ARF1_YEAST
ID ARF1_YEAST Reviewed; 181 AA.
AC P11076; D6VRG1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=ADP-ribosylation factor 1;
GN Name=ARF1; OrderedLocusNames=YDL192W; ORFNames=D1244;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3133654; DOI=10.1073/pnas.85.13.4620;
RA Sewell J., Kahn R.A.;
RT "Sequences of the bovine and yeast ADP-ribosylation factor and comparison
RT to other GTP-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4620-4624(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896272;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1065::aid-yea995>3.0.co;2-f;
RA Verhasselt P., Voet M., Mathys J., Volckaert G.;
RT "The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast
RT chromosome IV reveals the location of five known genes and characterizes at
RT least six new open reading frames including putative genes for ribosomal
RT protein L35 and a sugar transport protein.";
RL Yeast 12:1065-1070(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP INTERACTION WITH RUD3.
RX PubMed=15504911; DOI=10.1083/jcb.200407088;
RA Gillingham A.K., Tong A.H.Y., Boone C., Munro S.;
RT "The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to
RT recruit the golgin Rud3p to the cis-Golgi.";
RL J. Cell Biol. 167:281-292(2004).
RN [7]
RP FUNCTION IN MRNA TRANSPORT, AND INTERACTION WITH ARF1.
RX PubMed=15356266; DOI=10.1091/mbc.e04-05-0411;
RA Trautwein M., Dengjel J., Schirle M., Spang A.;
RT "Arf1p provides an unexpected link between COPI vesicles and mRNA in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 15:5021-5037(2004).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [9]
RP STRUCTURE BY NMR OF 2-181 IN COMPLEX WITH GDP, AND MYRISTOYLATION AT GLY-2.
RX PubMed=19141284; DOI=10.1016/j.str.2008.10.020;
RA Liu Y., Kahn R.A., Prestegard J.H.;
RT "Structure and membrane interaction of myristoylated ARF1.";
RL Structure 17:79-87(2009).
RN [10]
RP STRUCTURE BY NMR OF 2-181 IN COMPLEX WITH GTP, AND MYRISTOYLATION AT GLY-2.
RX PubMed=20601958; DOI=10.1038/nsmb.1853;
RA Liu Y., Kahn R.A., Prestegard J.H.;
RT "Dynamic structure of membrane-anchored Arf*GTP.";
RL Nat. Struct. Mol. Biol. 17:876-881(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 18-181.
RX PubMed=22304919; DOI=10.1016/j.cell.2012.01.015;
RA Yu X., Breitman M., Goldberg J.;
RT "A structure-based mechanism for Arf1-dependent recruitment of coatomer to
RT membranes.";
RL Cell 148:530-542(2012).
RN [12]
RP FUNCTION, AND INTERACTION WITH VPS13.
RX PubMed=34830155; DOI=10.3390/ijms222212274;
RA Kolakowski D., Rzepnikowska W., Kaniak-Golik A., Zoladek T., Kaminska J.;
RT "The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi
RT Apparatus.";
RL Int. J. Mol. Sci. 22:12274-12274(2021).
CC -!- FUNCTION: GTP-binding protein involved in Golgi vesicle trafficking
CC (PubMed:15356266, PubMed:34830155). May modulate vesicle budding and
CC uncoating within the Golgi apparatus (PubMed:15356266). May recruit the
CC lipid transfer protein VPS13 to Golgi membranes (PubMed:34830155).
CC Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this
CC is required for correct localization of the asymmetrically distributed
CC ASH1 mRNA (PubMed:15356266). {ECO:0000269|PubMed:15356266,
CC ECO:0000269|PubMed:34830155}.
CC -!- SUBUNIT: Interacts with RUD3 (PubMed:15356266, PubMed:15504911,
CC PubMed:19141284, PubMed:20601958). Interacts with VPS13 (via C-terminal
CC part); the interaction is direct (PubMed:34830155).
CC {ECO:0000269|PubMed:15356266, ECO:0000269|PubMed:15504911,
CC ECO:0000269|PubMed:19141284, ECO:0000269|PubMed:20601958,
CC ECO:0000269|PubMed:34830155}.
CC -!- INTERACTION:
CC P11076; P19146: ARF2; NbExp=4; IntAct=EBI-2816, EBI-2820;
CC P11076; Q05029: BCH1; NbExp=3; IntAct=EBI-2816, EBI-27508;
CC P11076; P36122: BCH2; NbExp=2; IntAct=EBI-2816, EBI-26374;
CC P11076; Q08754: BUD7; NbExp=2; IntAct=EBI-2816, EBI-32770;
CC P11076; Q12114: CHS5; NbExp=5; IntAct=EBI-2816, EBI-4640;
CC P11076; P40955: CHS6; NbExp=3; IntAct=EBI-2816, EBI-4649;
CC P11076; P41909: PXA1; NbExp=2; IntAct=EBI-2816, EBI-14344;
CC P11076; P34230: PXA2; NbExp=2; IntAct=EBI-2816, EBI-2464632;
CC P11076; Q12234: RUD3; NbExp=5; IntAct=EBI-2816, EBI-31697;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC -!- MISCELLANEOUS: Present with 19300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; J03276; AAA34431.1; -; Genomic_DNA.
DR EMBL; X83276; CAA58255.1; -; Genomic_DNA.
DR EMBL; Z74240; CAA98769.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11671.1; -; Genomic_DNA.
DR PIR; B36167; B36167.
DR RefSeq; NP_010089.1; NM_001180252.1.
DR PDB; 2K5U; NMR; -; A=2-181.
DR PDB; 2KSQ; NMR; -; A=2-181.
DR PDB; 3TJZ; X-ray; 2.90 A; A/D=18-181.
DR PDB; 4Q66; X-ray; 3.35 A; C/F/I/L=18-181.
DR PDB; 5A1U; EM; 13.00 A; A/B=1-181.
DR PDB; 5A1V; EM; 21.00 A; A/B/I/J/R/S=1-181.
DR PDB; 5A1W; EM; 18.00 A; A/B=1-181.
DR PDB; 5A1X; EM; 23.00 A; A/B/I/J=1-181.
DR PDB; 5A1Y; EM; 21.00 A; A/B/I/J/R=1-181.
DR PDB; 5NZR; EM; 9.20 A; F/M/R=1-181.
DR PDB; 5NZS; EM; 10.10 A; F/M/R=1-181.
DR PDB; 5NZT; EM; 17.00 A; F/J/M/R=1-181.
DR PDB; 5NZU; EM; 15.00 A; F/M/R=1-181.
DR PDB; 5NZV; EM; 17.30 A; F/M/P/R/T=1-181.
DR PDBsum; 2K5U; -.
DR PDBsum; 2KSQ; -.
DR PDBsum; 3TJZ; -.
DR PDBsum; 4Q66; -.
DR PDBsum; 5A1U; -.
DR PDBsum; 5A1V; -.
DR PDBsum; 5A1W; -.
DR PDBsum; 5A1X; -.
DR PDBsum; 5A1Y; -.
DR PDBsum; 5NZR; -.
DR PDBsum; 5NZS; -.
DR PDBsum; 5NZT; -.
DR PDBsum; 5NZU; -.
DR PDBsum; 5NZV; -.
DR AlphaFoldDB; P11076; -.
DR BMRB; P11076; -.
DR SMR; P11076; -.
DR BioGRID; 31853; 387.
DR DIP; DIP-2213N; -.
DR IntAct; P11076; 63.
DR MINT; P11076; -.
DR STRING; 4932.YDL192W; -.
DR iPTMnet; P11076; -.
DR MaxQB; P11076; -.
DR PaxDb; P11076; -.
DR PRIDE; P11076; -.
DR TopDownProteomics; P11076; -.
DR EnsemblFungi; YDL192W_mRNA; YDL192W; YDL192W.
DR GeneID; 851335; -.
DR KEGG; sce:YDL192W; -.
DR SGD; S000002351; ARF1.
DR VEuPathDB; FungiDB:YDL192W; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000165468; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P11076; -.
DR OMA; LWRILNI; -.
DR BioCyc; YEAST:G3O-29577-MON; -.
DR Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-SCE-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-SCE-6811438; Intra-Golgi traffic.
DR EvolutionaryTrace; P11076; -.
DR PRO; PR:P11076; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P11076; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0005798; C:Golgi-associated vesicle; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IGI:SGD.
DR GO; GO:0048193; P:Golgi vesicle transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
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; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Isopeptide bond; Lipoprotein; Myristate; Nucleotide-binding;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..181
FT /note="ADP-ribosylation factor 1"
FT /id="PRO_0000207418"
FT BINDING 25..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20601958"
FT BINDING 48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20601958"
FT BINDING 70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20601958"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20601958"
FT BINDING 160..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20601958"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:19141284,
FT ECO:0000269|PubMed:20601958"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2K5U"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2KSQ"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2KSQ"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:3TJZ"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:2KSQ"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2K5U"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3TJZ"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3TJZ"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:3TJZ"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:3TJZ"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2KSQ"
SQ SEQUENCE 181 AA; 20529 MW; 796859026AC63CC0 CRC64;
MGLFASKLFS NLFGNKEMRI LMVGLDGAGK TTVLYKLKLG EVITTIPTIG FNVETVQYKN
ISFTVWDVGG QDRIRSLWRH YYRNTEGVIF VVDSNDRSRI GEAREVMQRM LNEDELRNAA
WLVFANKQDL PEAMSAAEIT EKLGLHSIRN RPWFIQATCA TSGEGLYEGL EWLSNSLKNS
T
