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Vacuolar protein sorting-associated protein 54 (CPF1 genetically-interacting protein 1) (Temperature-sensitive clathrin synthetic mutation protein 3)

 VPS54_YEAST             Reviewed;         889 AA.
Q12071; D6VS12;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 129.
RecName: Full=Vacuolar protein sorting-associated protein 54;
AltName: Full=CPF1 genetically-interacting protein 1;
AltName: Full=Temperature-sensitive clathrin synthetic mutation protein 3;
Name=VPS54; Synonyms=CGP1, LUV1, RKI1, TCS3;
OrderedLocusNames=YDR027C; ORFNames=PZF889, YD9813.05C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8896275;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1085::AID-YEA9>3.3.CO;2-S;
Eide L.G., Sander C., Prydz H.;
"Sequencing and analysis of a 35.4 kb region on the right arm of
chromosome IV from Saccharomyces cerevisiae reveal 23 open reading
frames.";
Yeast 12:1085-1090(1996).
[2]
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).
[3]
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).
[4]
INTERACTION WITH RBL2.
PubMed=9914379; DOI=10.1007/s004120050331;
Smith A.M., Archer J.E., Solomon F.;
"Regulation of tubulin polypeptides and microtubule function: Luv1p
interacts with the beta-tubulin binding protein Rbl2p.";
Chromosoma 107:471-478(1998).
[5]
FUNCTION.
PubMed=10628971;
Bensen E.S., Costaguta G., Payne G.S.;
"Synthetic genetic interactions with temperature-sensitive clathrin in
Saccharomyces cerevisiae. Roles for synaptojanin-like Inp53p and
dynamin-related Vps1p in clathrin-dependent protein sorting at the
trans-Golgi network.";
Genetics 154:83-97(2000).
[6]
FUNCTION, AND INTERACTION WITH VSP52 AND VSP53.
PubMed=10637310; DOI=10.1091/mbc.11.1.305;
Conibear E., Stevens T.H.;
"Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required
for protein sorting at the yeast late Golgi.";
Mol. Biol. Cell 11:305-323(2000).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10888679; DOI=10.1091/mbc.11.7.2429;
Conboy M.J., Cyert M.S.;
"Luv1p/Rki1p/Tcs3p/Vps54p, a yeast protein that localizes to the late
Golgi and early endosome, is required for normal vacuolar
morphology.";
Mol. Biol. Cell 11:2429-2443(2000).
[8]
FUNCTION, AND INTERACTION WITH TLG1 AND YPT6.
PubMed=11689439; DOI=10.1093/emboj/20.21.5991;
Siniossoglou S., Pelham H.R.B.;
"An effector of Ypt6p binds the SNARE Tlg1p and mediates selective
fusion of vesicles with late Golgi membranes.";
EMBO J. 20:5991-5998(2001).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS51; VSP52 AND
VSP53.
PubMed=12377769; DOI=10.1074/jbc.M209428200;
Siniossoglou S., Pelham H.R.B.;
"Vps51p links the VFT complex to the SNARE Tlg1p.";
J. Biol. Chem. 277:48318-48324(2002).
[10]
FUNCTION, AND INTERACTION WITH VPS52; SEC10; SEC15 AND EXO84.
PubMed=12395193; DOI=10.1007/s00438-002-0748-4;
Fiedler T.A., Karpova T.S., Fleig U., Young M.E., Cooper J.A.,
Hegemann J.H.;
"The vesicular transport protein Cgp1p/Vps54p/Tcs3p/Luv1p is required
for the integrity of the actin cytoskeleton.";
Mol. Genet. Genomics 268:190-205(2002).
[11]
INTERACTION WITH ARL1.
PubMed=12620189; DOI=10.1016/S0960-9822(03)00091-5;
Panic B., Whyte J.R.C., Munro S.;
"The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts
with vesicle-tethering factors at the Golgi apparatus.";
Curr. Biol. 13:405-410(2003).
[12]
FUNCTION, AND INTERACTION WITH VPS51; VPS52 AND VPS53.
PubMed=12446664; DOI=10.1074/jbc.M210436200;
Reggiori F., Wang C.-W., Stromhaug P.E., Shintani T., Klionsky D.J.;
"Vps51 is part of the yeast Vps fifty-three tethering complex
essential for retrograde traffic from the early endosome and Cvt
vesicle completion.";
J. Biol. Chem. 278:5009-5020(2003).
[13]
FUNCTION, AND INTERACTION WITH VPS51; VPS52 AND VPS53.
PubMed=12686613; DOI=10.1091/mbc.E02-10-0654;
Conibear E., Cleck J.N., Stevens T.H.;
"Vps51p mediates the association of the GARP (Vps52/53/54) complex
with the late Golgi t-SNARE Tlg1p.";
Mol. Biol. Cell 14:1610-1623(2003).
[14]
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).
[15]
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).
[16]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-72, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND THR-74, AND
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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Involved in retrograde transport from early and late
endosomes to late Golgi by linking the vesicle through the t-SNARE
TGL1 to the Golgi, leading to the membrane fusion between late
Golgi and endosomal vesicles. Seems also to be involved in protein
transport from Golgi to the plasma membrane and is required for
the integrity of the actin cytoskeleton.
{ECO:0000269|PubMed:10628971, ECO:0000269|PubMed:10637310,
ECO:0000269|PubMed:10888679, ECO:0000269|PubMed:11689439,
ECO:0000269|PubMed:12377769, ECO:0000269|PubMed:12395193,
ECO:0000269|PubMed:12446664, ECO:0000269|PubMed:12686613}.
-!- SUBUNIT: Component of the Golgi-associated retrograde protein
(GARP) complex, also called VFT (VPS fifty-three) complex,
composed of VPS51, VPS52, VPS53 and VPS54. Interacts also with
YPT6, TLG1, RBL2, SEC10, SEC15, EXO84 and ARL1.
{ECO:0000269|PubMed:10637310, ECO:0000269|PubMed:11689439,
ECO:0000269|PubMed:12377769, ECO:0000269|PubMed:12395193,
ECO:0000269|PubMed:12446664, ECO:0000269|PubMed:12620189,
ECO:0000269|PubMed:12686613, ECO:0000269|PubMed:9914379}.
-!- INTERACTION:
P38116:ARL1; NbExp=3; IntAct=EBI-36751, EBI-2869;
P36116:VPS51; NbExp=3; IntAct=EBI-36751, EBI-26352;
P39904:VPS52; NbExp=8; IntAct=EBI-36751, EBI-16418;
P47061:VPS53; NbExp=9; IntAct=EBI-36751, EBI-25828;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane; Peripheral membrane protein. Endosome membrane;
Peripheral membrane protein. Mitochondrion membrane {ECO:0000305};
Peripheral membrane protein {ECO:0000305}. Note=May also be
mitochondrial.
-!- MISCELLANEOUS: Present with 2540 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the VPS54 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X95966; CAA65220.1; -; Genomic_DNA.
EMBL; Z47814; CAA87806.1; -; Genomic_DNA.
EMBL; Z74323; CAA98849.1; -; Genomic_DNA.
EMBL; BK006938; DAA11872.1; -; Genomic_DNA.
PIR; S50934; S50934.
RefSeq; NP_010310.1; NM_001180335.1.
ProteinModelPortal; Q12071; -.
BioGrid; 32077; 232.
DIP; DIP-5903N; -.
IntAct; Q12071; 17.
MINT; MINT-643806; -.
STRING; 4932.YDR027C; -.
iPTMnet; Q12071; -.
MaxQB; Q12071; -.
PRIDE; Q12071; -.
EnsemblFungi; YDR027C; YDR027C; YDR027C.
GeneID; 851591; -.
KEGG; sce:YDR027C; -.
EuPathDB; FungiDB:YDR027C; -.
SGD; S000002434; VPS54.
HOGENOM; HOG000065963; -.
InParanoid; Q12071; -.
KO; K17600; -.
OMA; ERWRQVD; -.
OrthoDB; EOG092C0WVF; -.
BioCyc; YEAST:G3O-29643-MONOMER; -.
PRO; PR:Q12071; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0000938; C:GARP complex; IPI:SGD.
GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
GO; GO:0090156; P:cellular sphingolipid homeostasis; IMP:SGD.
GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:SGD.
1: Evidence at protein level;
Coiled coil; Complete proteome; Endosome; Golgi apparatus; Membrane;
Mitochondrion; Phosphoprotein; Protein transport; Reference proteome;
Transport.
CHAIN 1 889 Vacuolar protein sorting-associated
protein 54.
/FTId=PRO_0000148737.
COILED 286 321 {ECO:0000255}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 74 74 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
SEQUENCE 889 AA; 101520 MW; 67E930C34E8CC5AA CRC64;
MSISETPHNK SQGLQKAAGR PKIVVPEGSP SRNSDSGSFT IEGDTSLNDD LLSISGSVTP
RARRSSRLSL DSITPRRSFD SRTLSVANSR SFGFENETHS GSMDFSPLGN NSIYEIVMNT
RRKNWLNYPT VADIPQVSLS KNDLDDHWKT HVIEYVKNIK SDYQIFQSTN NIRNMNQMEQ
LKELREGENM HEESFEANLR QGDAELINSI PDFYFSDKFQ LDNPRTFHKV LDAIDLFLTK
LDMKRQAERD EAFSELRDRL NDFLDIVETL LVTEISKSSH KFFHALSEVD NIQKRALDTM
SELKELAQNI KTIDAENIRK KISHLEMIFK RKNVEKLEQG LLQAKLVLNK TDECKSMYEE
NKLDNCLELI KSIDYLIKGD DSINEDVQSW TRCWPYKLSN LRTIPALSAT REFLTNMKIE
IGGKFSLQLS ILLIDDLRSF CKSIKPKETL HRIQTGSNDK KQTIFTDNFS SKITELIVRL
NRCEELTSAF DLYREKSITE LKSIIKIYLP TENAHADNNH DEKHLNNGST SGSKLSRLIK
EQTPAEFQSM LVNIFTHALE ALRRLYGHQK LLLDISLNEL ASVKSPNENQ HNMITQLDIR
TGINEIIRII QLRTGKIIAV RRELNLSLRY DYFLKFYAIC VIFIQECEVL SGEFLTKYLS
NVLASQIKHY ANAQSSKNYR NIKKKIDAEE WIPYIVDSSI QSDVNDIVSS IDIDPLSWTT
ILDMVGGSHD CENGRSEDKE KDEGNETYQG HRKSVVVGDK TFVASSSLLA TIEVIKELMV
LSINLPSIYL SNFEKLCYDA LQYYNSSAMA SVTQPGNSLL KTGRNLSIMG ESLDCLAEFV
IIVQRFYQRL SNSNRDFEPF DASHYTTLLG QFQASSNKIY MANAPPPPV


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