ID ARF1_HUMAN Reviewed; 181 AA. AC P84077; P10947; P32889; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 28-JAN-2026, entry version 210. DE RecName: Full=ADP-ribosylation factor 1; DE EC=3.6.5.2 {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10102276, ECO:0000269|PubMed:15107860, ECO:0000269|PubMed:8253837}; GN Name=ARF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2474826; DOI=10.1073/pnas.86.16.6101; RA Bobak D.A., Nightingale M.S., Murtagh J.J. Jr., Price S.R., Moss J., RA Vaughan M.; RT "Molecular cloning, characterization, and expression of human ADP- RT ribosylation factors: two guanine nucleotide-dependent activators of RT cholera toxin."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6101-6105(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1899243; DOI=10.1016/s0021-9258(18)52288-2; RA Kahn R.A., Kern F.G., Clark J., Gelmann E.P., Rulka C.; RT "Human ADP-ribosylation factors. A functionally conserved family of GTP- RT binding proteins."; RL J. Biol. Chem. 266:2606-2614(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1577740; DOI=10.1016/s0021-9258(19)50383-0; RA Lee C.M., Haun R.S., Tsai S.C., Moss J., Vaughan M.; RT "Characterization of the human gene encoding ADP-ribosylation factor 1, a RT guanine nucleotide-binding activator of cholera toxin."; RL J. Biol. Chem. 267:9028-9034(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=9110174; DOI=10.1101/gr.7.4.353; RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.; RT "Large-scale concatenation cDNA sequencing."; RL Genome Res. 7:353-358(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix, Eye, and Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 20-30; 80-97 AND 118-142, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLN-71. RX PubMed=8253837; DOI=10.1083/jcb.123.6.1365; RA Tanigawa G., Orci L., Amherdt M., Ravazzola M., Helms J.B., Rothman J.E.; RT "Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived RT COP-coated vesicles."; RL J. Cell Biol. 123:1365-1371(1993). RN [11] RP INTERACTION WITH HERC1, AND SUBCELLULAR LOCATION. RX PubMed=8861955; DOI=10.1002/j.1460-2075.1996.tb00801.x; RA Rosa J.L., Casaroli-Marano R.P., Buckler A.J., Vilaro S., Barbacid M.; RT "p619, a giant protein related to the chromosome condensation regulator RT RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins."; RL EMBO J. 15:4262-4273(1996). RN [12] RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH ASAP2. RX PubMed=10022920; DOI=10.1128/mcb.19.3.2338; RA Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G., Randazzo P.A., RA Schlessinger J.; RT "Identification of a new Pyk2 target protein with Arf-GAP activity."; RL Mol. Cell. Biol. 19:2338-2350(1999). RN [13] RP INTERACTION WITH GGA1; GGA2 AND GGA3. RX PubMed=11950392; DOI=10.1042/bj20020428; RA Takatsu H., Yoshino K., Toda K., Nakayama K.; RT "GGA proteins associate with Golgi membranes through interaction between RT their GGAH domains and ADP-ribosylation factors."; RL Biochem. J. 365:369-378(2002). RN [14] RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH PLEKHA8. RX PubMed=15107860; DOI=10.1038/ncb1119; RA Godi A., Di Campli A., Konstantakopoulos A., Di Tullio G., Alessi D.R., RA Kular G.S., Daniele T., Marra P., Lucocq J.M., De Matteis M.A.; RT "FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and RT PtdIns(4)P."; RL Nat. Cell Biol. 6:393-404(2004). RN [15] RP INTERACTION WITH ARHGAP21. RX PubMed=17347647; DOI=10.1038/sj.emboj.7601634; RA Menetrey J., Perderiset M., Cicolari J., Dubois T., Elkhatib N., RA El Khadali F., Franco M., Chavrier P., Houdusse A.; RT "Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi RT membranes."; RL EMBO J. 26:1953-1962(2007). RN [16] RP INTERACTION WITH PI4KB AND NCS1. RX PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x; RA Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.; RT "Specificity, promiscuity and localization of ARF protein interactions with RT NCS-1 and phosphatidylinositol-4 kinase-III beta."; RL Traffic 8:1080-1092(2007). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [18] RP MYRISTOYLATION AT GLY-2. RX PubMed=20213681; DOI=10.1002/pmic.200900783; RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., RA Tsunasawa S., Utsumi T.; RT "Strategy for comprehensive identification of human N-myristoylated RT proteins using an insect cell-free protein synthesis system."; RL Proteomics 10:1780-1793(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP INTERACTION WITH PLEKHA3. RX PubMed=21454700; DOI=10.1074/jbc.m111.233015; RA He J., Scott J.L., Heroux A., Roy S., Lenoir M., Overduin M., RA Stahelin R.V., Kutateladze T.G.; RT "Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase RT recognition by the FAPP1 pleckstrin homology (PH) domain."; RL J. Biol. Chem. 286:18650-18657(2011). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [22] RP MYRISTOYLATION AT GLY-2, AND DEMYRISTOYLATION. RX PubMed=23535599; DOI=10.1038/nature12004; RA Burnaevskiy N., Fox T.G., Plymire D.A., Ertelt J.M., Weigele B.A., RA Selyunin A.S., Way S.S., Patrie S.M., Alto N.M.; RT "Proteolytic elimination of N-myristoyl modifications by the Shigella RT virulence factor IpaJ."; RL Nature 496:106-109(2013). RN [23] RP INTERACTION WITH PICK1 AND GRIA2. RX PubMed=23889934; DOI=10.1016/j.neuron.2013.05.003; RA Rocca D.L., Amici M., Antoniou A., Suarez E.B., Halemani N., Murk K., RA McGarvey J., Jaafari N., Mellor J.R., Collingridge G.L., Hanley J.G.; RT "The small GTPase Arf1 modulates Arp2/3-mediated actin polymerization via RT PICK1 to regulate synaptic plasticity."; RL Neuron 79:293-307(2013). RN [24] RP INTERACTION WITH IQSEC1. RX PubMed=24058294; DOI=10.1371/journal.pbio.1001652; RA Aizel K., Biou V., Navaza J., Duarte L.V., Campanacci V., Cherfils J., RA Zeghouf M.; RT "Integrated conformational and lipid-sensing regulation of endosomal ArfGEF RT BRAG2."; RL PLoS Biol. 11:E1001652-E1001652(2013). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [26] RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25255805; DOI=10.1038/ncomms5919; RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.; RT "Global profiling of co- and post-translationally N-myristoylated proteomes RT in human cells."; RL Nat. Commun. 5:4919-4919(2014). RN [27] RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25807930; DOI=10.1002/anie.201500342; RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I., RA Tate E.W.; RT "Multifunctional reagents for quantitative proteome-wide analysis of RT protein modification in human cells and dynamic profiling of protein RT lipidation during vertebrate development."; RL Angew. Chem. Int. Ed. 54:5948-5951(2015). RN [28] RP INTERACTION WITH GGA3, INVOLVEMENT IN PVNH8, VARIANTS PVNH8 HIS-35; HIS-99 RP AND GLU-127, AND CHARACTERIZATION OF VARIANT PVNH8 HIS-35. RX PubMed=28868155; DOI=10.1038/npjgenmed.2016.36; RA Ge X., Gong H., Dumas K., Litwin J., Phillips J.J., Waisfisz Q., RA Weiss M.M., Hendriks Y., Stuurman K.E., Nelson S.F., Grody W.W., Lee H., RA Kwok P.Y., Shieh J.T.; RT "Missense-depleted regions in population exomes implicate ras superfamily RT nucleotide-binding protein alteration in patients with brain RT malformation."; RL NPJ Genom. Med. 1:0-0(2016). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [30] {ECO:0007744|PDB:1HUR} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GDP. RX PubMed=7990966; DOI=10.1038/372704a0; RA Amor J.C., Harrison D.H., Kahn R.A., Ringe D.; RT "Structure of the human ADP-ribosylation factor 1 complexed with GDP."; RL Nature 372:704-708(1994). RN [31] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RAT ARFGAP1 RP CATALYTIC DOMAIN, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=10102276; DOI=10.1016/s0092-8674(00)80598-x; RA Goldberg J.; RT "Structural and functional analysis of the ARF1-ARFGAP complex reveals a RT role for coatomer in GTP hydrolysis."; RL Cell 96:893-902(1999). RN [32] {ECO:0007744|PDB:1RE0} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-181 IN COMPLEX WITH GDP; RP BREFELDIN AND YEAST GEA1. RX PubMed=14690595; DOI=10.1016/s1097-2765(03)00475-1; RA Mossessova E., Corpina R.A., Goldberg J.; RT "Crystal structure of ARF1*Sec7 complexed with brefeldin A and its RT implications for the guanine nucleotide exchange mechanism."; RL Mol. Cell 12:1403-1411(2003). RN [33] {ECO:0007744|PDB:1U81} RP STRUCTURE BY NMR OF 18-181 IN COMPLEX WITH GDP. RX PubMed=15308674; DOI=10.1074/jbc.m402109200; RA Seidel R.D., Amor J.C., Kahn R.A., Prestegard J.H.; RT "Conformational changes in human Arf1 on nucleotide exchange and deletion RT of membrane-binding elements."; RL J. Biol. Chem. 279:48307-48318(2004). RN [34] {ECO:0007744|PDB:3O47} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 11-181 IN COMPLEX WITH GDP. RG Structural genomics consortium (SGC).; RT "Crystal structure of ARFGAP1-ARF1 fusion protein."; RL Submitted (JUL-2010) to the PDB data bank. CC -!- FUNCTION: Small GTPase involved in protein trafficking between CC different compartments (PubMed:8253837). Modulates vesicle budding and CC uncoating within the Golgi complex (PubMed:8253837). In its GTP-bound CC form, triggers the recruitment of coatomer proteins to the Golgi CC membrane (PubMed:8253837). The hydrolysis of ARF1-bound GTP, which is CC mediated by ARFGAPs proteins, is required for dissociation of coat CC proteins from Golgi membranes and vesicles (PubMed:8253837). The GTP- CC bound form interacts with PICK1 to limit PICK1-mediated inhibition of CC Arp2/3 complex activity; the function is linked to AMPA receptor CC (AMPAR) trafficking, regulation of synaptic plasticity of excitatory CC synapses and spine shrinkage during long-term depression (LTD) (By CC similarity). Plays a key role in the regulation of intestinal stem CC cells and gut microbiota, and is essential for maintaining intestinal CC homeostasis (By similarity). Also plays a critical role in mast cell CC expansion but not in mast cell maturation by facilitating optimal CC mTORC1 activation (By similarity). {ECO:0000250|UniProtKB:P84079, CC ECO:0000269|PubMed:8253837}. CC -!- FUNCTION: (Microbial infection) Functions as an allosteric activator of CC the cholera toxin catalytic subunit, an ADP-ribosyltransferase. CC {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; CC Evidence={ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10102276, CC ECO:0000269|PubMed:15107860, ECO:0000269|PubMed:8253837}; CC -!- ACTIVITY REGULATION: Alternates between an inactive GDP-bound form and CC an active GTP-bound form (PubMed:10022920, PubMed:10102276, CC PubMed:15107860). Intrinsic GTPase activity is almost undetectable in CC vitro (PubMed:10022920, PubMed:15107860). Activated by guanine CC nucleotide-exchange factors (GEFs) and inactivated by GTPase-activating CC proteins (GAPs) (PubMed:10022920, PubMed:10102276, PubMed:15107860). CC {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10102276, CC ECO:0000269|PubMed:15107860}. CC -!- SUBUNIT: Interacts (when activated) with GGA1, GGA2 and GGA3; the CC interaction is required for proper subcellular location of GGA1, GGA2 CC and GGA3 (PubMed:11950392, PubMed:28868155). Interacts with ARHGAP21, CC ASAP2, HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2 CC (PubMed:10022920, PubMed:17347647, PubMed:23889934, PubMed:8861955). CC Interacts with ARFGAP1, which hydrolyzes GTP and thus, regulates its CC function (PubMed:10102276). Interacts with PI4KB in the Golgi complex CC (PubMed:17555535). Interacts with NCS1/FREQ in the Golgi and at the CC plasma membrane (PubMed:17555535). Interacts with PLEKHA3 CC (PubMed:21454700). Interacts with PLEKHA8; the interaction, together CC with phosphatidylinositol 4-phosphate binding, is required for FAPP2- CC mediated glucosylceramide transfer activity (PubMed:15107860). CC Interacts (activated) with PICK1 (via PDZ domain); the interaction CC blocks Arp2/3 complex inhibition (PubMed:23889934). Interacts with CC IQSEC1 (PubMed:24058294). Interacts with C9orf72 (By similarity) CC (PubMed:24058294). {ECO:0000250|UniProtKB:P84078, CC ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10102276, CC ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:15107860, CC ECO:0000269|PubMed:17347647, ECO:0000269|PubMed:17555535, CC ECO:0000269|PubMed:21454700, ECO:0000269|PubMed:23889934, CC ECO:0000269|PubMed:24058294, ECO:0000269|PubMed:28868155, CC ECO:0000269|PubMed:8861955}. CC -!- INTERACTION: CC P84077; P53367: ARFIP1; NbExp=2; IntAct=EBI-447171, EBI-2808808; CC P84077; P53365: ARFIP2; NbExp=3; IntAct=EBI-447171, EBI-638194; CC P84077; Q99418: CYTH2; NbExp=5; IntAct=EBI-447171, EBI-448974; CC P84077; P46940: IQGAP1; NbExp=4; IntAct=EBI-447171, EBI-297509; CC P84077; O60271-2: SPAG9; NbExp=3; IntAct=EBI-447171, EBI-21502566; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:17555535}; Lipid-anchor CC {ECO:0000269|PubMed:17555535}; Cytoplasmic side {ECO:0000305}. Synapse, CC synaptosome {ECO:0000250|UniProtKB:P84079}. Postsynaptic density CC {ECO:0000250|UniProtKB:P84079}. Note=In the GDP-bound form, associates CC transiently with the membranes via its myristoylated N-terminus where CC guanine nucleotide-exchange factor (GEF)-mediated nucleotide exchange CC occurs (By similarity). Following nucleotide exchange, the GTP-bound CC form undergoes a conformational change, leading to the exposure of a CC myristoylated N-terminal amphipathic helix that provides stable CC membrane anchorage (By similarity). {ECO:0000250|UniProtKB:P84080}. CC -!- PTM: (Microbial infection) Demyristoylated by S.flexneri cysteine CC protease IpaJ which cleaves the peptide bond between N-myristoylated CC Gly-2 and Asn-3. {ECO:0000269|PubMed:20213681, CC ECO:0000269|PubMed:23535599}. CC -!- DISEASE: Periventricular nodular heterotopia 8 (PVNH8) [MIM:618185]: A CC form of periventricular nodular heterotopia, a disorder resulting from CC a defect in the pattern of neuronal migration in which ectopic CC collections of neurons lie along the lateral ventricles of the brain or CC just beneath, contiguously or in isolated patches. PVNH8 is an CC autosomal dominant disease characterized by developmental disabilities, CC speech delay, seizures and attention deficit-hyperactivity disorder. CC {ECO:0000269|PubMed:28868155}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M36340; AAA35552.1; -; mRNA. DR EMBL; M84326; AAA35512.1; -; mRNA. DR EMBL; AF052179; AAC28623.1; -; mRNA. DR EMBL; AF055002; AAC09356.1; -; mRNA. DR EMBL; AF493881; AAM12595.1; -; mRNA. DR EMBL; BT007393; AAP36057.1; -; mRNA. DR EMBL; AL136379; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009247; AAH09247.1; -; mRNA. DR EMBL; BC010429; AAH10429.1; -; mRNA. DR EMBL; BC011358; AAH11358.1; -; mRNA. DR EMBL; M84332; AAA35511.1; -; Genomic_DNA. DR CCDS; CCDS1565.1; -. DR PIR; B40187; A33283. DR RefSeq; NP_001019397.1; NM_001024226.2. DR RefSeq; NP_001019398.1; NM_001024227.1. DR RefSeq; NP_001019399.1; NM_001024228.2. DR RefSeq; NP_001649.1; NM_001658.4. DR PDB; 1HUR; X-ray; 2.00 A; A/B=2-181. DR PDB; 1RE0; X-ray; 2.40 A; A=18-181. DR PDB; 1U81; NMR; -; A=18-181. DR PDB; 3O47; X-ray; 2.80 A; A/B=11-181. DR PDB; 4HMY; X-ray; 7.00 A; C=17-181. DR PDB; 6CM9; EM; 3.73 A; C/H=17-181. DR PDB; 6CRI; EM; 6.80 A; C/H/K/L/U/V=17-181. DR PDB; 6D83; EM; 4.27 A; C/H=17-181. DR PDB; 6D84; EM; 6.72 A; C/H/I/N=17-181. DR PDB; 6DFF; EM; 3.90 A; C/H=17-181. DR PDB; 6FAE; X-ray; 2.35 A; B=18-181. DR PDB; 7DN8; X-ray; 2.61 A; B/D/F/H=17-181. DR PDB; 7DN9; X-ray; 3.29 A; B/D/F/H=17-181. DR PDB; 7MGE; EM; 3.94 A; E=17-180. DR PDB; 7R4H; EM; 2.34 A; C/H=17-181. DR PDB; 7UX3; EM; 9.60 A; C/H=2-181. DR PDB; 8D4C; EM; 9.30 A; C/D/F/H=2-181. DR PDB; 8D4D; EM; 9.60 A; C/D/F/H=2-181. DR PDB; 8D4E; EM; 9.20 A; C/H/Z=2-181. DR PDB; 8D4F; EM; 9.80 A; C/D/F/H/Q/Z=2-181. DR PDB; 8D4G; EM; 11.60 A; C/D/F/H/Q/Z=1-181. DR PDB; 8D9R; EM; 20.00 A; 3/4/5/6/7/C/H/J/K/O/P/Q/X/Z/a/b/c/d=2-181. DR PDB; 8D9S; EM; 20.00 A; 3/4/5/6/7/C/H/J/K/O/P/Q/X/Z/a/b/c/d=2-181. DR PDB; 8D9U; EM; 20.00 A; C/H/J/K/O/P/Q/X/Z/a/b/c=2-181. DR PDB; 8D9W; EM; 9.30 A; F/I=2-181. DR PDB; 8SDW; X-ray; 1.75 A; A=1-181. DR PDB; 9C58; EM; 4.70 A; A=2-181. DR PDB; 9C59; EM; 4.30 A; A/C/a/c=2-181. DR PDB; 9C5A; EM; 4.20 A; C/c=2-181. DR PDB; 9C5B; EM; 4.50 A; A/C=2-181. DR PDBsum; 1HUR; -. DR PDBsum; 1RE0; -. DR PDBsum; 1U81; -. DR PDBsum; 3O47; -. DR PDBsum; 4HMY; -. DR PDBsum; 6CM9; -. DR PDBsum; 6CRI; -. DR PDBsum; 6D83; -. DR PDBsum; 6D84; -. DR PDBsum; 6DFF; -. DR PDBsum; 6FAE; -. DR PDBsum; 7DN8; -. DR PDBsum; 7DN9; -. DR PDBsum; 7MGE; -. DR PDBsum; 7R4H; -. DR PDBsum; 7UX3; -. DR PDBsum; 8D4C; -. DR PDBsum; 8D4D; -. DR PDBsum; 8D4E; -. DR PDBsum; 8D4F; -. DR PDBsum; 8D4G; -. DR PDBsum; 8D9R; -. DR PDBsum; 8D9S; -. DR PDBsum; 8D9U; -. DR PDBsum; 8D9W; -. DR PDBsum; 8SDW; -. DR PDBsum; 9C58; -. DR PDBsum; 9C59; -. DR PDBsum; 9C5A; -. DR PDBsum; 9C5B; -. DR AlphaFoldDB; P84077; -. DR BMRB; P84077; -. DR EMDB; EMD-14312; -. DR EMDB; EMD-23827; -. DR EMDB; EMD-26853; -. DR EMDB; EMD-27181; -. DR EMDB; EMD-27182; -. DR EMDB; EMD-27183; -. DR EMDB; EMD-27184; -. DR EMDB; EMD-27185; -. DR EMDB; EMD-45207; -. DR EMDB; EMD-45208; -. DR EMDB; EMD-45209; -. DR EMDB; EMD-45210; -. DR EMDB; EMD-45211; -. DR EMDB; EMD-45212; -. DR EMDB; EMD-45213; -. DR EMDB; EMD-7563; -. DR SMR; P84077; -. DR BioGRID; 106870; 290. DR CORUM; P84077; -. DR DIP; DIP-31597N; -. DR ELM; P84077; -. DR FunCoup; P84077; 3004. DR IntAct; P84077; 80. DR MINT; P84077; -. DR STRING; 9606.ENSP00000440005; -. DR BindingDB; P84077; -. DR ChEMBL; CHEMBL5985; -. DR DrugBank; DB02774; 1,3-Propanediol. DR DrugBank; DB07348; Brefeldin A. DR DrugBank; DB09093; Chlortetracycline. DR DrugBank; DB09462; Glycerin. DR DrugBank; DB04121; Guanosine-3'-monophosphate-5'-diphosphate. DR DrugBank; DB04315; Guanosine-5'-Diphosphate. DR DrugBank; DB04137; Guanosine-5'-Triphosphate. DR DrugBank; DB08231; Myristic acid. DR GlyGen; P84077; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P84077; -. DR MetOSite; P84077; -. DR PhosphoSitePlus; P84077; -. DR SwissPalm; P84077; -. DR BioMuta; ARF1; -. DR DMDM; 51316985; -. DR jPOST; P84077; -. DR MassIVE; P84077; -. DR PaxDb; 9606-ENSP00000440005; -. DR PeptideAtlas; P84077; -. DR PRIDE; P84077; -. DR ProteomicsDB; 57747; -. DR Pumba; P84077; -. DR TopDownProteomics; P84077; -. DR Antibodypedia; 3569; 603 antibodies from 37 providers. DR DNASU; 375; -. DR Ensembl; ENST00000272102.10; ENSP00000272102.5; ENSG00000143761.18. DR Ensembl; ENST00000470558.5; ENSP00000514654.1; ENSG00000143761.18. DR Ensembl; ENST00000478336.5; ENSP00000514657.1; ENSG00000143761.18. DR Ensembl; ENST00000478424.5; ENSP00000514653.1; ENSG00000143761.18. DR GeneID; 375; -. DR KEGG; hsa:375; -. DR MANE-Select; ENST00000272102.10; ENSP00000272102.5; NM_001658.4; NP_001649.1. DR UCSC; uc001hrr.4; human. DR AGR; HGNC:652; -. DR ClinPGx; PA24934; -. DR CTD; 375; -. DR DisGeNET; 375; -. DR GeneCards; ARF1; -. DR HGNC; HGNC:652; ARF1. DR HPA; ENSG00000143761; Low tissue specificity. DR MalaCards; ARF1; -. DR MIM; 103180; gene. DR MIM; 618185; phenotype. DR OpenTargets; ENSG00000143761; -. DR Orphanet; 98892; Periventricular nodular heterotopia. DR VEuPathDB; HostDB:ENSG00000143761; -. DR eggNOG; KOG0070; Eukaryota. DR GeneTree; ENSGT00950000183080; -. DR HOGENOM; CLU_040729_9_3_1; -. DR InParanoid; P84077; -. DR OMA; LCYNGHI; -. DR OrthoDB; 2011769at2759; -. DR PAN-GO; P84077; 5 GO annotations based on evolutionary models. DR PhylomeDB; P84077; -. DR PathwayCommons; P84077; -. DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane. DR Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane. DR Reactome; R-HSA-167590; Nef Mediated CD4 Down-regulation. DR Reactome; R-HSA-199992; trans-Golgi Network Vesicle Budding. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-6811438; Intra-Golgi traffic. DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR Reactome; R-HSA-9845576; Glycosphingolipid transport. DR SignaLink; P84077; -. DR SIGNOR; P84077; -. DR Agora; ENSG00000143761; -. DR BioGRID-ORCS; 375; 213 hits in 1177 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ARF1; human. DR EvolutionaryTrace; P84077; -. DR GeneWiki; ARF1; -. DR GenomeRNAi; 375; -. DR Pharos; P84077; Tchem. DR PRO; PR:P84077; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P84077; protein. DR Bgee; ENSG00000143761; Expressed in adult organism and 210 other cell types or tissues. DR ExpressionAtlas; P84077; baseline and differential. DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell. DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA. DR GO; GO:0030017; C:sarcomere; IEA:Ensembl. DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IDA:MGI. DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IMP:CAFA. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB. DR GO; GO:0097061; P:dendritic spine organization; ISS:UniProtKB. DR GO; GO:0006878; P:intracellular copper ion homeostasis; IMP:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0060292; P:long-term synaptic depression; ISS:UniProtKB. DR GO; GO:1990386; P:mitotic cleavage furrow ingression; IEA:Ensembl. DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB. DR GO; GO:0002090; P:regulation of receptor internalization; ISS:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central. DR CDD; cd04150; Arf1_5_like; 1. DR FunFam; 3.40.50.300:FF:003500; ADP-ribosylation factor 1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR045872; Arf1-5-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR024156; Small_GTPase_ARF. DR InterPro; IPR006689; Small_GTPase_ARF/SAR. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00178; SAR; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51417; ARF; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant; KW ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein; KW Membrane; Myristate; Nucleotide-binding; Protein transport; KW Proteomics identification; Reference proteome; Synapse; Synaptosome; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:25255805, FT ECO:0000269|PubMed:25807930, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..181 FT /note="ADP-ribosylation factor 1" FT /id="PRO_0000207378" FT REGION 3..16 FT /note="Important for the stable binding to the membranes" FT /evidence="ECO:0000250|UniProtKB:P84080" FT BINDING 24..32 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:7990966, FT ECO:0007744|PDB:1HUR" FT BINDING 126..129 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:14690595, FT ECO:0000269|PubMed:15308674, ECO:0000269|PubMed:7990966, FT ECO:0000269|Ref.34, ECO:0007744|PDB:1HUR, FT ECO:0007744|PDB:1RE0, ECO:0007744|PDB:1U81, FT ECO:0007744|PDB:3O47" FT BINDING 160 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:15308674, FT ECO:0000269|PubMed:7990966, ECO:0000269|Ref.34, FT ECO:0007744|PDB:1HUR, ECO:0007744|PDB:1RE0, FT ECO:0007744|PDB:3O47" FT MOD_RES 2 FT /note="N-acetylglycine; alternate" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT LIPID 2 FT /note="N-myristoyl glycine; alternate" FT /evidence="ECO:0000269|PubMed:20213681, FT ECO:0000269|PubMed:23535599, ECO:0000269|PubMed:25255805, FT ECO:0000269|PubMed:25807930" FT VARIANT 35 FT /note="Y -> H (in PVNH8; decreased interaction with GGA3; FT dbSNP:rs879036238)" FT /evidence="ECO:0000269|PubMed:28868155" FT /id="VAR_081272" FT VARIANT 99 FT /note="R -> H (in PVNH8; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28868155" FT /id="VAR_081273" FT VARIANT 127 FT /note="K -> E (in PVNH8)" FT /evidence="ECO:0000269|PubMed:28868155" FT /id="VAR_081274" FT MUTAGEN 71 FT /note="Q->L: Inhibits GTP hydrolysis. Coatomer proteins FT recruitment to the Golgi membrane and formation of coated FT vesicles are normal. However, Golgi transport is severely FT reduced due to impaired vesicle uncoating." FT /evidence="ECO:0000269|PubMed:8253837" FT TURN 8..11 FT /evidence="ECO:0007829|PDB:8SDW" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:1HUR" FT STRAND 18..25 FT /evidence="ECO:0007829|PDB:8SDW" FT HELIX 30..37 FT /evidence="ECO:0007829|PDB:8SDW" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:8SDW" FT STRAND 51..58 FT /evidence="ECO:0007829|PDB:8SDW" FT STRAND 61..67 FT /evidence="ECO:0007829|PDB:8SDW" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:7R4H" FT HELIX 76..83 FT /evidence="ECO:0007829|PDB:8SDW" FT STRAND 86..93 FT /evidence="ECO:0007829|PDB:8SDW" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:8SDW" FT HELIX 100..111 FT /evidence="ECO:0007829|PDB:8SDW" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:8SDW" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:8SDW" FT STRAND 131..134 FT /evidence="ECO:0007829|PDB:1U81" FT HELIX 136..143 FT /evidence="ECO:0007829|PDB:8SDW" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:8SDW" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:8SDW" FT TURN 160..163 FT /evidence="ECO:0007829|PDB:8SDW" FT HELIX 166..178 FT /evidence="ECO:0007829|PDB:8SDW" SQ SEQUENCE 181 AA; 20697 MW; AAC773D4A60186B6 CRC64; MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K //