PEP3_YEAST
ID PEP3_YEAST Reviewed; 918 AA.
AC P27801; D6VYE3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Vacuolar membrane protein PEP3;
DE AltName: Full=Carboxypeptidase Y-deficient protein 3;
DE AltName: Full=Vacuolar morphogenesis protein 8;
DE AltName: Full=Vacuolar protein sorting-associated protein 18;
DE AltName: Full=Vacuolar protein-targeting protein 18;
GN Name=PEP3; Synonyms=VAM8, VPS18, VPT18; OrderedLocusNames=YLR148W;
GN ORFNames=L9634.2;
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].
RX PubMed=1944264; DOI=10.1128/mcb.11.12.5801-5812.1991;
RA Preston R., Manolson M.F., Becherer K., Weindnhammer E., Kirkpatrick D.,
RA Wright R., Jones E.W.;
RT "Isolation and characterization of PEP3, a gene required for vacuolar
RT biogenesis in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 11:5801-5812(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1840635; DOI=10.1128/mcb.11.12.5813-5824.1991;
RA Robinson J.S., Graham T.R., Emr S.D.;
RT "A putative zinc finger protein, Saccharomyces cerevisiae Vps18p, affects
RT late Golgi functions required for vacuolar protein sorting and efficient
RT alpha-factor prohormone maturation.";
RL Mol. Cell. Biol. 11:5813-5824(1991).
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 FUNCTION, AND INTERACTION WITH PEP5 AND PEP7.
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 [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-907, 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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-907, 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: Required for vacuolar biogenesis and for trafficking of
CC hydrolase precursors to the vacuole. Mediates transport at the vacuolar
CC membrane where it may be responsible for tethering transport vesicles
CC on the target membranes. Acts as component of the HOPS complex that
CC acts during the docking stage of vacuole fusion. HOPS is an effector
CC for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE
CC complex assembly. It remains bound to SNARE complexes after vacuole
CC fusion. {ECO:0000269|PubMed:10978279, 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 PEP5, PEP7
CC and VAM7. {ECO:0000269|PubMed:10978279, ECO:0000269|PubMed:16601699}.
CC -!- INTERACTION:
CC P27801; P12868: PEP5; NbExp=6; IntAct=EBI-13130, EBI-6450;
CC P27801; P20795: VPS33; NbExp=8; IntAct=EBI-13130, EBI-20395;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- MISCELLANEOUS: Present with 2020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS18 family. {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; M65144; AAA34852.1; -; Genomic_DNA.
DR EMBL; Z73320; CAA97720.1; -; Genomic_DNA.
DR EMBL; U53879; AAB82382.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09459.1; -; Genomic_DNA.
DR PIR; A41943; A41943.
DR RefSeq; NP_013249.1; NM_001182035.1.
DR PDB; 4UUY; X-ray; 2.14 A; A/B=2-348.
DR PDBsum; 4UUY; -.
DR AlphaFoldDB; P27801; -.
DR SMR; P27801; -.
DR BioGRID; 31417; 86.
DR ComplexPortal; CPX-1625; HOPS complex.
DR ComplexPortal; CPX-1626; CORVET complex.
DR DIP; DIP-5912N; -.
DR IntAct; P27801; 25.
DR MINT; P27801; -.
DR STRING; 4932.YLR148W; -.
DR iPTMnet; P27801; -.
DR MaxQB; P27801; -.
DR PaxDb; P27801; -.
DR PRIDE; P27801; -.
DR EnsemblFungi; YLR148W_mRNA; YLR148W; YLR148W.
DR GeneID; 850840; -.
DR KEGG; sce:YLR148W; -.
DR SGD; S000004138; PEP3.
DR VEuPathDB; FungiDB:YLR148W; -.
DR eggNOG; KOG2034; Eukaryota.
DR GeneTree; ENSGT00940000153635; -.
DR HOGENOM; CLU_003488_0_0_1; -.
DR InParanoid; P27801; -.
DR OMA; HVQRESR; -.
DR BioCyc; YEAST:G3O-32284-MON; -.
DR PRO; PR:P27801; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P27801; protein.
DR GO; GO:0033263; C:CORVET complex; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IDA:ComplexPortal.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0000306; C:extrinsic component of vacuolar membrane; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0006895; P:Golgi to endosome transport; IGI:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0045324; P:late endosome to vacuole transport; IGI:SGD.
DR GO; GO:0048284; P:organelle fusion; IBA:GO_Central.
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; IDA:SGD.
DR GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IMP:SGD.
DR GO; GO:0099022; P:vesicle tethering; IDA:SGD.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR007810; Pep3_Vps18.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF05131; Pep3_Vps18; 1.
DR SMART; SM00299; CLH; 1.
DR PROSITE; PS50236; CHCR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Metal-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Vacuole; Zinc; Zinc-finger.
FT CHAIN 1..918
FT /note="Vacuolar membrane protein PEP3"
FT /id="PRO_0000055993"
FT REPEAT 585..741
FT /note="CHCR"
FT ZN_FING 826..851
FT /note="RING-type; atypical"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4UUY"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4UUY"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 103..118
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 206..219
FT /evidence="ECO:0007829|PDB:4UUY"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:4UUY"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:4UUY"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:4UUY"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:4UUY"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:4UUY"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:4UUY"
SQ SEQUENCE 918 AA; 107398 MW; 37AE3C34AE0470B8 CRC64;
MIKTRIEEVQ LQFLTGNTEL THLKVSNDQL IVTTQRTIYR INLQDPAIVN HFDCPLSKEL
ETIMNVHVSP MGSVILIRTN FGRYMLLKDG EFTQLNKIKN LDLSSLHWIN ETTFLMGIKK
TPKLYRVELT GKDITTKLWY ENKKLSGGID GIAYWEGSLL LTIKDNILYW RDVTNMKFPL
VLPDESEQFE RLKHHAIKKF DSYNGLFAWV TSNGIVFGDL KEKQMEKDPA SNNFGKFLSS
SKVLLNFELP DYQNDKDHLI KDIVLTAFHI LLLRKNTVTM VSQLNNDVVF HETIPRHQLT
GSNTDSNEKF LGLVRDSVKE TFWCFSNINV FEIIIENEPN SVWNLLVRDN KFDKALSLKG
LTVREIESVK LSKAMYLFHT AKDFHSAAQT LGSMKDLSHF GEIALNFLQI KDYNDLNVIL
IKQLDNVPWK STQVVLSSWI IWNFMKQLND IELKINTTKP ASTDEDNLLN WNLNLKEKSN
ELTKFLESHL EKLDNETVYQ IMSKQNRQNE LLIFASLIND MKFLLSFWID QGNWYESLKI
LLTINNHDLV YKYSLILLLN SPEATVSTWM KIKDLDPNKL IPTILKFFTN WQNNSKLITN
ISEYPENYSL TYLKWCVREV PKMCNPIVYN SILYMMITDP RNDMILENDI IKFMKSNENK
YDLNFQLRLS LKFKKTKTSI FLLTRLNLFE DAIDLALKNN LIDDCKVIVN DEILIEDYKL
RKRLWLKIAK HLLLSMKDID IKQLIRTILN DSNEILTIKD LLPFFNEYTT IANLKEELIK
FLENHNMKMN EISEDIINSK NLKVEINTEI SKFNEIYRIL EPGKSCDECG KFLQIKKFIV
FPCGHCFHWN CIIRVILNSN DYNLRQKTEN FLKAKSKHNL NDLENIIVEK CGLCSDININ
KIDQPISIDE TELAKWNE
