COPG1 encodes the gamma-1 subunit (gamma-1-COP) of the heptameric coatomer (COPI) complex. COPI is a cytosolic protein complex that reversibly associates with Golgi membranes and is essential for retrograde vesicle-mediated transport from the Golgi apparatus to the endoplasmic reticulum (ER). The gamma subunit resides in the adaptor "F" subcomplex (gamma/zeta) that connects ARF1-GTP to the coat and participates in cargo selection and vesicle formation. COPG1 contributes to recognition of dilysine (KKxx/KxKxx) retrieval motifs on cargo proteins and interacts with KDEL receptors for retrograde trafficking of ER-resident proteins. Mutations in COPG1 cause immunodeficiency 128 (IMD128), characterized by recurrent infections and ER stress due to defective retrograde transport of KDEL-bearing chaperones.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0030126 COPI vesicle coat | IBA GO_REF:0000033 | ACCEPT | Summary: COPG1 is a core structural subunit of the COPI vesicle coat. The COPI complex is a heptamer consisting of alpha, beta, beta', gamma, delta, epsilon and zeta subunits. gamma-COP (COPG1) is part of the adaptor F subcomplex (gamma/zeta) that mediates ARF1 binding and cargo selection. Reason: This is a well-established core function of COPG1. The deep research confirms that COPG1 is an essential component of the COPI coat, residing in the gamma/zeta adaptor subcomplex. UniProt describes this as a subunit of the "oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits." Supporting Evidence: PMID:11056392 The COP I coat is composed of seven subunits, alpha-, beta-, beta'-, gamma-, delta-, epsilon-, and zeta-COPs file:human/COPG1/COPG1-deep-research-falcon.md COPI architecture and COPG1's role: COPI is a heptamer (alpha, beta, beta', gamma, delta, epsilon, zeta). gamma-COP (COPG1) resides in the adaptor "F" subcomplex (gamma/zeta) that connects ARF1 to the coat and participates in cargo selection and vesicle formation. |
| GO:0072384 organelle transport along microtubule | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: COPI-coated vesicles are transported along microtubules between the Golgi and ER. The annotation is based on phylogenetic inference. While COPG1 is part of the vesicle coat, the direct role in microtubule-based transport is more a property of the motor proteins that interact with COPI vesicles. Reason: While COPI vesicles do travel along microtubules (as shown in Reactome pathway R-HSA-6809003 "ERGIC-to-Golgi vesicles bind dynein:dynactin"), COPG1's primary function is as a structural component of the coat, not as a motor or microtubule-binding protein. The transport along microtubules is mediated by dynein/dynactin that associate with the vesicles. This annotation represents an indirect consequence of being part of the transported vesicle coat. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI functions predominantly at cis-Golgi/ERGIC and mediates GolgiβER and intra-Golgi retrograde traffic |
| GO:0000139 Golgi membrane | IBA GO_REF:0000033 | ACCEPT | Summary: COPG1 localizes to the Golgi membrane as part of the COPI coat complex. UniProt confirms "Golgi apparatus membrane" localization with experimental evidence. Reason: COPG1 localizes to Golgi membranes where COPI is recruited by ARF1-GTP. This is well supported by UniProt subcellular location data showing "Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side" with experimental evidence from PMID:11056392. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region file:human/COPG1/COPG1-deep-research-falcon.md ARF1-GTP recruits coatomer to cis-Golgi/ERGIC membranes, where COPI polymerizes, generates curvature, and buds vesicles |
| GO:0005783 endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: COPI vesicles deliver their cargo to the ER, and the coat is released upon vesicle uncoating at the ER. COPG1 transiently associates with ER membranes during this process. Reason: COPI-mediated retrograde transport terminates at the ER, where COPI vesicles fuse and the coat (including COPG1) is released. The Reactome pathways (R-HSA-6811423 and R-HSA-6811427) document ER membrane localization during vesicle tethering and uncoating. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI's principal routes are GolgiβER retrograde retrieval (e.g., KDEL receptor/cargo receptors) and intra-Golgi retrograde transport |
| GO:0005793 endoplasmic reticulum-Golgi intermediate compartment | IBA GO_REF:0000033 | ACCEPT | Summary: The ERGIC is a key site of COPI function. COPI is recruited to ERGIC membranes and mediates retrograde transport from ERGIC back to the ER. Reason: The ERGIC is a documented site of COPI activity. GBF1 (ARF-GEF) activates ARF1 at ER-Golgi intermediates, enabling COPI recruitment. This is well supported by the literature. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md GBF1 (an ARF-GEF) activates ARF1 at ERβGolgi intermediates, enabling COPI recruitment and maturation of carriers moving toward the Golgi; COPI cycles rapidly on/off membranes |
| GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport | IBA GO_REF:0000033 | MODIFY | Summary: This annotation is problematic. COPI is primarily involved in RETROGRADE transport (Golgi-to-ER), not anterograde (ER-to-Golgi) transport. ER-to-Golgi anterograde transport is mediated by COPII, not COPI. Reason: COPI's primary function is retrograde transport from Golgi to ER, not anterograde transport. While COPI may have some role in ERGIC maturation during anterograde traffic, this is not its core function. The correct annotation should be for retrograde transport. This may represent an IBA inference that was too broad. Proposed replacements: retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI's principal routes are GolgiβER retrograde retrieval (e.g., KDEL receptor/cargo receptors) and intra-Golgi retrograde transport PMID:33529166 The coat protein I (COPI) complex mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) |
| GO:0006891 intra-Golgi vesicle-mediated transport | IBA GO_REF:0000033 | ACCEPT | Summary: COPI is involved in retrograde transport within the Golgi stack, moving material from trans to cis cisternae as part of cisternal maturation. Reason: Intra-Golgi retrograde transport is a well-documented function of COPI. The deep research confirms COPI's role in "GolgiβER retrograde retrieval and intra-Golgi retrograde transport." Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI's principal routes are GolgiβER retrograde retrieval (e.g., KDEL receptor/cargo receptors) and intra-Golgi retrograde transport |
| GO:0009306 protein secretion | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: While COPI function is essential for maintaining secretory pathway homeostasis, its direct role is in retrograde transport, not anterograde secretion. Reason: COPI's retrograde transport is required for recycling ER-resident proteins and maintaining the secretory pathway, but this is an indirect effect. COPI does not directly mediate anterograde secretion - that is COPII's role. This annotation may be too broad but represents a downstream consequence of COPI function. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md Core function of COPI: ARF1-GTP recruits coatomer to cis-Golgi/ERGIC membranes, where COPI polymerizes, generates curvature, and buds vesicles; subsequent ARF1 GTP hydrolysis triggers uncoating and fusion at target membranes |
| GO:0000139 Golgi membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic annotation supporting Golgi membrane localization, consistent with IBA and experimental evidence. Reason: This is consistent with the IBA annotation and experimental data. Redundant but correct. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region |
| GO:0005198 structural molecule activity | IEA GO_REF:0000002 | ACCEPT | Summary: COPG1 functions as a structural component of the COPI coatomer complex. The annotation is derived from InterPro domain mapping. Reason: COPG1's primary molecular function is structural - it is an essential subunit of the COPI coat that contributes to coat assembly, membrane curvature, and vesicle formation. This is appropriate as a high-level MF term. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md gamma-COP (COPG1) resides in the adaptor "F" subcomplex (gamma/zeta) that connects ARF1 to the coat and participates in cargo selection and vesicle formation |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: COPG1 is cytoplasmic when not membrane-associated. The coatomer cycles between cytosol and Golgi/ERGIC membranes. Reason: UniProt confirms cytoplasmic localization. "The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi." Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI cycles rapidly on/off membranes, requiring continuous cytosolic recruitment |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000117 | ACCEPT | Summary: General Golgi apparatus localization, consistent with more specific Golgi membrane annotations. Reason: Correct but less specific than Golgi membrane annotations. Consistent with experimental and IBA evidence. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region |
| GO:0006886 intracellular protein transport | IEA GO_REF:0000002 | ACCEPT | Summary: COPG1 is involved in intracellular protein transport as part of the COPI coat. This is a broad but accurate annotation. Reason: COPI mediates intracellular protein transport, specifically retrograde transport from Golgi to ER. This general annotation is correct. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI's principal routes are GolgiβER retrograde retrieval (e.g., KDEL receptor/cargo receptors) and intra-Golgi retrograde transport |
| GO:0015031 protein transport | IEA GO_REF:0000043 | ACCEPT | Summary: Very broad annotation for protein transport, derived from UniProt keyword mapping. Reason: Correct but very general. COPG1 is involved in protein transport via COPI-mediated vesicle trafficking. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI's principal routes are GolgiβER retrograde retrieval |
| GO:0016192 vesicle-mediated transport | IEA GO_REF:0000120 | ACCEPT | Summary: COPG1 functions in vesicle-mediated transport as a component of the COPI vesicle coat. Reason: Correct and well-supported. COPI mediates vesicle-mediated transport between Golgi and ER compartments. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md ARF1-GTP recruits coatomer to cis-Golgi/ERGIC membranes, where COPI polymerizes, generates curvature, and buds vesicles |
| GO:0030117 membrane coat | IEA GO_REF:0000002 | ACCEPT | Summary: COPG1 is part of a membrane coat - specifically the COPI vesicle coat. This is the parent term of COPI vesicle coat. Reason: Correct as a more general cellular component annotation. COPG1 is part of the COPI membrane coat. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI is a heptamer (alpha, beta, beta', gamma, delta, epsilon, zeta) |
| GO:0030126 COPI vesicle coat | IEA GO_REF:0000002 | ACCEPT | Summary: Electronic annotation from InterPro mapping confirming COPI vesicle coat component. Reason: Correct and consistent with IBA annotation. Core localization for COPG1. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md gamma-COP (COPG1) resides in the adaptor "F" subcomplex (gamma/zeta) |
| GO:0030133 transport vesicle | IEA GO_REF:0000117 | ACCEPT | Summary: General transport vesicle localization. COPG1 is found on COPI-coated transport vesicles. Reason: Correct but general. COPI vesicles are transport vesicles that carry cargo between Golgi and ER. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI polymerizes, generates curvature, and buds vesicles |
| GO:0030663 COPI-coated vesicle membrane | IEA GO_REF:0000044 | ACCEPT | Summary: COPG1 localizes to COPI-coated vesicle membrane as a peripheral membrane protein on the cytoplasmic face. Reason: Correct and specific localization. UniProt confirms "Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side." Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI polymerizes, generates curvature, and buds vesicles; subsequent ARF1 GTP hydrolysis triggers uncoating |
| GO:0031090 organelle membrane | IEA GO_REF:0000117 | ACCEPT | Summary: Very broad annotation for organelle membrane localization. Reason: Correct but very general. COPG1 associates with Golgi and ER membranes, which are organelle membranes. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region |
| GO:0031410 cytoplasmic vesicle | IEA GO_REF:0000043 | ACCEPT | Summary: General cytoplasmic vesicle localization. COPI vesicles are cytoplasmic vesicles. Reason: Correct but general. COPI-coated vesicles are cytoplasmic vesicles. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI polymerizes, generates curvature, and buds vesicles |
| GO:0051683 establishment of Golgi localization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: COPI function is important for Golgi integrity and organization. This annotation reflects COPI's role in maintaining Golgi structure through retrograde transport. Reason: COPI retrograde transport helps maintain Golgi organization by recycling proteins and lipids, but this is an indirect effect of its primary retrograde transport function rather than a direct role in Golgi localization establishment. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md the complex also influences the Golgi structural integrity |
| GO:0072384 organelle transport along microtubule | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic annotation from Ensembl Compara transfer, supporting COPI vesicle transport along microtubules. Reason: Same reasoning as IBA annotation - COPG1 is part of transported vesicles but does not directly mediate microtubule-based transport. This is an indirect role. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI functions predominantly at cis-Golgi/ERGIC |
| GO:0000139 Golgi membrane | NAS PMID:33378371 A genetic screen in Drosophila reveals an unexpected role fo... | ACCEPT | Summary: Golgi membrane localization from ComplexPortal annotation. Consistent with other evidence. Reason: Consistent with IBA and IEA annotations. Well-supported localization. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region PMID:33378371 eCollection 2020 Dec. |
| GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum | NAS PMID:33378371 A genetic screen in Drosophila reveals an unexpected role fo... | ACCEPT | Summary: Core biological process for COPG1 - retrograde transport from Golgi to ER. Reason: This is the primary biological process function of COPI and COPG1. The complex mediates retrograde transport of cargo bearing dilysine retrieval signals and KDEL receptor-bound cargo. This is extensively documented in the literature. Supporting Evidence: PMID:33529166 The coat protein I (COPI) complex mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) file:human/COPG1/COPG1-deep-research-falcon.md COPI's principal routes are GolgiβER retrograde retrieval (e.g., KDEL receptor/cargo receptors) and intra-Golgi retrograde transport PMID:33378371 eCollection 2020 Dec. |
| GO:0030126 COPI vesicle coat | NAS PMID:33378371 A genetic screen in Drosophila reveals an unexpected role fo... | ACCEPT | Summary: COPI vesicle coat component annotation from ComplexPortal. Reason: Core cellular component for COPG1. Consistent with IBA and IEA annotations. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI is a heptamer (alpha, beta, beta', gamma, delta, epsilon, zeta). gamma-COP (COPG1) resides in the adaptor "F" subcomplex PMID:33378371 eCollection 2020 Dec. |
| GO:0005794 Golgi apparatus | IDA GO_REF:0000052 | ACCEPT | Summary: Golgi apparatus localization from immunofluorescence data (HPA). Direct experimental evidence for Golgi localization. Reason: Direct experimental evidence from immunofluorescence confirms Golgi localization. This is consistent with COPG1's function as a COPI coat subunit. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-6811423 | ACCEPT | Summary: ER membrane localization during retrograde vesicle tethering at the ER. Reason: COPI vesicles are tethered at the ER membrane during retrograde transport. This Reactome annotation reflects the "Retrograde vesicle is tethered at the ER by the NRZ complex and t-SNAREs" step. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI's principal routes are GolgiβER retrograde retrieval |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-6811427 | ACCEPT | Summary: ER membrane localization during COPI vesicle uncoating at the ER. Reason: COPI uncoating occurs at the ER membrane. This Reactome annotation reflects "COPI vesicle uncoating at the ER" step where COPG1 is released from the vesicle. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md subsequent ARF1 GTP hydrolysis triggers uncoating and fusion at target membranes |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-6809006 | ACCEPT | Summary: Golgi membrane localization during vesicle tethering through GOLGA2:GORASP1. Reason: COPI vesicles are tethered at Golgi membranes. Consistent with core localization. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md ARF1-GTP recruits coatomer to cis-Golgi/ERGIC membranes |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-6809010 | ACCEPT | Summary: Golgi membrane localization during COPI vesicle uncoating. Reason: COPI uncoating also occurs at Golgi membranes during intra-Golgi transport. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md intra-Golgi retrograde transport |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-6809011 | ACCEPT | Summary: Golgi membrane localization during SNARE binding on tethered vesicle. Reason: Part of the COPI vesicle fusion process at Golgi membranes. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md ARF1-GTP recruits coatomer to cis-Golgi/ERGIC membranes |
| GO:0030133 transport vesicle | TAS Reactome:R-HSA-6807877 | ACCEPT | Summary: Transport vesicle localization during ARFGAPs stimulate ARF GTPase activity. Reason: COPG1 is present on transport vesicles during the ARF GTPase cycle. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI polymerizes, generates curvature, and buds vesicles |
| GO:0030133 transport vesicle | TAS Reactome:R-HSA-6809003 | ACCEPT | Summary: Transport vesicle localization during ERGIC-to-Golgi vesicle binding to dynein. Reason: COPI vesicles bind dynein:dynactin for transport along microtubules. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI functions predominantly at cis-Golgi/ERGIC |
| GO:0030133 transport vesicle | TAS Reactome:R-HSA-6809006 | ACCEPT | Summary: Transport vesicle localization during vesicle tethering. Reason: COPI vesicles are tethered through interactions with golgins and COG complex. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI polymerizes, generates curvature, and buds vesicles |
| GO:0030133 transport vesicle | TAS Reactome:R-HSA-6811418 | ACCEPT | Summary: Transport vesicle localization during ARFGAPs stimulate ARF GTPase activity at Golgi. Reason: Part of the COPI vesicle biogenesis cycle at the Golgi. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI polymerizes, generates curvature, and buds vesicles |
| GO:0030133 transport vesicle | TAS Reactome:R-HSA-6811423 | ACCEPT | Summary: Transport vesicle localization during retrograde vesicle tethering at ER. Reason: COPI vesicles are tethered at the ER by the NRZ complex. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI's principal routes are GolgiβER retrograde retrieval |
| GO:0030133 transport vesicle | TAS Reactome:R-HSA-6811426 | ACCEPT | Summary: Transport vesicle localization during retrograde COPI vesicle binding to kinesin. Reason: Retrograde COPI vesicles bind kinesin and microtubules for transport to ER. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI functions predominantly at cis-Golgi/ERGIC and mediates GolgiβER |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6807872 | ACCEPT | Summary: Cytosol localization during active ARF recruits coatomer step. Reason: Coatomer is recruited from the cytosol to membranes by ARF1-GTP. The free coatomer pool is cytosolic. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI cycles rapidly on/off membranes, requiring continuous cytosolic recruitment |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6807875 | ACCEPT | Summary: Cytosol localization during ARFGAP, cargo, v-SNAREs and p24 proteins bind nascent COPI complex. Reason: Cytosolic coatomer is recruited and additional factors bind during coat assembly. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI cycles rapidly on/off membranes, requiring continuous cytosolic recruitment |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6807877 | ACCEPT | Summary: Cytosol localization during ARFGAPs stimulate ARF GTPase activity. Reason: ARF GTPase cycle occurs at the cytosolic face of membranes. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md subsequent ARF1 GTP hydrolysis triggers uncoating |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6809010 | ACCEPT | Summary: Cytosol localization during COPI vesicle uncoating. Reason: Upon uncoating, COPG1 is released back to the cytosol. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md subsequent ARF1 GTP hydrolysis triggers uncoating |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6811412 | ACCEPT | Summary: Cytosol localization during active ARF recruits coatomer to the Golgi. Reason: Coatomer is recruited from cytosol to Golgi membranes. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md ARF1-GTP recruits coatomer to cis-Golgi/ERGIC membranes |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6811417 | ACCEPT | Summary: Cytosol localization during cargo and adaptor binding at Golgi. Reason: Cytosolic face of Golgi where coat assembly occurs. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI cycles rapidly on/off membranes |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6811418 | ACCEPT | Summary: Cytosol localization during ARFGAPs stimulate ARF GTPase activity at Golgi membrane. Reason: ARF GTPase activity regulation occurs at cytosolic face. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md subsequent ARF1 GTP hydrolysis triggers uncoating |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6811427 | ACCEPT | Summary: Cytosol localization during COPI vesicle uncoating at the ER. Reason: Upon uncoating at ER, coatomer is released to cytosol. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md subsequent ARF1 GTP hydrolysis triggers uncoating and fusion at target membranes |
| GO:0000139 Golgi membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Golgi membrane localization transferred from rat ortholog (Q4AEF8). Reason: Consistent with other evidence. COPG1 is well-conserved and the function is expected to be conserved across mammals. Supporting Evidence: PMID:11056392 Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region |
| GO:0051683 establishment of Golgi localization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Golgi localization establishment transferred from rat ortholog. Reason: COPI function contributes to Golgi organization but this is an indirect effect. Consistent with IEA annotation. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md the complex also influences the Golgi structural integrity |
| GO:0072384 organelle transport along microtubule | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Microtubule transport transferred from rat ortholog. Reason: COPI vesicles are transported along microtubules but COPG1 does not directly mediate this - motor proteins do. Indirect role. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md COPI functions predominantly at cis-Golgi/ERGIC |
| GO:0030126 COPI vesicle coat | ISS GO_REF:0000024 | ACCEPT | Summary: COPI vesicle coat component transferred from yeast ortholog (P53620). Reason: Core localization for COPG1. COPI is conserved from yeast to humans. Supporting Evidence: file:human/COPG1/COPG1-deep-research-falcon.md gamma-COP (COPG1) resides in the adaptor "F" subcomplex (gamma/zeta) |
| GO:0048205 COPI coating of Golgi vesicle | TAS PMID:33529166 Combined immunodeficiency due to a mutation in the Ξ³1 subuni... | NEW | Summary: COPG1 is directly involved in the COPI coating process. As part of the gamma/zeta adaptor subcomplex, it participates in coat assembly on Golgi membranes. Reason: This biological process term specifically describes the function of COPI subunits including COPG1. The deep research confirms that COPI "polymerizes, generates curvature, and buds vesicles" and the gamma subunit is essential for this process. The COPG1 K652E mutation causes immunodeficiency due to defective COPI function. Supporting Evidence: PMID:33529166 The coat protein I (COPI) complex mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) file:human/COPG1/COPG1-deep-research-falcon.md ARF1-GTP recruits coatomer to cis-Golgi/ERGIC membranes, where COPI polymerizes, generates curvature, and buds vesicles |
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)