ARF3_YEAST
ID ARF3_YEAST Reviewed; 183 AA.
AC P40994; D6W2F5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=ADP-ribosylation factor 3;
GN Name=ARF3; OrderedLocusNames=YOR094W; ORFNames=YOR3172W;
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 [MRNA].
RX PubMed=8063710; DOI=10.1016/s0021-9258(17)31911-7;
RA Lee F.-J.S., Stevens L.A., Kao Y.L., Moss J., Vaughan M.;
RT "Characterization of a glucose-repressible ADP-ribosylation factor 3 (ARF3)
RT from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:20931-20937(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [7]
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).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus.
CC -!- SUBUNIT: Interacts with RUD3. {ECO:0000269|PubMed:15504911}.
CC -!- INTERACTION:
CC P40994; P25369: LSB5; NbExp=2; IntAct=EBI-2824, EBI-10218;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; L28996; AAA61614.1; -; mRNA.
DR EMBL; X94335; CAA64016.1; -; Genomic_DNA.
DR EMBL; Z75002; CAA99291.1; -; Genomic_DNA.
DR EMBL; AY557751; AAS56077.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10871.1; -; Genomic_DNA.
DR PIR; A53917; A53917.
DR RefSeq; NP_014737.1; NM_001183513.1.
DR AlphaFoldDB; P40994; -.
DR SMR; P40994; -.
DR BioGRID; 34492; 121.
DR IntAct; P40994; 9.
DR MINT; P40994; -.
DR STRING; 4932.YOR094W; -.
DR MaxQB; P40994; -.
DR PaxDb; P40994; -.
DR PRIDE; P40994; -.
DR EnsemblFungi; YOR094W_mRNA; YOR094W; YOR094W.
DR GeneID; 854261; -.
DR KEGG; sce:YOR094W; -.
DR SGD; S000005620; ARF3.
DR VEuPathDB; FungiDB:YOR094W; -.
DR eggNOG; KOG0071; Eukaryota.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P40994; -.
DR OMA; WSVIPTI; -.
DR BioCyc; YEAST:G3O-33628-MON; -.
DR PRO; PR:P40994; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P40994; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0008047; F:enzyme activator activity; IMP:SGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IGI:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IMP:SGD.
DR GO; GO:0036267; P:invasive filamentous growth; IMP:SGD.
DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04149; Arf6; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041838; Arf6.
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 ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Myristate;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..183
FT /note="ADP-ribosylation factor 3"
FT /id="PRO_0000207420"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
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 /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 183 AA; 20696 MW; B015ABAF8324962D CRC64;
MGNSISKVLG KLFGSKEMKI LMLGLDKAGK TTILYKLKLN KIKTSTPTVG FNVETVTYKN
VKFNMWDVGG QQRLRPLWRH YFPATTALIF VIDSSARNRM EEAKEELYSI IGEKEMENVV
LLVWANKQDL KDAMKPQEVS DFLELEKNLK NQPWCVIGSN ALSGQGLVEG LSWISNNTNV
PKK
