ARF2_YEAST
ID ARF2_YEAST Reviewed; 181 AA.
AC P19146; A2TBP3; D6VRL1;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=ADP-ribosylation factor 2;
GN Name=ARF2; OrderedLocusNames=YDL137W; ORFNames=D2165;
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=2123295; DOI=10.1128/mcb.10.12.6690-6699.1990;
RA Stearns T., Kahn R.A., Botstein D., Hoyt M.A.;
RT "ADP ribosylation factor is an essential protein in Saccharomyces
RT cerevisiae and is encoded by two genes.";
RL Mol. Cell. Biol. 10:6690-6699(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972577;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1549::aid-yea42>3.0.co;2-s;
RA Woelfl S., Haneman V., Saluz H.P.;
RT "Analysis of a 26,756 bp segment from the left arm of yeast chromosome
RT IV.";
RL Yeast 12:1549-1554(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-54.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH GDP.
RX PubMed=11535602; DOI=10.1074/jbc.m106660200;
RA Amor J.C., Horton J.R., Zhu X., Wang Y., Sullards C., Ringe D., Cheng X.,
RA Kahn R.A.;
RT "Structures of yeast ARF2 and ARL1: distinct roles for the N-terminus in
RT the structure and function of ARF family GTPases.";
RL J. Biol. Chem. 276:42477-42484(2001).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus.
CC -!- INTERACTION:
CC P19146; P11076: ARF1; NbExp=4; IntAct=EBI-2820, EBI-2816;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 25000 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; M35158; AAA34430.1; -; Genomic_DNA.
DR EMBL; X96876; CAA65622.1; -; Genomic_DNA.
DR EMBL; Z74185; CAA98710.1; -; Genomic_DNA.
DR EMBL; AY693030; AAT93049.1; -; Genomic_DNA.
DR EMBL; EF123146; ABM97490.1; -; mRNA.
DR EMBL; BK006938; DAA11721.1; -; Genomic_DNA.
DR PIR; A36367; A36367.
DR RefSeq; NP_010144.1; NM_001180197.1.
DR PDB; 1MR3; X-ray; 1.60 A; F=1-181.
DR PDBsum; 1MR3; -.
DR AlphaFoldDB; P19146; -.
DR SMR; P19146; -.
DR BioGRID; 31924; 108.
DR DIP; DIP-2215N; -.
DR IntAct; P19146; 24.
DR MINT; P19146; -.
DR STRING; 4932.YDL137W; -.
DR iPTMnet; P19146; -.
DR MaxQB; P19146; -.
DR PaxDb; P19146; -.
DR PRIDE; P19146; -.
DR TopDownProteomics; P19146; -.
DR EnsemblFungi; YDL137W_mRNA; YDL137W; YDL137W.
DR GeneID; 851418; -.
DR KEGG; sce:YDL137W; -.
DR SGD; S000002296; ARF2.
DR VEuPathDB; FungiDB:YDL137W; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000165468; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P19146; -.
DR OMA; VEYRNIQ; -.
DR BioCyc; YEAST:G3O-29536-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; P19146; -.
DR PRO; PR:P19146; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P19146; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
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: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 2"
FT /id="PRO_0000207419"
FT BINDING 25..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 160..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P11076"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:1MR3"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:1MR3"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:1MR3"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1MR3"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1MR3"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1MR3"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:1MR3"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1MR3"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1MR3"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1MR3"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1MR3"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1MR3"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1MR3"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1MR3"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1MR3"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1MR3"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:1MR3"
SQ SEQUENCE 181 AA; 20658 MW; 7E43FF792E8D64E8 CRC64;
MGLYASKLFS NLFGNKEMRI LMVGLDGAGK TTVLYKLKLG EVITTIPTIG FNVETVQYKN
ISFTVWDVGG QDRIRSLWRH YYRNTEGVIF VIDSNDRSRI GEAREVMQRM LNEDELRNAV
WLVFANKQDL PEAMSAAEIT EKLGLHSIRN RPWFIQSTCA TSGEGLYEGL EWLSNNLKNQ
S
