PEP12_YEAST
ID PEP12_YEAST Reviewed; 288 AA.
AC P32854; D6W2A3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Syntaxin PEP12;
DE AltName: Full=Carboxypeptidase Y-deficient protein 12;
DE AltName: Full=Vacuolar protein sorting-associated protein 6;
DE AltName: Full=Vacuolar protein-targeting protein 13;
GN Name=PEP12; Synonyms=VPS6, VPT13; OrderedLocusNames=YOR036W;
GN ORFNames=OR26.29;
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=8730101; DOI=10.1091/mbc.7.4.579;
RA Becherer K.A., Rieder S.E., Emr S.D., Jones E.W.;
RT "Novel syntaxin homologue, Pep12p, required for the sorting of lumenal
RT hydrolases to the lysosome-like vacuole in yeast.";
RL Mol. Biol. Cell 7:579-594(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP UBIQUITINATION BY TUL1, AND MUTAGENESIS OF LEU-271.
RX PubMed=11788821; DOI=10.1038/ncb743;
RA Reggiori F., Pelham H.R.B.;
RT "A transmembrane ubiquitin ligase required to sort membrane proteins into
RT multivesicular bodies.";
RL Nat. Cell Biol. 4:117-123(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-23, AND
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 [7]
RP IDENTIFICATION BY 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: Plays a role in the sorting and targeting of vacuolar
CC proteases.
CC -!- INTERACTION:
CC P32854; Q12154: GET3; NbExp=5; IntAct=EBI-13098, EBI-2989;
CC P32854; P36015: YKT6; NbExp=2; IntAct=EBI-13098, EBI-26982;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:11788821}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; M90395; AAB38370.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60755.1; -; Genomic_DNA.
DR EMBL; Z74944; CAA99226.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10819.1; -; Genomic_DNA.
DR PIR; S62175; S62175.
DR RefSeq; NP_014679.1; NM_001183455.1.
DR AlphaFoldDB; P32854; -.
DR SMR; P32854; -.
DR BioGRID; 34438; 119.
DR ComplexPortal; CPX-5421; Endosomal SNARE complex PEP12-VTI1-SYN8-YKT6.
DR ComplexPortal; CPX-5422; Endosomal SNARE complex PEP12-VTI1-TLG1-YKT6.
DR ComplexPortal; CPX-5423; Endosomal SNARE complex PEP12-VTI1-TLG1-SNC1.
DR ComplexPortal; CPX-5424; Endosomal SNARE complex PEP12-VTI1-SYN8-SNC1.
DR ComplexPortal; CPX-5461; Endosomal SNARE complex PEP12-VTI1-SYN8-SNC2.
DR ComplexPortal; CPX-5462; Endosomal SNARE complex PEP12-VTI1-TLG1-SNC2.
DR DIP; DIP-2021N; -.
DR IntAct; P32854; 18.
DR MINT; P32854; -.
DR STRING; 4932.YOR036W; -.
DR iPTMnet; P32854; -.
DR MaxQB; P32854; -.
DR PaxDb; P32854; -.
DR PRIDE; P32854; -.
DR EnsemblFungi; YOR036W_mRNA; YOR036W; YOR036W.
DR GeneID; 854201; -.
DR KEGG; sce:YOR036W; -.
DR SGD; S000005562; PEP12.
DR VEuPathDB; FungiDB:YOR036W; -.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_059257_4_1_1; -.
DR InParanoid; P32854; -.
DR OMA; EHRQKLH; -.
DR BioCyc; YEAST:G3O-33582-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR PRO; PR:P32854; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32854; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IMP:SGD.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IMP:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0006895; P:Golgi to endosome transport; IC:ComplexPortal.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IC:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF14523; Syntaxin_2; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..288
FT /note="Syntaxin PEP12"
FT /id="PRO_0000210271"
FT TOPO_DOM 1..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..288
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 195..257
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 271
FT /note="L->D: Increases ubiquitination by TUL1."
FT /evidence="ECO:0000269|PubMed:11788821"
FT CONFLICT 13
FT /note="A -> G (in Ref. 1; AAB38370)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> I (in Ref. 1; AAB38370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 33006 MW; D9F5711339DA1CDA CRC64;
MSEDEFFGGD NEAVWNGSRF SDSPEFQTLK EEVAAELFEI NGQISTLQQF TATLKSFIDR
GDVSAKVVER INKRSVAKIE EIGGLIKKVN TSVKKMDAIE EASLDKTQII AREKLVRDVS
YSFQEFQGIQ RQFTQVMKQV NERAKESLEA SEMANDAALL DEEQRQNSSK STRIPGSQIV
IERDPINNEE FAYQQNLIEQ RDQEISNIER GITELNEVFK DLGSVVQQQG VLVDNIEANI
YTTSDNTQLA SDELRKAMRY QKRTSRWRVY LLIVLLVMLL FIFLIMKL
