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Vacuolar protein sorting-associated protein 64 (Factor arrest protein 9)

 VPS64_YEAST             Reviewed;         604 AA.
Q03944; D6VSI2;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 141.
RecName: Full=Vacuolar protein sorting-associated protein 64;
AltName: Full=Factor arrest protein 9;
Name=VPS64; Synonyms=FAR9; OrderedLocusNames=YDR200C;
ORFNames=YD9346.10C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=12134085; DOI=10.1091/mbc.02-01-0005;
Bonangelino C.J., Chavez E.M., Bonifacino J.S.;
"Genomic screen for vacuolar protein sorting genes in Saccharomyces
cerevisiae.";
Mol. Biol. Cell 13:2486-2501(2002).
[4]
SUBCELLULAR LOCATION.
PubMed=12514182; DOI=10.1074/jbc.M212725200;
Beilharz T., Egan B., Silver P.A., Hofmann K., Lithgow T.;
"Bipartite signals mediate subcellular targeting of tail-anchored
membrane proteins in Saccharomyces cerevisiae.";
J. Biol. Chem. 278:8219-8223(2003).
[5]
FUNCTION, AND INTERACTION WITH FAR3; FAR7; FAR8; FAR10 AND FAR11.
PubMed=12588993; DOI=10.1128/MCB.23.5.1750-1763.2003;
Kemp H.A., Sprague G.F. Jr.;
"Far3 and five interacting proteins prevent premature recovery from
pheromone arrest in the budding yeast Saccharomyces cerevisiae.";
Mol. Cell. Biol. 23:1750-1763(2003).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Participates in the control of the reentry into the cell
cycle following pheromone treatment. Involved in vacuolar protein
sorting. {ECO:0000269|PubMed:12134085,
ECO:0000269|PubMed:12588993}.
-!- SUBUNIT: Component of a complex at least composed of FAR3, FAR7,
FAR8, FAR10, FAR11 and VPS64.
-!- INTERACTION:
P46671:FAR3; NbExp=5; IntAct=EBI-30418, EBI-6789;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
-!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; Z48784; CAA88712.1; -; Genomic_DNA.
EMBL; BK006938; DAA12042.1; -; Genomic_DNA.
PIR; S52706; S52706.
RefSeq; NP_010486.3; NM_001180508.3.
ProteinModelPortal; Q03944; -.
SMR; Q03944; -.
BioGrid; 32251; 216.
ComplexPortal; CPX-1197; FAR complex.
DIP; DIP-1829N; -.
IntAct; Q03944; 29.
MINT; Q03944; -.
STRING; 4932.YDR200C; -.
iPTMnet; Q03944; -.
MaxQB; Q03944; -.
PaxDb; Q03944; -.
PRIDE; Q03944; -.
EnsemblFungi; YDR200C; YDR200C; YDR200C.
GeneID; 851781; -.
KEGG; sce:YDR200C; -.
EuPathDB; FungiDB:YDR200C; -.
SGD; S000002608; VPS64.
GeneTree; ENSGT00530000068298; -.
HOGENOM; HOG000065944; -.
InParanoid; Q03944; -.
OMA; SENNDAL; -.
OrthoDB; EOG092C44DL; -.
BioCyc; YEAST:G3O-29785-MONOMER; -.
PRO; PR:Q03944; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0000321; P:re-entry into mitotic cell cycle after pheromone arrest; IGI:SGD.
GO; GO:0031929; P:TOR signaling; IGI:SGD.
CDD; cd00060; FHA; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR008984; SMAD_FHA_dom_sf.
Pfam; PF00498; FHA; 1.
SMART; SM00240; FHA; 1.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
1: Evidence at protein level;
Cell cycle; Coiled coil; Complete proteome; Endoplasmic reticulum;
Membrane; Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 604 Vacuolar protein sorting-associated
protein 64.
/FTId=PRO_0000065907.
TOPO_DOM 1 578 Cytoplasmic. {ECO:0000255}.
TRANSMEM 579 598 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 599 604 Lumenal. {ECO:0000255}.
DOMAIN 185 257 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
COILED 404 563 {ECO:0000255}.
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


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