PEP7_YEAST
ID PEP7_YEAST Reviewed; 515 AA.
AC P32609; D6VSV6; Q99229;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Vacuolar segregation protein PEP7;
DE AltName: Full=Carboxypeptidase Y-deficient protein 7;
DE AltName: Full=Protein VAC1;
DE AltName: Full=Vacuolar protein sorting-associated protein 19;
DE AltName: Full=Vacuolar protein-targeting protein 19;
GN Name=PEP7; Synonyms=VAC1, VPL21, VPS19, VPT19; OrderedLocusNames=YDR323C;
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], AND FUNCTION.
RC STRAIN=LWY148;
RX PubMed=1730622; DOI=10.1016/s0021-9258(18)48539-0;
RA Weisman L.S., Wickner W.;
RT "Molecular characterization of VAC1, a gene required for vacuole
RT inheritance and vacuole protein sorting.";
RL J. Biol. Chem. 267:618-623(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9168472; DOI=10.1091/mbc.8.5.871;
RA Webb G.C., Zhang J., Garlow S.J., Wesp A., Riezman H., Jones E.W.;
RT "Pep7p provides a novel protein that functions in vesicle-mediated
RT transport between the yeast Golgi and endosome.";
RL Mol. Biol. Cell 8:871-895(1997).
RN [3]
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 [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 VPS21 AND VPS45, AND SUBCELLULAR LOCATION.
RX PubMed=10359603; DOI=10.1091/mbc.10.6.1873;
RA Tall G.G., Hama H., DeWald D.B., Horazdovsky B.F.;
RT "The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with
RT a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar
RT protein sorting.";
RL Mol. Biol. Cell 10:1873-1889(1999).
RN [6]
RP INTERACTION WITH PEP3 AND PEP5.
RX PubMed=10978279; DOI=10.1093/genetics/156.1.105;
RA Srivastava A., Woolford C.A., Jones E.W.;
RT "Pep3p/Pep5p complex: a putative docking factor at multiple steps of
RT vesicular transport to the vacuole of Saccharomyces cerevisiae.";
RL Genetics 156:105-122(2000).
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).
CC -!- FUNCTION: Required for vacuole segregation and vacuole protein sorting.
CC Possibly part of a complex which tethers the vacuole membrane to
CC microtubules, either directly or via kinesin or dynein-like motor
CC proteins. Probably functions in several interorganelle traffic
CC pathways. {ECO:0000269|PubMed:1730622, ECO:0000269|PubMed:9168472}.
CC -!- SUBUNIT: Interacts with VPS21, VPS45, PEP3 and PEP5.
CC {ECO:0000269|PubMed:10359603, ECO:0000269|PubMed:10978279}.
CC -!- INTERACTION:
CC P32609; P38932: VPS45; NbExp=3; IntAct=EBI-20208, EBI-20444;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10359603};
CC Peripheral membrane protein {ECO:0000269|PubMed:10359603}; Cytoplasmic
CC side {ECO:0000269|PubMed:10359603}.
CC -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M80596; AAA35203.1; -; Genomic_DNA.
DR EMBL; U22070; AAB60290.1; -; Genomic_DNA.
DR EMBL; U32517; AAB64759.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12166.1; -; Genomic_DNA.
DR PIR; S59811; S59811.
DR RefSeq; NP_010610.3; NM_001180631.3.
DR AlphaFoldDB; P32609; -.
DR SMR; P32609; -.
DR BioGRID; 32381; 152.
DR DIP; DIP-5240N; -.
DR IntAct; P32609; 6.
DR STRING; 4932.YDR323C; -.
DR iPTMnet; P32609; -.
DR MaxQB; P32609; -.
DR PaxDb; P32609; -.
DR PRIDE; P32609; -.
DR EnsemblFungi; YDR323C_mRNA; YDR323C; YDR323C.
DR GeneID; 851923; -.
DR KEGG; sce:YDR323C; -.
DR SGD; S000002731; PEP7.
DR VEuPathDB; FungiDB:YDR323C; -.
DR eggNOG; KOG1842; Eukaryota.
DR HOGENOM; CLU_026440_0_0_1; -.
DR InParanoid; P32609; -.
DR OMA; GLWCRVC; -.
DR BioCyc; YEAST:G3O-29880-MON; -.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P32609; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32609; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010009; C:cytoplasmic side of endosome membrane; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:SGD.
DR GO; GO:0006896; P:Golgi to vacuole transport; IPI:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IMP:SGD.
DR GO; GO:0006906; P:vesicle fusion; IMP:SGD.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR021565; Rbsn_Rab-bd.
DR InterPro; IPR036531; Rbsn_Rab-bd_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF11464; Rbsn; 1.
DR SMART; SM00064; FYVE; 2.
DR SUPFAM; SSF140125; SSF140125; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS50178; ZF_FYVE; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Reference proteome; Repeat; Vacuole; Zinc;
KW Zinc-finger.
FT CHAIN 1..515
FT /note="Vacuolar segregation protein PEP7"
FT /id="PRO_0000046858"
FT ZN_FING 6..29
FT /note="C2H2-type"
FT ZN_FING 72..137
FT /note="FYVE-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT ZN_FING 215..297
FT /note="FYVE-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 36..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT CONFLICT 366
FT /note="H -> Y (in Ref. 1; AAA35203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 59443 MW; 53C304F1ADA5B7A1 CRC64;
MDLENVSCPI CLRKFDNLQA LNAHLDVEHG FNDNEDSLGS NDSRLVNGKQ KKARSVDSSA
QKLKRSHWEK FKKGKSCCHT CGRTLNNNIG AINCRKCGKL YCRRHLPNMI KLNLSAQYDP
RNGKWYNCCH DCFVTKPGYN DYGEVIDLTP EFFKVRNIKR EDKNLRLLQL ENRFVRLVDG
LITLYNTYSR SIIHNLKMNS EMSKLERTVT PWRDDRSVLF CNICSEPFGL LLRKHHCRLC
GMVVCDDANR NCSNEISIGY LMSAASDLPF EYNIQKDDLL HIPISIRLCS HCIDMLFIGR
KFNKDVRMPL SGIFAKYDSM QNISKVIDSL LPIFEDSLNS LKVETAKDSE NTLDPKNLND
LARLRHKLLN SFNLYNTLTR QLLSVEPQSH LERQLQNSIK IASAAYINEK ILPLKSLPAI
LNPEGHKTNE DGQKAEPEVK KLSQLMIENL TIKEVKELRE ELMVLKEQSY LIESTIQDYK
KQRRLEEIVT LNKNLEELHS RIHTVQSKLG DHGFN
