VPS52_YEAST
ID VPS52_YEAST Reviewed; 641 AA.
AC P39904; D6VTA7; Q03379;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Vacuolar protein sorting-associated protein 52;
DE AltName: Full=Suppressor of actin mutation protein 2;
GN Name=VPS52; Synonyms=SAC2; OrderedLocusNames=YDR484W; ORFNames=D8035.27;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7754710; DOI=10.1002/yea.320100909;
RA Koelling R., Lee A., Chen E.Y., Botstein D.;
RT "Nucleotide sequence of the SAC2 gene of Saccharomyces cerevisiae.";
RL Yeast 10:1211-1216(1994).
RN [2]
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 [3]
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 [4]
RP FUNCTION.
RX PubMed=2656401; DOI=10.1093/genetics/121.4.659;
RA Novick P., Osmond B.C., Botstein D.;
RT "Suppressors of yeast actin mutations.";
RL Genetics 121:659-674(1989).
RN [5]
RP FUNCTION, AND INTERACTION WITH VPS53 AND VPS54.
RX PubMed=10637310; DOI=10.1091/mbc.11.1.305;
RA Conibear E., Stevens T.H.;
RT "Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for
RT protein sorting at the yeast late Golgi.";
RL Mol. Biol. Cell 11:305-323(2000).
RN [6]
RP FUNCTION, AND INTERACTION WITH TLG1 AND YPT6.
RX PubMed=11689439; DOI=10.1093/emboj/20.21.5991;
RA Siniossoglou S., Pelham H.R.B.;
RT "An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion
RT of vesicles with late Golgi membranes.";
RL EMBO J. 20:5991-5998(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS51; VSP53 AND
RP VSP54.
RX PubMed=12377769; DOI=10.1074/jbc.m209428200;
RA Siniossoglou S., Pelham H.R.B.;
RT "Vps51p links the VFT complex to the SNARE Tlg1p.";
RL J. Biol. Chem. 277:48318-48324(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH VPS51; VPS53; VPS54 AND TGL1.
RX PubMed=12446664; DOI=10.1074/jbc.m210436200;
RA Reggiori F., Wang C.-W., Stromhaug P.E., Shintani T., Klionsky D.J.;
RT "Vps51 is part of the yeast Vps fifty-three tethering complex essential for
RT retrograde traffic from the early endosome and Cvt vesicle completion.";
RL J. Biol. Chem. 278:5009-5020(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH VPS51; VPS53; VPS54 AND TGL1.
RX PubMed=12686613; DOI=10.1091/mbc.e02-10-0654;
RA Conibear E., Cleck J.N., Stevens T.H.;
RT "Vps51p mediates the association of the GARP (Vps52/53/54) complex with the
RT late Golgi t-SNARE Tlg1p.";
RL Mol. Biol. Cell 14:1610-1623(2003).
RN [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in retrograde transport from early and late
CC endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1
CC to the Golgi, leading to the membrane fusion between late Golgi and
CC endosomal vesicles. May also be involved in the actin cytoskeleton
CC organization. {ECO:0000269|PubMed:10637310,
CC ECO:0000269|PubMed:11689439, ECO:0000269|PubMed:12377769,
CC ECO:0000269|PubMed:12446664, ECO:0000269|PubMed:12686613,
CC ECO:0000269|PubMed:2656401}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex, also called VFT (VPS fifty-three) complex, composed of VPS51,
CC VPS52, VPS53 and VPS54. Interacts also with TLG1 and YPT6.
CC {ECO:0000269|PubMed:10637310, ECO:0000269|PubMed:11689439,
CC ECO:0000269|PubMed:12377769, ECO:0000269|PubMed:12446664,
CC ECO:0000269|PubMed:12686613}.
CC -!- INTERACTION:
CC P39904; P36116: VPS51; NbExp=5; IntAct=EBI-16418, EBI-26352;
CC P39904; P47061: VPS53; NbExp=7; IntAct=EBI-16418, EBI-25828;
CC P39904; Q12071: VPS54; NbExp=8; IntAct=EBI-16418, EBI-36751;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane;
CC Peripheral membrane protein. Endosome membrane; Peripheral membrane
CC protein. Cytoplasm, cytoskeleton.
CC -!- MISCELLANEOUS: Present with 3130 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS52 family. {ECO:0000305}.
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DR EMBL; Z29988; CAA82878.1; -; Genomic_DNA.
DR EMBL; U33050; AAB64912.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12317.1; -; Genomic_DNA.
DR PIR; S69651; S69651.
DR RefSeq; NP_010772.1; NM_001180792.1.
DR AlphaFoldDB; P39904; -.
DR BioGRID; 32536; 427.
DR ComplexPortal; CPX-1718; GARP complex.
DR DIP; DIP-3967N; -.
DR IntAct; P39904; 11.
DR MINT; P39904; -.
DR STRING; 4932.YDR484W; -.
DR iPTMnet; P39904; -.
DR MaxQB; P39904; -.
DR PaxDb; P39904; -.
DR PRIDE; P39904; -.
DR EnsemblFungi; YDR484W_mRNA; YDR484W; YDR484W.
DR GeneID; 852095; -.
DR KEGG; sce:YDR484W; -.
DR SGD; S000002892; VPS52.
DR VEuPathDB; FungiDB:YDR484W; -.
DR eggNOG; KOG1961; Eukaryota.
DR GeneTree; ENSGT00390000008815; -.
DR HOGENOM; CLU_010797_1_0_1; -.
DR InParanoid; P39904; -.
DR OMA; IRTSMTT; -.
DR BioCyc; YEAST:G3O-30009-MON; -.
DR PRO; PR:P39904; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39904; protein.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000938; C:GARP complex; IPI:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0030029; P:actin filament-based process; IMP:SGD.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; IMP:SGD.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IDA:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:SGD.
DR InterPro; IPR007258; Vps52.
DR PANTHER; PTHR14190; PTHR14190; 1.
DR Pfam; PF04129; Vps52; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Endosome; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..641
FT /note="Vacuolar protein sorting-associated protein 52"
FT /id="PRO_0000213318"
FT COILED 81..110
FT /evidence="ECO:0000255"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 204..209
FT /note="KRLIIS -> EKTYYF (in Ref. 1; CAA82878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 74333 MW; F2BF669A72A712C1 CRC64;
MDVLKEVLSL DQDKFDQLKE TSRDKTNETD DPFENYLKDC KFKAPSNKDQ SPFAKLKSLQ
ETHSNNEAAI NIIIPQLIDY LTEFTNRLSN YTQDLDFIKK KSNELQSLLE YNSTKLAHIS
PMVNDLMIPP ELIDDIIKGK INESWQDNIT FIADKEEIYN KYRSNNLDQD NKDAENSAML
APKDFDKLCQ LLDILKNVIL ERSKRLIISK IKTLRSHNPV PSQRIQNKLL KVQKIFPFIR
DNNLSLALEL RQAYCYTMKW YYREYFSRYI RSLTILQFQQ IDSQFALGNG LSTTSVSGFN
NSPSLFFSNY LTTSASNAFY NKLPVTDEKI DKYFQIKKRL NILTQEDNTV MVSQIAENNT
TKNYIEIGFK NLNLAILDNC TVEYHFLKDF FAMNGDNFEE INGLLEQIFQ PTFDEATTYT
QQLIQYNYDI FGVLISIRVA NQLQFESERR GIPSMFDSFL NGQLIQLWPR FQQLVDFQCE
SLRKAAITTN VAKYAGNSST SNSSPLTSPH ELTVQFGKFL SSFLTLAITH KQSIDERSEP
LYNSIIRLRN DFETVMTKCS KKTKSPERFL ATNYMYLYNN LQQLHLHLNI NDSDAQNYNF
DSAENVGTKV ANDDDNDSSV PLIIRETENH FKTLVEAFTR N
