VAC7_YEAST
ID VAC7_YEAST Reviewed; 1165 AA.
AC P53950; D6W1C5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Vacuolar segregation protein 7;
GN Name=VAC7; OrderedLocusNames=YNL054W; ORFNames=N2467, YNL2467W;
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 [GENOMIC DNA], FUNCTION, TOPOLOGY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9372916; DOI=10.1128/mcb.17.12.6847;
RA Bonangelino C.J., Catlett N.L., Weisman L.S.;
RT "Vac7p, a novel vacuolar protein, is required for normal vacuole
RT inheritance and morphology.";
RL Mol. Cell. Biol. 17:6847-6858(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=8533472; DOI=10.1002/yea.320111008;
RA Bergez P., Doignon F., Crouzet M.;
RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT XIV from Saccharomyces cerevisiae.";
RL Yeast 11:967-974(1995).
RN [3]
RP ERRATUM OF PUBMED:8533472.
RX PubMed=8904343;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA Bergez P., Doignon F., Crouzet M.;
RL Yeast 12:297-297(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=11950935; DOI=10.1091/mbc.01-10-0498;
RA Gary J.D., Sato T.K., Stefan C.J., Bonangelino C.J., Weisman L.S.,
RA Emr S.D.;
RT "Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by
RT Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member.";
RL Mol. Biol. Cell 13:1238-1251(2002).
RN [7]
RP FUNCTION.
RX PubMed=16492811; DOI=10.1083/jcb.200512105;
RA Duex J.E., Tang F., Weisman L.S.;
RT "The Vac14p-Fig4p complex acts independently of Vac7p and couples PI3,5P2
RT synthesis and turnover.";
RL J. Cell Biol. 172:693-704(2006).
RN [8]
RP IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19037259; DOI=10.1038/emboj.2008.248;
RA Jin N., Chow C.Y., Liu L., Zolov S.N., Bronson R., Davisson M.,
RA Petersen J.L., Zhang Y., Park S., Duex J.E., Goldowitz D., Meisler M.H.,
RA Weisman L.S.;
RT "VAC14 nucleates a protein complex essential for the acute interconversion
RT of PI3P and PI(3,5)P(2) in yeast and mouse.";
RL EMBO J. 27:3221-3234(2008).
RN [9]
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).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, 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: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC Positively regulates FAB1 kinase activity. Major activator of FAB1
CC during hyperosmotic shock and can elevate levels of PtdIns(3,5)P2 in
CC the absence of VAC14 and FIG4. Directly involved in vacuolar membrane
CC scission. Required for normal vacuole acidification, inheritance and
CC morphology. {ECO:0000269|PubMed:11950935, ECO:0000269|PubMed:16492811,
CC ECO:0000269|PubMed:19037259, ECO:0000269|PubMed:9372916}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex, composed of
CC ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the
CC complex and serves as a scaffold. {ECO:0000269|PubMed:19037259}.
CC -!- INTERACTION:
CC P53950; Q06708: VAC14; NbExp=4; IntAct=EBI-28714, EBI-27189;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:19037259,
CC ECO:0000269|PubMed:9372916}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:19037259, ECO:0000269|PubMed:9372916}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
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DR EMBL; U12141; AAA99658.1; -; Genomic_DNA.
DR EMBL; Z71330; CAA95925.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10491.1; -; Genomic_DNA.
DR PIR; S62982; S62982.
DR RefSeq; NP_014344.3; NM_001182893.3.
DR AlphaFoldDB; P53950; -.
DR SMR; P53950; -.
DR BioGRID; 35770; 387.
DR ComplexPortal; CPX-3088; PAS complex.
DR DIP; DIP-4368N; -.
DR IntAct; P53950; 4.
DR MINT; P53950; -.
DR STRING; 4932.YNL054W; -.
DR iPTMnet; P53950; -.
DR MaxQB; P53950; -.
DR PaxDb; P53950; -.
DR PRIDE; P53950; -.
DR EnsemblFungi; YNL054W_mRNA; YNL054W; YNL054W.
DR GeneID; 855673; -.
DR KEGG; sce:YNL054W; -.
DR SGD; S000004999; VAC7.
DR VEuPathDB; FungiDB:YNL054W; -.
DR eggNOG; ENOG502QU5B; Eukaryota.
DR HOGENOM; CLU_006002_0_0_1; -.
DR InParanoid; P53950; -.
DR OMA; GNTISCP; -.
DR BioCyc; MetaCyc:G3O-33086-MON; -.
DR BioCyc; YEAST:G3O-33086-MON; -.
DR PRO; PR:P53950; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53950; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0070772; C:PAS complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IDA:UniProtKB.
DR GO; GO:1903100; P:1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate metabolic process; IC:ComplexPortal.
DR GO; GO:0033674; P:positive regulation of kinase activity; IGI:SGD.
DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IGI:SGD.
DR GO; GO:1903778; P:protein localization to vacuolar membrane; IMP:SGD.
DR GO; GO:0010511; P:regulation of phosphatidylinositol biosynthetic process; IC:ComplexPortal.
DR GO; GO:0000011; P:vacuole inheritance; IBA:GO_Central.
DR InterPro; IPR024260; Vac7.
DR PANTHER; PTHR28258; PTHR28258; 1.
DR Pfam; PF12751; Vac7; 2.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..1165
FT /note="Vacuolar segregation protein 7"
FT /id="PRO_0000065757"
FT TOPO_DOM 1..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 920..940
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..1165
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 118..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1098
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 1020
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1099
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1165 AA; 128140 MW; 0414978AA3066CE7 CRC64;
MTEEDRKLTV ETETVEAPVA NNLLLSNNSN VVAPNPSIPS ASTSTSPLHR EIVDDSVATA
NTTSNVVQHN LPTIDNNLMD SDATSHNQDH WHSDINRAGT SMSTSDIPTD LHLEHIGSVS
STNNNSNNAL INHNPLSSHL SNPSSSLRNK KSSLLVASNP AFASDVELSK KKPAVISNNM
PTSNIALYQT ARSANIHGPS STSASKAFRK ASAFSNNTAP STSNNIGSNT PPAPLLPLPS
LSQQNKPKII ERPTMHVTNS REILLGENLL DDTKAKNAPA NSTTHDNGPV ANDGLRIPNH
SNADDNENNN KMKKNKNINS GKNERNDDTS KICTTSTKTA PSTAPLGSTD NTQALTASVS
SSNADNHNNN KKKTSSNNNG NNSNSASNKT NADIKNSNAD LSASTSNNNA INDDSHESNS
EKPTKADFFA ARLATAVGEN EISDSEETFV YESAANSTKN LIFPDSSSQQ QQQQQQPPKQ
QQQQQNHGIT SKISAPLLNN NKKLLSRLKN SRHISTGAIL NNTIATISTN PNLNSNVMQN
NNNLMSGHNH LDELSSIKQE PPHQLQQQQP PMDVQSVDSY TSDNPDSNVI AKSPDKRSSL
VSLSKVSPHL LSSTSSNGNT ISCPNVATNS QELEPNNDIS TKKSLSNSTL RHSSANRNSN
YGDNKRPLRT TVSKIFDSNP NGAPLRRYSG VPDHVNLEDY IEQPHNYPTM QNSVKKDEFY
NSRNNKFPHG LNFYGDNNVI EEENNGDSSN VNRPQHTNLQ HEFIPEDNES DENDIHSMFY
YNHKNDLETK PLISDYGEDE DVDDYDRPNA TFNSYYGSAS NTHELPLHGR MPSRSNNDYY
DFMVGNNTGN NNQLNEYTPL RMKRGQRHLS RTNNSIMNGS IHMNGNDDVT HSNINNNDIV
GYSPHNFYSR KSPFVKVKNF LYLAFVISSL LMTGFILGFL LATNKELQDV DVVVMDNVIS
SSDELIFDIT VSAFNPGFFS ISVSQVDLDI FAKSSYLKCD SNGDCTVMEQ ERKILQITTN
LSLVEESANN DISGGNIETV LLGTAKKLET PLKFQGGAFN RNYDVSVSSV KLLSPGSREA
KHENDDDDDD DGDDGDDENN TNERQYKSKP NARDDKEDDT KKWKLLIKHD YELIVRGSMK
YEVPFFNTQK STAIQKDSMV HPGKK
