ARF1_HUMAN
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 03-AUG-2022, entry version 193.
DE RecName: Full=ADP-ribosylation factor 1;
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 INTERACTION WITH HERC1.
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 [11]
RP 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 [12]
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 [13]
RP 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 [14]
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 [15]
RP INTERACTION WITH PI4KB AND NCS1, AND SUBCELLULAR LOCATION.
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RAT ARFGAP1
RP CATALYTIC DOMAIN.
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 [31]
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 [32]
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 [33]
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: GTP-binding protein involved in protein trafficking among
CC different compartments. Modulates vesicle budding and uncoating within
CC the Golgi complex. Deactivation induces the redistribution of the
CC entire Golgi complex to the endoplasmic reticulum, suggesting a crucial
CC role in protein trafficking. In its GTP-bound form, its triggers the
CC association with coat proteins with the Golgi membrane. The hydrolysis
CC of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required
CC for dissociation of coat proteins from Golgi membranes and vesicles.
CC The GTP-bound form interacts with PICK1 to limit PICK1-mediated
CC inhibition of Arp2/3 complex activity; the function is linked to AMPA
CC receptor (AMPAR) trafficking, regulation of synaptic plasicity of
CC excitatory synapses and spine shrinkage during long-term depression
CC (LTD).
CC -!- FUNCTION: (Microbial infection) Functions as an allosteric activator of
CC the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
CC {ECO:0000305}.
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; Q99418: CYTH2; NbExp=5; IntAct=EBI-447171, EBI-448974;
CC P84077; O60271: SPAG9; NbExp=3; IntAct=EBI-447171, EBI-1023301;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17555535}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}. Synapse,
CC synaptosome {ECO:0000250}. Postsynaptic density {ECO:0000250}. Membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250|UniProtKB:P84078}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P84078}.
CC -!- PTM: Demyristoylated by S.flexneri cysteine protease IpaJ which cleaves
CC the peptide bond between N-myristoylated Gly-2 and Asn-3.
CC {ECO:0000269|PubMed:20213681, 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}.
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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_001024226.1.
DR RefSeq; NP_001019398.1; NM_001024227.1.
DR RefSeq; NP_001019399.1; NM_001024228.1.
DR RefSeq; NP_001649.1; NM_001658.3.
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 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 AlphaFoldDB; P84077; -.
DR BMRB; P84077; -.
DR SMR; P84077; -.
DR BioGRID; 106870; 223.
DR CORUM; P84077; -.
DR DIP; DIP-31597N; -.
DR ELM; P84077; -.
DR IntAct; P84077; 63.
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; 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 iPTMnet; P84077; -.
DR MetOSite; P84077; -.
DR PhosphoSitePlus; P84077; -.
DR SwissPalm; P84077; -.
DR BioMuta; ARF1; -.
DR DMDM; 51316985; -.
DR EPD; P84077; -.
DR jPOST; P84077; -.
DR MassIVE; P84077; -.
DR MaxQB; P84077; -.
DR PaxDb; P84077; -.
DR PeptideAtlas; P84077; -.
DR PRIDE; P84077; -.
DR ProteomicsDB; 57747; -.
DR TopDownProteomics; P84077; -.
DR Antibodypedia; 3569; 584 antibodies from 38 providers.
DR DNASU; 375; -.
DR Ensembl; ENST00000272102.10; ENSP00000272102.5; ENSG00000143761.16.
DR Ensembl; ENST00000540651.5; ENSP00000442980.1; ENSG00000143761.16.
DR Ensembl; ENST00000541182.1; ENSP00000440005.1; ENSG00000143761.16.
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 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 neXtProt; NX_P84077; -.
DR OpenTargets; ENSG00000143761; -.
DR Orphanet; 98892; Periventricular nodular heterotopia.
DR PharmGKB; PA24934; -.
DR VEuPathDB; HostDB:ENSG00000143761; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00950000183080; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P84077; -.
DR OMA; RIWITTL; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P84077; -.
DR TreeFam; TF300808; -.
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 SignaLink; P84077; -.
DR SIGNOR; P84077; -.
DR BioGRID-ORCS; 375; 193 hits in 1096 CRISPR screens.
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 208 other tissues.
DR ExpressionAtlas; P84077; baseline and differential.
DR Genevisible; P84077; HS.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
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:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
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:0006878; P:cellular copper ion homeostasis; IMP: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: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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045872; Arf1-5-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Disease variant; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Protein transport;
KW Reference proteome; Synapse; Synaptosome; 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 BINDING 24..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305, ECO:0007744|PDB:1HUR"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305, 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: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; unknown pathological
FT 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 HELIX 6..9
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:1HUR"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6FAE"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1HUR"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1HUR"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6FAE"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1HUR"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1U81"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1HUR"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1HUR"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1HUR"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1HUR"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:1HUR"
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
