VPS60_YEAST
ID VPS60_YEAST Reviewed; 229 AA.
AC Q03390; D6VTA9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Vacuolar protein-sorting-associated protein 60;
DE AltName: Full=Charged multivesicular body protein 5;
GN Name=VPS60; Synonyms=CHM5, MOS10; OrderedLocusNames=YDR486C;
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 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 [4]
RP FUNCTION.
RX PubMed=11559748; DOI=10.1242/jcs.114.13.2395;
RA Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
RT "CHMP1 functions as a member of a newly defined family of vesicle
RT trafficking proteins.";
RL J. Cell Sci. 114:2395-2404(2001).
RN [5]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(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 FUNCTION, INTERACTION WITH VTA1, AND SUBCELLULAR LOCATION.
RX PubMed=14701806; DOI=10.1074/jbc.m312669200;
RA Shiflett S.L., Ward D.M., Huynh D., Vaughn M.B., Simmons J.C., Kaplan J.;
RT "Characterization of Vta1p, a class E Vps protein in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 279:10982-10990(2004).
RN [9]
RP FUNCTION, INTERACTION WITH VTA1, AND MUTAGENESIS OF 144-ILE--ASP-148.
RX PubMed=18194652; DOI=10.1016/j.devcel.2007.10.021;
RA Azmi I.F., Davies B.A., Xiao J., Babst M., Xu Z., Katzmann D.J.;
RT "ESCRT-III family members stimulate Vps4 ATPase activity directly or via
RT Vta1.";
RL Dev. Cell 14:50-61(2008).
RN [10]
RP INTERACTION WITH VTA1.
RX PubMed=18032584; DOI=10.1091/mbc.e07-07-0694;
RA Rue S.M., Mattei S., Saksena S., Emr S.D.;
RT "Novel Ist1-Did2 complex functions at a late step in multivesicular body
RT sorting.";
RL Mol. Biol. Cell 19:475-484(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Has a role in a late stage of multivesicular body (MVB)
CC formation. Can stimulate VPS4 ATPase activity via VTA1.
CC {ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:14701806,
CC ECO:0000269|PubMed:18194652}.
CC -!- SUBUNIT: Interacts with VTA1; the interaction occurs at he endosomal
CC membrane. {ECO:0000269|PubMed:14701806, ECO:0000269|PubMed:18032584,
CC ECO:0000269|PubMed:18194652}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein.
CC Vacuole membrane; Peripheral membrane protein.
CC -!- MISCELLANEOUS: Present with 2110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64922.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS56499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U33050; AAB64922.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY558173; AAS56499.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA12319.1; -; Genomic_DNA.
DR PIR; S69653; S69653.
DR RefSeq; NP_010774.4; NM_001180794.3.
DR PDB; 2LUH; NMR; -; B=128-186.
DR PDBsum; 2LUH; -.
DR AlphaFoldDB; Q03390; -.
DR BMRB; Q03390; -.
DR SMR; Q03390; -.
DR BioGRID; 32538; 248.
DR DIP; DIP-8785N; -.
DR IntAct; Q03390; 2.
DR MINT; Q03390; -.
DR STRING; 4932.YDR486C; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; Q03390; -.
DR MaxQB; Q03390; -.
DR PaxDb; Q03390; -.
DR PRIDE; Q03390; -.
DR TopDownProteomics; Q03390; -.
DR EnsemblFungi; YDR486C_mRNA; YDR486C; YDR486C.
DR GeneID; 852097; -.
DR KEGG; sce:YDR486C; -.
DR SGD; S000002894; VPS60.
DR VEuPathDB; FungiDB:YDR486C; -.
DR eggNOG; KOG1655; Eukaryota.
DR GeneTree; ENSGT00550000074817; -.
DR HOGENOM; CLU_079409_0_0_1; -.
DR InParanoid; Q03390; -.
DR OMA; MEQAQTM; -.
DR BioCyc; YEAST:G3O-30011-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-SCE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:Q03390; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03390; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0030447; P:filamentous growth; IMP:SGD.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Vacuole.
FT CHAIN 1..229
FT /note="Vacuolar protein-sorting-associated protein 60"
FT /id="PRO_0000211507"
FT REGION 128..159
FT /note="Interaction with VTA1"
FT REGION 186..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..155
FT /evidence="ECO:0000255"
FT COMPBIAS 214..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 144..148
FT /note="IEQGD->AAAAA: Abolishes interaction with VTA1 and
FT reduces endosomal localization."
FT /evidence="ECO:0000269|PubMed:18194652"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:2LUH"
FT HELIX 140..158
FT /evidence="ECO:0007829|PDB:2LUH"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2LUH"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:2LUH"
SQ SEQUENCE 229 AA; 25862 MW; 292DD033F00E2728 CRC64;
MNRIFGYGNK KSHDQLLQES NQSMNQAQQS LSNRISQLDT QIAQLNFQLQ NIQKNLQRSN
NKQPSLRKQA LKILNKRKQL ENMKDSLDSQ SWSMTQAQLT NDNLQNTMIT INALKQTNNA
MKAQYGKINI DKLQDMQDEM LDLIEQGDEL QEVLAMNNNS GELDDISDAE LDAELDALAQ
EDFTLPTSEN SLGNDMPSYL LGANAPPAFI DEEPNLDTED KNKALESAQ
