VPS33_YEAST
ID VPS33_YEAST Reviewed; 691 AA.
AC P20795; D6VZ31;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Vacuolar protein sorting-associated protein 33;
DE AltName: Full=Protein SLP1;
DE AltName: Full=Vacuolar morphogenesis protein 5;
GN Name=VPS33; Synonyms=SLP1, VAM5; OrderedLocusNames=YLR396C;
GN ORFNames=L8084.15;
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 [MRNA].
RX PubMed=2183024; DOI=10.1128/mcb.10.5.2214-2223.1990;
RA Wada Y., Kitamoto K., Kanbe T., Tanaka K., Anraku Y.;
RT "The SLP1 gene of Saccharomyces cerevisiae is essential for vacuolar
RT morphogenesis and function.";
RL Mol. Cell. Biol. 10:2214-2223(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2201898; DOI=10.1128/mcb.10.9.4638-4649.1990;
RA Banta L.M., Vida T.A., Herman P.K., Emr S.D.;
RT "Characterization of yeast Vps33p, a protein required for vacuolar protein
RT sorting and vacuole biogenesis.";
RL Mol. Cell. Biol. 10:4638-4649(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [5]
RP INTERACTION WITH IVY1.
RX PubMed=12553664; DOI=10.1078/0171-9335-00290;
RA Lazar T., Scheglmann D., Gallwitz D.;
RT "A novel phospholipid-binding protein from the yeast Saccharomyces
RT cerevisiae with dual binding specificities for the transport GTPase Ypt7p
RT and the Sec1-related Vps33p.";
RL Eur. J. Cell Biol. 81:635-646(2002).
RN [6]
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 [7]
RP IDENTIFICATION IN THE HOPS COMPLEX, FUNCTION OF THE HOPS COMPLEX, AND
RP INTERACTION WITH VAM7.
RX PubMed=16601699; DOI=10.1038/sj.emboj.7601051;
RA Stroupe C., Collins K.M., Fratti R.A., Wickner W.;
RT "Purification of active HOPS complex reveals its affinities for
RT phosphoinositides and the SNARE Vam7p.";
RL EMBO J. 25:1579-1589(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, 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: Essential for vacuolar biogenesis, maturation and function.
CC Involved in the sorting of vacuolar proteins from the Golgi apparatus
CC and their targeting to the vacuole. Acts as component of the HOPS
CC complex that acts during the docking stage of vacuole fusion. HOPS is
CC an effector for the vacuolar Rab GTPase YPT7 and is required for
CC vacuolar SNARE complex assembly. It remains bound to SNARE complexes
CC after vacuole fusion. {ECO:0000269|PubMed:16601699}.
CC -!- SUBUNIT: Component of the HOPS complex which is composed of PEP5,
CC VPS16, PEP3, VPS33, VPS39 and VPS41. HOPS associates with
CC phosphoinositides and the PX domain of VAM7. Interacts with IVY1 and
CC VAM7. {ECO:0000269|PubMed:12553664, ECO:0000269|PubMed:16601699}.
CC -!- INTERACTION:
CC P20795; Q04934: IVY1; NbExp=3; IntAct=EBI-20395, EBI-35255;
CC P20795; P27801: PEP3; NbExp=8; IntAct=EBI-20395, EBI-13130;
CC P20795; P12868: PEP5; NbExp=5; IntAct=EBI-20395, EBI-6450;
CC P20795; Q12241: VAM3; NbExp=12; IntAct=EBI-20395, EBI-20227;
CC P20795; Q07468: VAM6; NbExp=6; IntAct=EBI-20395, EBI-20422;
CC P20795; P32912: VAM7; NbExp=4; IntAct=EBI-20395, EBI-20232;
CC P20795; Q03308: VPS16; NbExp=5; IntAct=EBI-20395, EBI-20355;
CC P20795; P38959: VPS41; NbExp=4; IntAct=EBI-20395, EBI-20432;
CC -!- SUBCELLULAR LOCATION: Vacuole.
CC -!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; M34474; AAA35052.1; -; mRNA.
DR EMBL; M34638; AAA35217.1; -; Genomic_DNA.
DR EMBL; U19729; AAB82354.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09697.1; -; Genomic_DNA.
DR PIR; A34708; A34708.
DR RefSeq; NP_013500.3; NM_001182284.3.
DR AlphaFoldDB; P20795; -.
DR SMR; P20795; -.
DR BioGRID; 31655; 83.
DR ComplexPortal; CPX-1625; HOPS complex.
DR ComplexPortal; CPX-1626; CORVET complex.
DR DIP; DIP-5910N; -.
DR IntAct; P20795; 19.
DR MINT; P20795; -.
DR STRING; 4932.YLR396C; -.
DR iPTMnet; P20795; -.
DR MaxQB; P20795; -.
DR PaxDb; P20795; -.
DR PRIDE; P20795; -.
DR EnsemblFungi; YLR396C_mRNA; YLR396C; YLR396C.
DR GeneID; 851112; -.
DR KEGG; sce:YLR396C; -.
DR SGD; S000004388; VPS33.
DR VEuPathDB; FungiDB:YLR396C; -.
DR eggNOG; KOG1302; Eukaryota.
DR GeneTree; ENSGT00940000156813; -.
DR HOGENOM; CLU_398604_0_0_1; -.
DR InParanoid; P20795; -.
DR OMA; FWNLHPL; -.
DR BioCyc; YEAST:G3O-32460-MON; -.
DR PRO; PR:P20795; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P20795; protein.
DR GO; GO:0033263; C:CORVET complex; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0031901; C:early endosome membrane; IDA:ComplexPortal.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0030897; C:HOPS complex; IPI:SGD.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; IDA:SGD.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IDA:ComplexPortal.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR GO; GO:0048278; P:vesicle docking; IGI:SGD.
DR GO; GO:0051469; P:vesicle fusion with vacuole; IGI:SGD.
DR GO; GO:0099022; P:vesicle tethering; IDA:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.40.850; -; 1.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR InterPro; IPR027121; VPS33.
DR InterPro; IPR043155; VPS33_dom3b.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR PANTHER; PTHR11679:SF1; PTHR11679:SF1; 1.
DR Pfam; PF00995; Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Vacuole.
FT CHAIN 1..691
FT /note="Vacuolar protein sorting-associated protein 33"
FT /id="PRO_0000206311"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 691 AA; 79271 MW; ED78DF55109C20E7 CRC64;
MNRFWNTKKF SLTNADGLCA TLNEISQNDE VLVVQPSVLP VLNSLLTFQD LTQSTPVRKI
TLLDDQLSDD LPSALGSVPQ MDLIFLIDVR TSLRLPPQLL DAAQKHNLSS LHIIYCRWKP
SFQNTLEDTE QWQKDGFDLN SKKTHFPNVI ESQLKELSNE YTLYPWDLLP FPQIDENVLL
THSLYNMENV NMYYPNLRSL QSATESILVD DMVNSLQSLI FETNSIITNV VSIGNLSKRC
SHLLKKRIDE HQTENDLFIK GTLYGERTNC GLEMDLIILE RNTDPITPLL TQLTYAGILD
DLYEFNSGIK IKEKDMNFNY KEDKIWNDLK FLNFGSIGPQ LNKLAKELQT QYDTRHKAES
VHEIKEFVDS LGSLQQRQAF LKNHTTLSSD VLKVVETEEY GSFNKILELE LEILMGNTLN
NDIEDIILEL QYQYEVDQKK ILRLICLLSL CKNSLREKDY EYLRTFMIDS WGIEKCFQLE
SLAELGFFTS KTGKTDLHIT TSKSTRLQKE YRYISQWFNT VPIEDEHAAD KITNENDDFS
EATFAYSGVV PLTMRLVQML YDRSILFHNY SSQQPFILSR EPRVSQTEDL IEQLYGDSHA
IEESIWVPGT ITKKINASIK SNNRRSIDGS NGTFHAAEDI ALVVFLGGVT MGEIAIMKHL
QKILGKKGIN KRFIIIADGL INGTRIMNSI S
