-2
nikolatou2023thearfgtpase pages 1-3
rosenberg2023thesmallmolecule pages 1-3
chen2023sequencebaseddrugdesign pages 8-9
li2023thearffamily pages 1-3
rosenberg2023thesmallmolecule pages 3-4
jackson2023anevolutionaryperspective pages 1-5
dejgaard2025arfsonthe pages 1-2
li2023thearffamily pages 3-5
rosenberg2023thesmallmolecule pages 13-14
https://doi.org/10.1126/sciadv.add3914
https://doi.org/10.1002/bies.202200214
https://doi.org/10.1042/bst20221355
https://doi.org/10.1038/s41467-023-42150-4
https://doi.org/10.1038/s41556-023-01180-2
https://doi.org/10.1016/j.jbc.2023.102992
https://doi.org/10.1111/jnc.16141
https://doi.org/10.1002/bies.202200214,
https://doi.org/10.1016/j.ceb.2023.102268,
https://doi.org/10.3389/fmolb.2025.1612531,
https://doi.org/10.1126/sciadv.add3914,
https://doi.org/10.1042/bst20221355,
https://doi.org/10.3389/fmolb.2025.1668286,
https://doi.org/10.1038/s41467-023-42150-4,
https://doi.org/10.1111/jnc.16141,
https://doi.org/10.1038/s41556-023-01180-2,
https://doi.org/10.1016/j.jbc.2023.102992,
https://doi.org/10.1038/s41467-023-39856-w,

📚 Additional Documentation

Notes

(ARF1-notes.md)

2026-06-03 - Proteostasis PN review

ARF1 is a class I ADP-ribosylation factor small GTPase whose core cellular role is regulated membrane recruitment of trafficking machinery at the Golgi/TGN. The core experimental model is a GTP/GDP cycle in which ARF-GTP triggers coat assembly and ARF GTP hydrolysis triggers coat disassembly [PMID:8253837 Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles, "Coat assembly is triggered when ARF binds GTP"].
ARF1 is mechanistically tied to COPI dynamics but is not itself a coatomer subunit. The ARF1-ARFGAP-coatomer work supports ARF1 as the regulatory GTPase that controls COPI coat disassembly, not as a structural component of the COPI vesicle coat [PMID:10102276 Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis, "a tripartite complex controls the GTP hydrolysis reaction triggering disassembly"].
The PN projection places ARF1 under ER proteostasis > Protein transport > ER-Golgi trafficking > Retrograde transport > COPI coating and uncoating. The projected GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum is biologically reasonable for ARF1 because Reactome lists ARF1 in COPI-dependent Golgi-to-ER retrograde traffic and the cached pathway summary states that retrograde traffic from cis-Golgi to ERGIC/ER is mediated by COPI-coated vesicles [Reactome:R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic, "Retrograde traffic from the cis-Golgi to the ERGIC or the ER"].
The projected GO:0030126 COPI vesicle coat should not be added for ARF1. This component term is suitable for coatomer subunits such as COPG1, but ARF1 is a membrane-associated regulatory GTPase that recruits and releases coat machinery. Adding the component term would imply ARF1 is part of the COPI vesicle coat rather than a regulator of COPI coating/uncoating.
The broader PN-projected GO:0015031 protein transport is already entailed by ARF1 GOA through GO:0006886 intracellular protein transport, so it does not need a new annotation.
ARF1 has additional validated but non-core contexts: FAPP2-dependent glycosphingolipid synthesis/export [PMID:17687330 Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide, "sensitive to regulation by phosphatidylinositol 4-phosphate and ARF1"], PI4KB/NCS-1 interactions at the Golgi [PMID:17555535 Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta, "ARF1 but not ARF5 or 6 enhanced"], copper uptake through trafficking of CTR1 [PMID:21034850 The ADP-ribosylation factor 1 (Arf1) is involved in regulating copper uptake, "required for optimal copper uptake efficiency"], and recruitment to damaged lysosomal membranes without clear ARF1-specific repair requirement [PMID:41293316 Loss of ARF5 impairs recovery after lysosomal damage, "ARF1, ARF5, and ARF6 localize to lysosomal membranes"].
Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
The magnesium ion binding annotation is retained as a cofactor-level biochemical property of the nucleotide/GTPase mechanism, not as an independent biological role.
Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.
Generic protein-containing complex annotations are treated as over-annotated because ARF1 forms transient regulatory complexes with coat, adaptor, GEF, and GAP machinery rather than acting as a stable structural complex subunit.
High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
Sarcomere localization and mitotic cleavage furrow ingression are not supported as core ARF1 biology in this review; the curated evidence supports Golgi/TGN endomembrane trafficking instead.
Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
Falcon deep research was launched with just deep-research-falcon human ARF1 --fallback perplexity-lite. The Falcon provider timed out after 600 seconds, and the perplexity-lite fallback failed with a 401 quota error, so no provider deep-research file was available for this pass. This review is therefore supported by the local GOA seed, UniProt, cached publications, cached Reactome records, and PN projection/mapping files.

Falcon deep research findings (2026-06-07)

A Falcon (Edison Scientific) deep-research report (ARF1-deep-research-falcon.md, 32 citations) was generated on 2026-06-07 and reviewed against the existing COMPLETE review. Most content CONFIRMS existing annotations (GTPase cycle, COPI/cis-Golgi via GBF1, AP-1/TGN, PI4KB-PI4P, myristoyl switch, retrograde Golgi-to-ER, glycosphingolipid export). The following are the genuinely new or mechanistically refined items. PMIDs were resolved from DOIs via PubMed.

NEW (disease/process): ARF1 is a negative regulator of cGAS-STING type I interferon signaling; heterozygous GTPase-defective ARF1 missense mutations (e.g. R99C/R99H) cause a previously unrecognized type I interferonopathy. Mechanistically mutant ARF1 perturbs mitochondrial morphology (driving mtDNA release and cGAS activation) and causes accumulation of active STING at the Golgi/ERGIC owing to defective retrograde transport — a dual role in mitochondrial integrity and STING recycling [PMID:37914730 "we identify the GTPase ADP-ribosylation factor 1 (ARF1) as a crucial negative regulator of cGAS-STING signalling"; "Heterozygous ARF1 missense mutations cause a previously unrecognized type I interferonopathy"]. This connects the existing KEEP_AS_NON_CORE GO:0098586 cellular response to virus annotation to a defined STING-recycling/retrograde-transport mechanism, but I am NOT changing that action — STING regulation remains a specialized, non-core context rather than the conserved core trafficking role.
NEW (process/organelle coupling): Arf1 coordinates fatty-acid metabolism with mitochondrial homeostasis. A hyperactive Arf1 mutant decreased fatty-acid transporter/beta-oxidation enzyme expression, driving fatty-acid accumulation in lipid droplets, mitochondrial fragmentation, and reduced ATP synthesis; the role in fatty-acid metabolism is conserved in mammals and is proposed to act presumably via organelle contact sites PMID:37400497. PROVISIONAL for human annotation purposes (primary mechanism shown in yeast); recorded as expanded biology only, not used to add or change annotations.
NEW (structural/mechanistic): Cryo-EM structure of a clathrin-INDEPENDENT AP-1:Arf1 tubular membrane coat. Myristoylated GTP-bound Arf1 recruits AP-1 to membranes and stabilizes it in an active conformation, and AP-1:Arf1 self-assembles into a tubular coat via Arf1 dimer interfaces without clathrin. HIV-1 Nef hijacks this AP-1:Arf1 coat to sequester MHC-I (AP-1:Arf1:Nef:MHC-I tubular coat), giving a structural mechanism for immune evasion; coat-contact residues are conserved across Arf isoforms and across AP-1/AP-3/AP-4 PMID:36269825. This refines the existing AP-1/TGN and Reactome Nef:ARF1:CD4 annotations with a defined coat-assembly mechanism but does not warrant changing any existing action.
CONFIRMS (regulation/localization): GBF-family GEFs activate ARF1 at the cis-Golgi/ER exit sites for COPI-positive budding, whereas BIG1 activates ARF1 at the trans-Golgi/TGN for clathrin/AP-1-positive budding toward endosomes/plasma membrane (compartment-specific GEF control) [Torii 2024 J Neurochem, doi:10.1111/jnc.16141]. Consistent with the existing GBF1 (PMID:17956946) and TGN/AP-1 annotations; no change.
CONFIRMS / PROVISIONAL (chemical biology, not annotation-relevant): NAV-2729 has a complex off-target profile inhibiting multiple ArfGEFs/ArfGAPs rather than binding ARFs directly; Brefeldin A inhibits GBF1 and BIG1/2 GEFs; a computational pipeline proposes ARF1 as a target of rabeprazole [Rosenberg 2023 JBC doi:10.1016/j.jbc.2023.102992; Chen 2023 Nat Commun doi:10.1038/s41467-023-39856-w]. Pharmacology/repurposing context only; PROVISIONAL and not used to alter annotations.
Action on the review: added the three new primary references (PMID:37914730, PMID:37400497, PMID:36269825) to references: as statement-only findings (full_text_unavailable, no supporting_text since these full texts are not in the local publications cache), and added a STING/cGAS suggested question plus an interferonopathy-variant suggested experiment. No existing annotation action was changed; the STING and fatty-acid roles remain non-core/specialized contexts relative to the conserved Golgi/TGN trafficking function.

Pn Notes

(ARF1-pn-notes.md)

ARF1 PN Consistency Notes

Generated: 2026-06-18
Project: PROTEOSTASIS
Scope: PN consistency rereview against local AIGR review and available deep-research artifacts
UniProt: P84077
AIGR review status: COMPLETE
Review batch: proteostasis-batch-2026-06-03 (PR 1364)
Batch change status: added

Source Files Checked

AIGR review YAML: present - genes/human/ARF1/ARF1-ai-review.yaml
AIGR review HTML: present - genes/human/ARF1/ARF1-ai-review.html
Gene notes: present - genes/human/ARF1/ARF1-notes.md
GOA TSV: present - genes/human/ARF1/ARF1-goa.tsv
UniProt record: present - genes/human/ARF1/ARF1-uniprot.txt
PN dossier: projects/PROTEOSTASIS/reports/phase1_dossiers/ARF1.md
PN consistency section: projects/PROTEOSTASIS/reports/phase1_dossiers/_sections/ARF1.md
PN projection report: projects/PROTEOSTASIS/reports/pn_projection/pn_projected_gene_go_summary.tsv
PN mapping audit: projects/PROTEOSTASIS/reports/pn_mapping_audit/current_mapping_scrutiny.tsv

Deep Research Files

genes/human/ARF1/ARF1-deep-research-falcon.md

AIGR Review Snapshot

Description: ARF1 encodes ADP-ribosylation factor 1, a myristoylated class I ARF-family small GTPase that cycles between cytosolic GDP-bound and membrane-associated GTP-bound states. Active ARF1 acts mainly on Golgi and trans-Golgi network membranes, where it recruits and regulates coat/adaptor and lipid-transfer machinery for vesicle budding, coat disassembly, intra-Golgi traffic, Golgi-to-ER retrograde transport, TGN-to-endosomal/plasma-membrane routes, and glycosphingolipid export. Its major cellular role is regulation of membrane trafficking through the secretory and endomembrane systems rather than serving as a structural coat subunit.
Existing/core annotation action counts: ACCEPT: 40; KEEP_AS_NON_CORE: 15; MARK_AS_OVER_ANNOTATED: 18; NEW: 1; REMOVE: 1

PN Consistency Summary

Consistency: Fully consistent across DR, notes, review YAML, and PN. The notes explicitly walk all three projected terms. No contradiction.
PN story / NEW pressure: PN asserts retrograde Golgi-to-ER transport + COPI coat handling. Review ADDS GO:0006890 (verified real; action: NEW, TAS, Reactome:R-HSA-6811434) — defensible, matches PN type-node projection. GO:0015031 already captured (entailed via GO:0006886 IBA). GO:0030126 COPI vesicle coat: PN subtype over-reaches — ARF1 is a regulatory GTPase that recruits/releases coat, not a coatomer subunit; review correctly REJECTS adding it (mirrors the TOMM20/RAB7A "wrong-bucket" precedent — a CC membership term projected onto a regulator).
Evidence alignment: PN row carried no PMIDs; review/notes anchor on PMID:8253837 (ARF GTP cycle), PMID:10102276 (ARF1-ARFGAP-coatomer), Reactome:R-HSA-6811434. Falcon DR added PMID:37914730 (cGAS-STING), 37400497 (FA/mito), 36269825 (AP-1:Arf1 coat) as statement-only, non-core. No divergence.
Verdict: Consistent; GO:0006890 NEW is warranted and matches PN. PN GO:0030126 over-reaches for ARF1 (regulator vs coat subunit) and review correctly declines.

Full Consistency Review

UniProt: P84077 · batch: proteostasis-batch-2026-06-03 (Falcon DR 2026-06-07) · review status: COMPLETE
PN placement: 1 row, ER. ER proteostasis|Protein transport|ER-Golgi trafficking|Retrograde transport|COPI coating and uncoating. PN-node mapping: subtype=mapped→GO:0030126 COPI vesicle coat (more_specific); type (Retrograde transport)=mapped→GO:0006890 retrograde Golgi-to-ER transport (more_specific); group (ER-Golgi trafficking)=no_mapping; class (Protein transport)=mapped→GO:0015031 (entailed_by_goa_closure); branch=no_mapping.
Consistency: Fully consistent across DR, notes, review YAML, and PN. The notes explicitly walk all three projected terms. No contradiction.
PN story / NEW pressure: PN asserts retrograde Golgi-to-ER transport + COPI coat handling. Review ADDS GO:0006890 (verified real; action: NEW, TAS, Reactome:R-HSA-6811434) — defensible, matches PN type-node projection. GO:0015031 already captured (entailed via GO:0006886 IBA). GO:0030126 COPI vesicle coat: PN subtype over-reaches — ARF1 is a regulatory GTPase that recruits/releases coat, not a coatomer subunit; review correctly REJECTS adding it (mirrors the TOMM20/RAB7A "wrong-bucket" precedent — a CC membership term projected onto a regulator).
Mapping strategy: ARF1 does not change the node mapping. The retrograde-transport (GO:0006890) and protein-transport (GO:0015031) projections are right. The COPI-coat subtype (GO:0030126) is sound for coatomer members but should not project to ARF1; review files this as a suggested question (distinguish structural coatomer from regulatory GTPases).
Evidence alignment: PN row carried no PMIDs; review/notes anchor on PMID:8253837 (ARF GTP cycle), PMID:10102276 (ARF1-ARFGAP-coatomer), Reactome:R-HSA-6811434. Falcon DR added PMID:37914730 (cGAS-STING), 37400497 (FA/mito), 36269825 (AP-1:Arf1 coat) as statement-only, non-core. No divergence.
Verdict: Consistent; GO:0006890 NEW is warranted and matches PN. PN GO:0030126 over-reaches for ARF1 (regulator vs coat subunit) and review correctly declines.
Recommended edits: none to ARF1-ai-review.yaml. [MAP] flag PN "COPI coating and uncoating" subtype to not project GO:0030126 (CC membership) to regulatory GTPases such as ARF1; restrict to coatomer subunits.

PN Dossier Context

review_batch: proteostasis-batch-2026-06-03
review_yaml: genes/human/ARF1/ARF1-ai-review.yaml
PN workbook rows: 1

PN row 1: ER proteostasis | Protein transport | ER-Golgi trafficking | Retrograde transport | COPI coating and uncoating

UniProt: P84077
In branches: ER
PN-node mapping records (path + ancestors):
- [subtype] ER proteostasis|Protein transport|ER-Golgi trafficking|Retrograde transport|COPI coating and uncoating
  status=mapped scope=ok_for_propagation_to_go GO=[GO:0030126 COPI vesicle coat]
  rationale: This PN subtype is a COPI coat handling bucket in retrograde ER-Golgi transport. COPI vesicle coat is the appropriate shared cellular-component target.
- [type] ER proteostasis|Protein transport|ER-Golgi trafficking|Retrograde transport
  status=mapped scope=ok_for_propagation_to_go GO=[GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum]
  rationale: In 4.3.11, the earlier retrograde-transport bucket has been folded into ER-Golgi trafficking and now specifically denotes COPI/KDEL-style retrograde trafficking from Golgi back to ER. The correct GO target is therefore retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum rather than ER-to-cytosol retrotranslocation.
- [group] ER proteostasis|Protein transport|ER-Golgi trafficking
  status=no_mapping scope= GO=[]
  rationale: Reviewed as a broad PN category rather than a single GO class. The member genes span multiple activities, complexes, or contexts, so direct propagation from this node would overstate the shared biology.
- [class] ER proteostasis|Protein transport
  status=mapped scope=ok_for_propagation_to_go GO=[GO:0015031 protein transport]
  rationale: The PN ER Protein transport class groups ER-targeting and ER-insertion pathways. GO protein transport is the appropriate propagation target, while the source class remains ER-specific and broader than any single GO transport subtype.
- [branch] ER proteostasis
  status=no_mapping scope= GO=[]
  rationale: Reviewed as a top-level PN branch. This is a systems/taxonomy umbrella, not a direct GO assertion; narrower child curations carry any propagating GO mappings.

Projected GO annotations (3)

GO:0015031 protein transport | scope=ok_for_propagation_to_go | goa_status=entailed_by_goa_closure | from=ER proteostasis|Protein transport
GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum | scope=ok_for_propagation_to_go | goa_status=more_specific_than_existing_goa | from=ER proteostasis|Protein transport|ER-Golgi trafficking|Retrograde transport
GO:0030126 COPI vesicle coat | scope=ok_for_propagation_to_go | goa_status=more_specific_than_existing_goa | from=ER proteostasis|Protein transport|ER-Golgi trafficking|Retrograde transport|COPI coating and uncoating

Note

This file is generated from the current PROTEOSTASIS phase-1 dossier and local gene-review artifacts. Edit the source review, PN mapping, or dossier rather than this generated note when correcting the underlying curation.

📄 View Raw YAML

id: P84077
gene_symbol: ARF1
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: ARF1 encodes ADP-ribosylation factor 1, a myristoylated class I ARF-family small GTPase that cycles between cytosolic GDP-bound and membrane-associated GTP-bound states. Active ARF1 acts mainly on Golgi and trans-Golgi network membranes, where it recruits and regulates coat/adaptor and lipid-transfer machinery for vesicle budding, coat disassembly, intra-Golgi traffic, Golgi-to-ER retrograde transport, TGN-to-endosomal/plasma-membrane routes, and glycosphingolipid export. Its major cellular role is regulation of membrane trafficking through the secretory and endomembrane systems rather than serving as a structural coat subunit.
existing_annotations:
- term:
    id: GO:0006886
    label: intracellular protein transport
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Intracellular protein transport is a valid broad process for ARF1-dependent Golgi/TGN and COPI-related trafficking.
    action: ACCEPT
    reason: This IBA term captures the conserved trafficking role of ARF1. It is broader than the PN retrograde-transport candidate but biologically sound.
    supported_by:
    - reference_id: Reactome:R-HSA-6811434
      supporting_text: Retrograde traffic from the cis-Golgi to the ERGIC or the ER is mediated in part by microtubule-directed COPI-coated vesicles
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
- term:
    id: GO:0005525
    label: GTP binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: GTP binding is the nucleotide-binding state required for ARF1 activation and membrane-effector recruitment.
    action: ACCEPT
    reason: This is a core biochemical property of ARF1 and is directly tied to ARF1-dependent coat recruitment and vesicle budding.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: Plasma membrane association/activity is reported in signaling and PLD contexts but is not the primary ARF1 compartment.
    action: KEEP_AS_NON_CORE
    reason: ARF1 can participate in plasma-membrane-linked signaling or trafficking, but the dominant conserved role is Golgi/TGN membrane trafficking.
    supported_by:
    - reference_id: PMID:8529647
      supporting_text: The results indicate that ARF proteins and their nucleotide-exchange factor are apparently involved in the signalling pathway leading from mAChR activation to PLD stimulation in human embryonic kidney cells.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle.
    action: ACCEPT
    reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
- term:
    id: GO:0003925
    label: G protein activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000003
  qualifier: enables
  review:
    summary: ARF1 is an ADP-ribosylation factor family small G protein whose active GTP-bound state recruits trafficking effectors.
    action: ACCEPT
    reason: Although broader than GTPase activity, small G protein activity is an appropriate molecular-function description for ARF1.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
- term:
    id: GO:0005525
    label: GTP binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: GTP binding is the nucleotide-binding state required for ARF1 activation and membrane-effector recruitment.
    action: ACCEPT
    reason: This is a core biochemical property of ARF1 and is directly tied to ARF1-dependent coat recruitment and vesicle budding.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
- term:
    id: GO:0014069
    label: postsynaptic density
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Synaptic and postsynaptic-density annotations reflect transferred neuronal ARF1/PICK1 biology rather than the core conserved Golgi trafficking function.
    action: KEEP_AS_NON_CORE
    reason: These annotations are plausible as specialized neuronal contexts, but they are not the main ARF1 function and are supported here by similarity rather than direct human ARF1 experiments.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
- term:
    id: GO:0045202
    label: synapse
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Synaptic and postsynaptic-density annotations reflect transferred neuronal ARF1/PICK1 biology rather than the core conserved Golgi trafficking function.
    action: KEEP_AS_NON_CORE
    reason: These annotations are plausible as specialized neuronal contexts, but they are not the main ARF1 function and are supported here by similarity rather than direct human ARF1 experiments.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:10198630
  qualifier: enables
  review:
    summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: 'Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:14654833
  qualifier: enables
  review:
    summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: 'Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17563369
  qualifier: enables
  review:
    summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: 'Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19644450
  qualifier: enables
  review:
    summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: 'Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22981988
  qualifier: enables
  review:
    summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: 'Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:31467278
  qualifier: enables
  review:
    summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: 'Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:35271311
  qualifier: enables
  review:
    summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: 'Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:36396045
  qualifier: enables
  review:
    summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: 'Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.'
- term:
    id: GO:0000287
    label: magnesium ion binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: enables
  review:
    summary: Magnesium binding is consistent with ARF1 nucleotide binding and GTPase chemistry.
    action: ACCEPT
    reason: Small GTPases require Mg2+-coordinated nucleotide binding/hydrolysis; this is a supporting biochemical property rather than a standalone biological role.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: The magnesium ion binding annotation is retained as a cofactor-level biochemical property of the nucleotide/GTPase mechanism, not as an independent biological role.
- term:
    id: GO:0005794
    label: Golgi apparatus
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: located_in
  review:
    summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles.
    action: ACCEPT
    reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
- term:
    id: GO:0012505
    label: endomembrane system
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: located_in
  review:
    summary: Endomembrane localization is broad but consistent with ARF1 function at Golgi/TGN and related trafficking membranes.
    action: ACCEPT
    reason: ARF1 acts on Golgi, TGN, and related endomembrane trafficking intermediates; this term is less specific than Golgi membrane but accurate.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
    - reference_id: Reactome:R-HSA-6811434
      supporting_text: Retrograde traffic from the cis-Golgi to the ERGIC or the ER is mediated in part by microtubule-directed COPI-coated vesicles
- term:
    id: GO:0030017
    label: sarcomere
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: located_in
  review:
    summary: Sarcomere localization is not supported by the reviewed ARF1 functional literature and is not part of the ARF1 trafficking model.
    action: REMOVE
    reason: This automatic transfer appears disconnected from ARF1 core Golgi/TGN trafficking and should not be retained without stronger direct evidence.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Sarcomere localization and mitotic cleavage furrow ingression are not supported as core ARF1 biology in this review; the curated evidence supports Golgi/TGN endomembrane trafficking instead.
- term:
    id: GO:0032991
    label: protein-containing complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: part_of
  review:
    summary: ARF1 forms transient regulatory complexes with effectors and regulators, but a generic protein-containing complex annotation is not informative.
    action: MARK_AS_OVER_ANNOTATED
    reason: This term loses the biology of an active small GTPase recruiting coat/adaptor machinery. It should not be treated as a core complex-membership assertion.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Generic protein-containing complex annotations are treated as over-annotated because ARF1 forms transient regulatory complexes with coat, adaptor, GEF, and GAP machinery rather than acting as a stable structural complex subunit.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
- term:
    id: GO:1990386
    label: mitotic cleavage furrow ingression
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Mitotic cleavage furrow ingression is a possible specialized small-GTPase trafficking context but is not supported here by direct ARF1 evidence.
    action: MARK_AS_OVER_ANNOTATED
    reason: The annotation is too specific for the available electronically transferred evidence and should not be considered core ARF1 biology.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Sarcomere localization and mitotic cleavage furrow ingression are not supported as core ARF1 biology in this review; the curated evidence supports Golgi/TGN endomembrane trafficking instead.
- term:
    id: GO:0003925
    label: G protein activity
  evidence_type: IDA
  original_reference_id: PMID:17687330
  qualifier: enables
  review:
    summary: ARF1 is an ADP-ribosylation factor family small G protein whose active GTP-bound state recruits trafficking effectors.
    action: ACCEPT
    reason: Although broader than GTPase activity, small G protein activity is an appropriate molecular-function description for ARF1.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
- term:
    id: GO:0046836
    label: glycolipid transport
  evidence_type: IDA
  original_reference_id: PMID:17687330
  qualifier: involved_in
  review:
    summary: ARF1 regulates FAPP2-dependent glucosylceramide transfer and glycosphingolipid synthesis/export.
    action: KEEP_AS_NON_CORE
    reason: The process is experimentally supported, but it is a specialized lipid-trafficking context downstream of ARF1 effector recruitment rather than the broad conserved core role.
    supported_by:
    - reference_id: PMID:17687330
      supporting_text: the whole glycosphingolipid synthetic pathway sensitive to regulation by phosphatidylinositol 4-phosphate and ARF1.
- term:
    id: GO:1903292
    label: protein localization to Golgi membrane
  evidence_type: IDA
  original_reference_id: PMID:17687330
  qualifier: involved_in
  review:
    summary: ARF1 promotes Golgi/TGN localization of PH-domain effectors such as FAPP proteins by cooperating with phosphatidylinositol 4-phosphate.
    action: ACCEPT
    reason: Effector recruitment to Golgi/TGN membranes is a central consequence of ARF1 activation and is directly supported by the FAPP studies.
    supported_by:
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
    - reference_id: PMID:17687330
      supporting_text: the whole glycosphingolipid synthetic pathway sensitive to regulation by phosphatidylinositol 4-phosphate and ARF1.
- term:
    id: GO:0005765
    label: lysosomal membrane
  evidence_type: IDA
  original_reference_id: PMID:41293316
  qualifier: located_in
  review:
    summary: ARF1 can relocalize to damaged lysosomal membranes in LLOME-treated cells.
    action: KEEP_AS_NON_CORE
    reason: The localization is experimentally observed, but the same study identifies ARF5, not ARF1, as the isoform required for lysosomal recovery, so this should not be treated as a core ARF1 function.
    supported_by:
    - reference_id: PMID:41293316
      supporting_text: we found that ARF1, ARF5, and ARF6 localize to lysosomal membranes following L-leucyl-L-leucine methyl ester (LLOME)-induced permeabilization.
- term:
    id: GO:0160281
    label: cytoplasmic side of trans-Golgi network membrane
  evidence_type: IDA
  original_reference_id: PMID:17687330
  qualifier: is_active_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: EXP
  original_reference_id: PMID:17555535
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: EXP
  original_reference_id: PMID:10022920
  qualifier: enables
  review:
    summary: This paper identifies a Golgi/plasma-membrane ARF-GAP with activity toward ARF1, supporting ARF1 as a regulated GTPase.
    action: ACCEPT
    reason: GTPase activity is the core ARF1 molecular function; the paper supports regulation of ARF1 GTPase cycling by ARF-GAPs.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: EXP
  original_reference_id: PMID:10102276
  qualifier: enables
  review:
    summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle.
    action: ACCEPT
    reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: EXP
  original_reference_id: PMID:15107860
  qualifier: enables
  review:
    summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle.
    action: ACCEPT
    reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: EXP
  original_reference_id: PMID:8253837
  qualifier: enables
  review:
    summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle.
    action: ACCEPT
    reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
- term:
    id: GO:0014069
    label: postsynaptic density
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: located_in
  review:
    summary: Synaptic and postsynaptic-density annotations reflect transferred neuronal ARF1/PICK1 biology rather than the core conserved Golgi trafficking function.
    action: KEEP_AS_NON_CORE
    reason: These annotations are plausible as specialized neuronal contexts, but they are not the main ARF1 function and are supported here by similarity rather than direct human ARF1 experiments.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8847883
  qualifier: enables
  review:
    summary: ARF1 is a canonical small GTPase that binds guanine nucleotide and hydrolyzes GTP as part of its membrane-trafficking cycle.
    action: ACCEPT
    reason: The GTP/GDP cycle is the core molecular function of ARF1. GTP binding promotes membrane/effector engagement and GTP hydrolysis, stimulated by ARFGAPs and coatomer, drives coat disassembly.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:12668765
  qualifier: enables
  review:
    summary: ARF-dependent GGA localization is supported, but generic protein binding is too vague.
    action: MARK_AS_OVER_ANNOTATED
    reason: The GGA GAT-domain interaction is biologically real, but ARF1 should not be curated mainly as protein binding; its informative role is active small-GTPase recruitment of trafficking adaptors.
    supported_by:
    - reference_id: PMID:12668765
      supporting_text: The ARF binding site is located in the N-terminal extension and is separate from the core three-helix bundle.
- term:
    id: GO:0019904
    label: protein domain specific binding
  evidence_type: IMP
  original_reference_id: PMID:12668765
  qualifier: enables
  review:
    summary: ARF1 binding to the GGA1 GAT domain is a characterized adaptor-recruitment interaction, but it is not the core ARF1 molecular function.
    action: KEEP_AS_NON_CORE
    reason: The IMP-supported GGA1-GAT interaction is real and relevant to ARF-dependent adaptor recruitment, but GTPase activity and trafficking-process annotations better capture ARF1 core function.
    supported_by:
    - reference_id: PMID:12668765
      supporting_text: The ARF binding site is located in the N-terminal extension and is separate from the core three-helix bundle.
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: IDA
  original_reference_id: PMID:12771146
  qualifier: enables
  review:
    summary: ASAP1 phosphorylation modulates GAP activity and hence ARF1 activity.
    action: ACCEPT
    reason: This directly supports ARF1 as a regulated GTPase in signaling/trafficking pathways.
    supported_by:
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
- term:
    id: GO:0098586
    label: cellular response to virus
  evidence_type: IMP
  original_reference_id: PMID:28389568
  qualifier: involved_in
  review:
    summary: The viral-response annotation reflects HCV-induced Golgi remodeling through IRGM/GBF1/ARF-GTPase circuitry.
    action: KEEP_AS_NON_CORE
    reason: This is a real infection-specific context but not the conserved core function of ARF1.
    supported_by:
    - reference_id: PMID:28389568
      supporting_text: which normally operates in Golgi membrane dynamics and vesicle coating in resting cells.
- term:
    id: GO:0032991
    label: protein-containing complex
  evidence_type: IMP
  original_reference_id: PMID:12668765
  qualifier: part_of
  review:
    summary: ARF1 forms transient regulatory complexes with effectors and regulators, but a generic protein-containing complex annotation is not informative.
    action: MARK_AS_OVER_ANNOTATED
    reason: This term loses the biology of an active small GTPase recruiting coat/adaptor machinery. It should not be treated as a core complex-membership assertion.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Generic protein-containing complex annotations are treated as over-annotated because ARF1 forms transient regulatory complexes with coat, adaptor, GEF, and GAP machinery rather than acting as a stable structural complex subunit.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17956946
  qualifier: enables
  review:
    summary: The physical interaction is real or plausible, but generic protein binding does not describe ARF1 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Protein binding is non-informative for this gene. ARF1 should be represented by GTP binding/GTPase activity and by specific trafficking processes rather than generic interaction terms.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: 'Generic protein binding annotations are treated as over-annotated because ARF1 has many real effectors and regulators, but the term does not capture the informative activity: regulated small-GTPase recruitment of trafficking machinery.'
- term:
    id: GO:0031252
    label: cell leading edge
  evidence_type: IDA
  original_reference_id: PMID:22573891
  qualifier: located_in
  review:
    summary: Cell-leading-edge localization is plausible in chemotactic signaling contexts involving PI3K/GBF1/ARF1 activation.
    action: KEEP_AS_NON_CORE
    reason: This is a specialized signaling/localization context, not the central Golgi/TGN ARF1 role.
    supported_by:
    - reference_id: PMID:22573891
      supporting_text: is primarily responsible for Arf1 activation upon GPCR stimulation and is important for neutrophil chemotaxis and superoxide production.
- term:
    id: GO:0005925
    label: focal adhesion
  evidence_type: HDA
  original_reference_id: PMID:21423176
  qualifier: located_in
  review:
    summary: This high-throughput localization is compatible with broad trafficking biology but does not define ARF1 core function.
    action: MARK_AS_OVER_ANNOTATED
    reason: High-throughput compartment detections should not outweigh the well-supported Golgi/TGN trafficking model for ARF1.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:23533145
  qualifier: located_in
  review:
    summary: This high-throughput localization is compatible with broad trafficking biology but does not define ARF1 core function.
    action: MARK_AS_OVER_ANNOTATED
    reason: High-throughput compartment detections should not outweigh the well-supported Golgi/TGN trafficking model for ARF1.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
- term:
    id: GO:0003723
    label: RNA binding
  evidence_type: HDA
  original_reference_id: PMID:22681889
  qualifier: enables
  review:
    summary: RNA binding is from a high-throughput mRNA-bound proteome study and is not a known ARF1 biochemical function.
    action: MARK_AS_OVER_ANNOTATED
    reason: The canonical ARF1 function is guanine nucleotide binding/hydrolysis and membrane trafficking; RNA binding should not be promoted without targeted validation.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
- term:
    id: GO:0002090
    label: regulation of receptor internalization
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: regulation of receptor internalization reflects transferred neuronal PICK1/AMPAR-related ARF1 biology.
    action: KEEP_AS_NON_CORE
    reason: These neuronal terms are plausible specialized contexts but are not the conserved core function of ARF1 and are supported by similarity transfer in this GOA set.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
- term:
    id: GO:0034315
    label: regulation of Arp2/3 complex-mediated actin nucleation
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: regulation of Arp2/3 complex-mediated actin nucleation reflects transferred neuronal PICK1/AMPAR-related ARF1 biology.
    action: KEEP_AS_NON_CORE
    reason: These neuronal terms are plausible specialized contexts but are not the conserved core function of ARF1 and are supported by similarity transfer in this GOA set.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
- term:
    id: GO:0060292
    label: long-term synaptic depression
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: long-term synaptic depression reflects transferred neuronal PICK1/AMPAR-related ARF1 biology.
    action: KEEP_AS_NON_CORE
    reason: These neuronal terms are plausible specialized contexts but are not the conserved core function of ARF1 and are supported by similarity transfer in this GOA set.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
- term:
    id: GO:0097061
    label: dendritic spine organization
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: dendritic spine organization reflects transferred neuronal PICK1/AMPAR-related ARF1 biology.
    action: KEEP_AS_NON_CORE
    reason: These neuronal terms are plausible specialized contexts but are not the conserved core function of ARF1 and are supported by similarity transfer in this GOA set.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Neuronal annotations transferred from orthology, including postsynaptic density, synapse, receptor internalization, Arp2/3 regulation, long-term synaptic depression, and dendritic spine organization, are retained only as non-core specialized contexts.
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:19199708
  qualifier: located_in
  review:
    summary: This high-throughput localization is compatible with broad trafficking biology but does not define ARF1 core function.
    action: MARK_AS_OVER_ANNOTATED
    reason: High-throughput compartment detections should not outweigh the well-supported Golgi/TGN trafficking model for ARF1.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:20458337
  qualifier: located_in
  review:
    summary: This high-throughput localization is compatible with broad trafficking biology but does not define ARF1 core function.
    action: MARK_AS_OVER_ANNOTATED
    reason: High-throughput compartment detections should not outweigh the well-supported Golgi/TGN trafficking model for ARF1.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: High-throughput-only focal adhesion, extracellular exosome, and RNA-binding annotations are treated as over-annotated because they do not define the established ARF1 Golgi/TGN trafficking function.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1675883
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1676152
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-2130619
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-350769
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-421831
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-421833
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-432706
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-432712
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8847875
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8847880
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8847883
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8870499
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8951498
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0000139
    label: Golgi membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9845055
  qualifier: located_in
  review:
    summary: Golgi membrane localization is central to ARF1 function in coat recruitment and Golgi/TGN trafficking.
    action: ACCEPT
    reason: ARF1 cycles between cytosol and Golgi/TGN membranes, where the active GTP-bound form recruits coat and lipid-metabolism effectors.
    supported_by:
    - reference_id: PMID:17555535
      supporting_text: ARF1 but not ARF5 or 6 enhanced the stimulatory effect of PI4Kbeta on regulated exocytosis.
    - reference_id: PMID:15107860
      supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-200879
  qualifier: located_in
  review:
    summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles.
    action: ACCEPT
    reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-350769
  qualifier: located_in
  review:
    summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles.
    action: ACCEPT
    reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-421831
  qualifier: located_in
  review:
    summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles.
    action: ACCEPT
    reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-432706
  qualifier: located_in
  review:
    summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles.
    action: ACCEPT
    reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8950173
  qualifier: located_in
  review:
    summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles.
    action: ACCEPT
    reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8951498
  qualifier: located_in
  review:
    summary: Cytosolic localization is consistent with the soluble GDP-bound pool of ARF1 between membrane-recruitment cycles.
    action: ACCEPT
    reason: ARF1 is a peripheral, myristoylated small GTPase that cycles between cytosol and membranes; cytosol is therefore a real localization, though not the active membrane-bound state.
    supported_by:
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: Cytosol and endomembrane annotations are accurate localization context for a cycling peripheral membrane GTPase, but the active functional emphasis remains Golgi/TGN membrane recruitment and coat/adaptor regulation.
- term:
    id: GO:0006878
    label: intracellular copper ion homeostasis
  evidence_type: IMP
  original_reference_id: PMID:21034850
  qualifier: involved_in
  review:
    summary: ARF1-dependent trafficking affects copper uptake and CTR1 distribution.
    action: KEEP_AS_NON_CORE
    reason: This is experimentally supported but appears to be a cargo/trafficking consequence rather than ARF1's primary molecular role.
    supported_by:
    - reference_id: PMID:21034850
      supporting_text: Arf1-dependent trafficking pathways are therefore required for optimal copper uptake efficiency.
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: PMID:8529647
  qualifier: located_in
  review:
    summary: Plasma membrane association/activity is reported in signaling and PLD contexts but is not the primary ARF1 compartment.
    action: KEEP_AS_NON_CORE
    reason: ARF1 can participate in plasma-membrane-linked signaling or trafficking, but the dominant conserved role is Golgi/TGN membrane trafficking.
    supported_by:
    - reference_id: PMID:8529647
      supporting_text: The results indicate that ARF proteins and their nucleotide-exchange factor are apparently involved in the signalling pathway leading from mAChR activation to PLD stimulation in human embryonic kidney cells.
- term:
    id: GO:0006890
    label: retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6811434
  qualifier: involved_in
  review:
    summary: PN projection and Reactome support adding the specific Golgi-to-ER retrograde transport process for ARF1.
    action: NEW
    reason: ARF1 is the regulatory small GTPase that promotes coat recruitment and controls COPI coat cycling. This supports a process-level retrograde transport annotation, while the projected COPI vesicle coat component term should not be added because ARF1 is not a coatomer subunit.
    additional_reference_ids:
    - Reactome:R-HSA-6811434
    - file:human/ARF1/ARF1-notes.md
    supported_by:
    - reference_id: Reactome:R-HSA-6811434
      supporting_text: Retrograde traffic from the cis-Golgi to the ERGIC or the ER is mediated in part by microtubule-directed COPI-coated vesicles
    - reference_id: PMID:8253837
      supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
    - reference_id: PMID:10102276
      supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
    - reference_id: file:human/ARF1/ARF1-notes.md
      supporting_text: The projected `GO:0030126 COPI vesicle coat` should not be added for ARF1.
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO terms
  findings: []
- id: GO_REF:0000003
  title: Gene Ontology annotation based on Enzyme Commission mapping
  findings: []
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:10022920
  title: Identification of a new Pyk2 target protein with Arf-GAP activity.
  findings: []
- id: PMID:10102276
  title: Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis.
  findings: []
- id: PMID:10198630
  title: 'Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain.'
  findings: []
- id: PMID:12668765
  title: 'Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor.'
  findings: []
- id: PMID:12771146
  title: The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1.
  findings: []
- id: PMID:14654833
  title: Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor.
  findings: []
- id: PMID:15107860
  title: FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P.
  findings: []
- id: PMID:17555535
  title: Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta.
  findings: []
- id: PMID:17563369
  title: Structure-based discovery of an inhibitor of Arf activation by Sec7 domains through targeting of protein-protein complexes.
  findings: []
- id: PMID:17687330
  title: Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide.
  findings: []
- id: PMID:17956946
  title: Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking.
  findings: []
- id: PMID:19199708
  title: Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
  findings: []
- id: PMID:19644450
  title: 'The structural basis of Arf effector specificity: the crystal structure of ARF6 in a complex with JIP4.'
  findings: []
- id: PMID:20458337
  title: MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis.
  findings: []
- id: PMID:21034850
  title: The ADP-ribosylation factor 1 (Arf1) is involved in regulating copper uptake.
  findings: []
- id: PMID:21423176
  title: "Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for \u03B2-Pix in negative regulation of focal adhesion maturation."
  findings: []
- id: PMID:22573891
  title: "GBF1 bears a novel phosphatidylinositol-phosphate binding module, BP3K, to link PI3K\u03B3 activity with Arf1 activation involved in GPCR-mediated neutrophil chemotaxis and superoxide production."
  findings: []
- id: PMID:22681889
  title: The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.
  findings: []
- id: PMID:22981988
  title: The BAR domain protein Arfaptin-1 controls secretory granule biogenesis at the trans-Golgi network.
  findings: []
- id: PMID:23533145
  title: In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
  findings: []
- id: PMID:28389568
  title: Hepatitis C virus triggers Golgi fragmentation and autophagy through the immunity-related GTPase M.
  findings: []
- id: PMID:31467278
  title: Maximizing binary interactome mapping with a minimal number of assays.
  findings: []
- id: PMID:35271311
  title: 'OpenCell: Endogenous tagging for the cartography of human cellular organization.'
  findings: []
- id: PMID:36396045
  title: Targeting ARF1-IQGAP1 interaction to suppress colorectal cancer metastasis and vemurafenib resistance.
  findings: []
- id: PMID:41293316
  title: Loss of ARF5 impairs recovery after lysosomal damage.
  findings: []
- id: PMID:8253837
  title: Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles.
  findings: []
- id: PMID:8529647
  title: Evidence for ADP-ribosylation-factor-mediated activation of phospholipase D by m3 muscarinic acetylcholine receptor.
  findings: []
- id: PMID:37914730
  title: ARF1 prevents aberrant type I interferon induction by regulating STING activation and recycling.
  full_text_unavailable: true
  findings:
  - statement: ARF1 is a negative regulator of cGAS-STING type I interferon signaling; GTPase-defective heterozygous ARF1 missense mutations (e.g. R99C/R99H) cause a type I interferonopathy, with mutant ARF1 perturbing mitochondrial integrity (driving mtDNA release and cGAS activation) and causing accumulation of active STING at the Golgi/ERGIC due to defective retrograde transport.
- id: PMID:37400497
  title: Arf1 coordinates fatty acid metabolism and mitochondrial homeostasis.
  full_text_unavailable: true
  findings:
  - statement: Arf1 integrates cellular metabolism with energy production by regulating fatty-acid storage and utilization; a hyperactive Arf1 mutant causes fatty-acid accumulation in lipid droplets, mitochondrial fragmentation, and decreased ATP synthesis, with the role in fatty-acid metabolism conserved in mammals and proposed to act via organelle contact sites.
- id: PMID:36269825
  title: 'Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat.'
  findings:
  - statement: Myristoylated GTP-bound Arf1 recruits AP-1 and stabilizes it in an active conformation, and AP-1:Arf1 self-assembles into a clathrin-independent tubular membrane coat via Arf1 dimer interfaces; HIV-1 Nef hijacks this AP-1:Arf1 coat to sequester MHC-I, and coat-contact residues are conserved across Arf isoforms and AP-1/AP-3/AP-4.
- id: Reactome:R-HSA-1675883
  title: PI is phosphorylated to PI4P by PI4KB at the Golgi membrane
  findings: []
- id: Reactome:R-HSA-1676152
  title: PI4KB binds to ARF1/3:GTP at the Golgi membrane
  findings: []
- id: Reactome:R-HSA-200879
  title: Formation of a Nef:ARF1:CD4 complex
  findings: []
- id: Reactome:R-HSA-2130619
  title: TGN-lysosomal vesicle coat assembly
  findings: []
- id: Reactome:R-HSA-350769
  title: trans-Golgi Network Coat Activation
  findings: []
- id: Reactome:R-HSA-421831
  title: trans-Golgi Network Coat Assembly
  findings: []
- id: Reactome:R-HSA-421833
  title: Vamp And trans-Golgi Network AP-1 Binding Coupled With Cargo Capture
  findings: []
- id: Reactome:R-HSA-432706
  title: trans-Golgi Network Lysosome Vesicle Destined Membrane Coat Assembly
  findings: []
- id: Reactome:R-HSA-432712
  title: Vamp And trans-Golgi Network AP-1 Binding Coupled With Cargo Capture On Lysosome Vesicle Destined Golgi Membrane
  findings: []
- id: Reactome:R-HSA-8847875
  title: ARF1:GTP binds Golgin TRIP11
  findings: []
- id: Reactome:R-HSA-8847880
  title: CYTH proteins bind ARF1:GTP
  findings: []
- id: Reactome:R-HSA-8847883
  title: CYTH proteins stimulate ARF1 GTPase activity
  findings: []
- id: Reactome:R-HSA-8870499
  title: PLEKHA3,8 bind PI4P, ARF1
  findings: []
- id: Reactome:R-HSA-8950173
  title: Expression of ADP-ribosylation factor 1
  findings: []
- id: Reactome:R-HSA-8951498
  title: Dissociation of Arf1:GDP, AP-1 Clathrin coated nonameric complex
  findings: []
- id: Reactome:R-HSA-9845055
  title: PLEKHA8 catalyzes transport of GlcCer to plasma membrane
  findings: []
- id: file:human/ARF1/ARF1-notes.md
  title: ARF1 PN review notes
  findings:
  - statement: ARF1 is a regulatory ARF-family GTPase for Golgi/TGN trafficking; PN retrograde transport propagation is supported, but COPI vesicle coat component propagation is rejected.
- id: Reactome:R-HSA-6811434
  title: COPI-dependent Golgi-to-ER retrograde traffic
  findings:
  - statement: Reactome pathway supporting ARF1 participation in COPI-dependent Golgi-to-ER retrograde traffic.
- id: Reactome:R-HSA-6807878
  title: COPI-mediated anterograde transport
  findings: []
- id: Reactome:R-HSA-6811438
  title: Intra-Golgi traffic
  findings: []
- id: Reactome:R-HSA-432720
  title: Lysosome Vesicle Biogenesis
  findings: []
- id: Reactome:R-HSA-432722
  title: Golgi Associated Vesicle Biogenesis
  findings: []
- id: Reactome:R-HSA-9845576
  title: Glycosphingolipid transport
  findings: []
core_functions:
- description: ARF1 functions as a guanine-nucleotide-regulated membrane-trafficking switch at Golgi and TGN membranes. In its GTP-bound state it recruits coat/adaptor and lipid-metabolism effectors, including machinery for COPI-dependent Golgi-to-ER and intra-Golgi trafficking; GTP hydrolysis stimulated by ARFGAPs and coatomer promotes coat disassembly and recycling of the trafficking machinery. ARF1 is therefore best represented as a regulatory small GTPase in vesicle-mediated intracellular transport, not as a structural COPI coat subunit.
  molecular_function:
    id: GO:0003924
    label: GTPase activity
  directly_involved_in:
  - id: GO:0006886
    label: intracellular protein transport
  - id: GO:0006890
    label: retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
  - id: GO:1903292
    label: protein localization to Golgi membrane
  locations:
  - id: GO:0000139
    label: Golgi membrane
  - id: GO:0160281
    label: cytoplasmic side of trans-Golgi network membrane
  - id: GO:0005829
    label: cytosol
  supported_by:
  - reference_id: PMID:8253837
    supporting_text: The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport.
  - reference_id: PMID:10102276
    supporting_text: a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.
  - reference_id: Reactome:R-HSA-6811434
    supporting_text: Retrograde traffic from the cis-Golgi to the ERGIC or the ER is mediated in part by microtubule-directed COPI-coated vesicles
  - reference_id: PMID:15107860
    supporting_text: FAPPs are essential components of a PtdIns(4)P- and ARF-regulated machinery.
proposed_new_terms: []
suggested_questions:
- question: Should PN-to-GO propagation for `COPI coating and uncoating` distinguish structural coatomer subunits from regulatory GTPases such as ARF1 so that `GO:0030126 COPI vesicle coat` is not projected to ARF1?
- question: Would a process term for ARF-dependent COPI coat assembly/disassembly better capture ARF1 than the cellular-component term `COPI vesicle coat`?
- question: Should ARF1's role in terminating cGAS-STING signaling via retrograde Golgi-to-ER recycling of STING be captured as a distinct negative-regulation-of-type-I-interferon process annotation, or does it remain a downstream consequence of the core retrograde-transport function?
suggested_experiments:
- description: Use acute endogenous ARF1 depletion or rapid ARF1 inactivation together with rescue by GTPase-cycle mutants, then quantify KDEL receptor/chaperone retrieval from Golgi to ER and COPI coat recruitment/uncoating kinetics.
  hypothesis: ARF1 GTPase cycling is required for efficient Golgi-to-ER retrieval of escaped ER proteins, supporting the retrograde-transport annotation without implying ARF1 is a structural COPI coat component.
  experiment_type: cell biology
- description: Perform proximity labeling of endogenous ARF1 during synchronized COPI budding/uncoating and compare enrichment of coatomer subunits, ARFGAPs, KDEL receptors, and cargo proteins across GTP-locked and GDP-locked ARF1 states.
  hypothesis: ARF1 associates transiently with COPI coat-cycle machinery as a regulatory GTPase rather than as a stable COPI coat constituent.
  experiment_type: proteomics
- description: Express disease-associated GTPase-defective ARF1 variants (e.g. R99C/R99H) in ARF1-edited cells and quantify STING retrograde Golgi-to-ER recycling, mitochondrial morphology and mtDNA release, and interferon-stimulated gene induction relative to wild-type ARF1 rescue.
  hypothesis: Loss of ARF1 GTPase cycling impairs STING retrograde transport and mitochondrial integrity, causing cGAS-STING-dependent type I interferon hyperactivation, distinct from ARF1's bulk Golgi/TGN coat-recruitment role.
  experiment_type: cell biology

ARF1

Gene Description

Existing Annotations Review

Core Functions

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

Research report: Human ARF1 (UniProt P84077) — functional annotation

0) Target verification (gene/protein identity)

1) Key concepts and definitions (current understanding)

1.1 ARF1 as a membrane-coupled GTPase cycle (enzymology)

1.2 Domain architecture and family context

2) ARF1 primary cellular functions (what ARF1 does)

2.1 Core role: vesicle biogenesis and coat/adaptor recruitment

2.2 Lipid microdomain control and membrane identity (substrate specificity in context)

2.3 Beyond trafficking: nutrient signaling and organelle homeostasis

3) Subcellular localization (where ARF1 acts)

3.1 Golgi/ERGIC axis

3.2 TGN/endosomes and trafficking intermediates

3.3 Mitochondria-related locations / contact sites

4) Recent developments (prioritizing 2023–2024)

4.1 ARF1 in innate immunity: controlling cGAS–STING signaling (2023)

4.2 Metabolism/mitochondria: ARF1 integrates fatty-acid metabolism with mitochondrial homeostasis (2023)

4.3 Compartment-specific ARF1 activation via GEFs in physiology (2024)

5) Applications and real-world implementations

5.1 Pathogen exploitation of ARF1-dependent trafficking

5.2 Chemical biology and therapeutic exploration targeting the ARF pathway

6) Disease associations and expert consensus views

7) Evidence figure (structural/functional context)

8) Summary: functional annotation of ARF1 (P84077)

9) Key cited sources (URLs; publication dates)

Artifacts

Citations

📚 Additional Documentation

Notes

2026-06-03 - Proteostasis PN review

Falcon deep research findings (2026-06-07)

Pn Notes

ARF1 PN Consistency Notes

Source Files Checked

Deep Research Files

AIGR Review Snapshot

PN Consistency Summary

Full Consistency Review

PN Dossier Context

PN row 1: ER proteostasis | Protein transport | ER-Golgi trafficking | Retrograde transport | COPI coating and uncoating

Projected GO annotations (3)

Note

📄 View Raw YAML