VPS64_YEAST
ID VPS64_YEAST Reviewed; 604 AA.
AC Q03944; D6VSI2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Vacuolar protein sorting-associated protein 64;
DE AltName: Full=Factor arrest protein 9;
GN Name=VPS64; Synonyms=FAR9; OrderedLocusNames=YDR200C; ORFNames=YD9346.10C;
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 [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 [2]
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 [3]
RP FUNCTION.
RX PubMed=12134085; DOI=10.1091/mbc.02-01-0005;
RA Bonangelino C.J., Chavez E.M., Bonifacino J.S.;
RT "Genomic screen for vacuolar protein sorting genes in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:2486-2501(2002).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12514182; DOI=10.1074/jbc.m212725200;
RA Beilharz T., Egan B., Silver P.A., Hofmann K., Lithgow T.;
RT "Bipartite signals mediate subcellular targeting of tail-anchored membrane
RT proteins in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:8219-8223(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH FAR3; FAR7; FAR8; FAR10 AND FAR11.
RX PubMed=12588993; DOI=10.1128/mcb.23.5.1750-1763.2003;
RA Kemp H.A., Sprague G.F. Jr.;
RT "Far3 and five interacting proteins prevent premature recovery from
RT pheromone arrest in the budding yeast Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 23:1750-1763(2003).
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY 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: Participates in the control of the reentry into the cell
CC cycle following pheromone treatment. Involved in vacuolar protein
CC sorting. {ECO:0000269|PubMed:12134085, ECO:0000269|PubMed:12588993}.
CC -!- SUBUNIT: Component of a complex at least composed of FAR3, FAR7, FAR8,
CC FAR10, FAR11 and VPS64.
CC -!- INTERACTION:
CC Q03944; P46671: FAR3; NbExp=5; IntAct=EBI-30418, EBI-6789;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type IV membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z48784; CAA88712.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12042.1; -; Genomic_DNA.
DR PIR; S52706; S52706.
DR RefSeq; NP_010486.3; NM_001180508.3.
DR PDB; 6A8W; X-ray; 1.84 A; A=160-295.
DR PDBsum; 6A8W; -.
DR AlphaFoldDB; Q03944; -.
DR SMR; Q03944; -.
DR BioGRID; 32251; 219.
DR ComplexPortal; CPX-1197; FAR complex.
DR DIP; DIP-1829N; -.
DR IntAct; Q03944; 29.
DR MINT; Q03944; -.
DR STRING; 4932.YDR200C; -.
DR iPTMnet; Q03944; -.
DR MaxQB; Q03944; -.
DR PaxDb; Q03944; -.
DR PRIDE; Q03944; -.
DR EnsemblFungi; YDR200C_mRNA; YDR200C; YDR200C.
DR GeneID; 851781; -.
DR KEGG; sce:YDR200C; -.
DR SGD; S000002608; VPS64.
DR VEuPathDB; FungiDB:YDR200C; -.
DR eggNOG; KOG3872; Eukaryota.
DR GeneTree; ENSGT00940000176673; -.
DR HOGENOM; CLU_031992_0_0_1; -.
DR InParanoid; Q03944; -.
DR OMA; RNHACLS; -.
DR BioCyc; YEAST:G3O-29785-MON; -.
DR PRO; PR:Q03944; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03944; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:SGD.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071444; P:cellular response to pheromone; IC:ComplexPortal.
DR GO; GO:0006623; P:protein targeting to vacuole; HMP:SGD.
DR GO; GO:0000321; P:re-entry into mitotic cell cycle after pheromone arrest; IGI:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IC:ComplexPortal.
DR GO; GO:0031929; P:TOR signaling; IGI:SGD.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Coiled coil; Endoplasmic reticulum; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..604
FT /note="Vacuolar protein sorting-associated protein 64"
FT /id="PRO_0000065907"
FT TOPO_DOM 1..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..598
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..604
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 185..257
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..563
FT /evidence="ECO:0000255"
FT COMPBIAS 17..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:6A8W"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6A8W"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6A8W"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:6A8W"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6A8W"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:6A8W"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6A8W"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:6A8W"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6A8W"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6A8W"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:6A8W"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:6A8W"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:6A8W"
SQ SEQUENCE 604 AA; 67284 MW; A22CEDD852FC421A CRC64;
MVELEKRRRP PPQLQHSPYV RDQSNSQGMT KTPETSPPKR PMGRARSNSR SSGSRSNVDI
DQYTIPPGLD LLPTASSPPS VHQVSQQQQL SPILANKIRS PFENQSQDQN DNSIDPTPAG
QVTIPVEAVS PPALDELSKF QNGSTETLFR TGSPRKKHTH IIILKSLNAT FETKFLVVPF
KPDGLKLGRP VTNSVNKNNS GSKRDLFSQQ VRPDNGNFDS RVLSRNHACL SCDPTSGKIY
IRDLKSSNGT FVNGVKIRQN DVELKVGDTV DLGTDIDSKF EHRKISAYVE EISVIPLMNT
VSDPTNLVMK KQDHTNKNNG NSTNINGIKI DRGHHNQHIP IRSHLKENYT EAGVTSATTA
QRAAFEAAMF GDINNSELDD DILGPETEVL SGIFINNSAG TSINLINMIK TLTTELSLEK
QELEKLHSMQ NFMQNYTINL DFINKHMIDM NEKHLLKLST ALQKTLSENN DALLKESEDQ
LKEIKQQNNK VKSACSLKEK QNHEKLQELE SELRELNLQI EEERGKNLVL TQSNFNGGIN
NDNNAKVKQN DSREEKKDTE DTLISTEELG VVEGKRTRVS KGMLFGVVAI SFGLVATAVK
QLPQ
