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YKT6_YEAST
ID   YKT6_YEAST              Reviewed;         200 AA.
AC   P36015; D6VX04;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 198.
DE   RecName: Full=Synaptobrevin homolog YKT6;
DE            EC=2.3.1.-;
DE   Flags: Precursor;
GN   Name=YKT6; OrderedLocusNames=YKL196C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158, AND IDENTIFICATION BY
RP   MASS 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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158, 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).
RN   [7]
RP   STRUCTURE BY NMR OF 1-140.
RX   PubMed=11474112; DOI=10.1126/science.1062950;
RA   Tochio H., Tsui M.M., Banfield D.K., Zhang M.;
RT   "An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the
RT   structure of Ykt6p.";
RL   Science 293:698-702(2001).
CC   -!- INTERACTION:
CC       P36015; P32854: PEP12; NbExp=2; IntAct=EBI-26982, EBI-13098;
CC       P36015; Q04338: VTI1; NbExp=6; IntAct=EBI-26982, EBI-20519;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; Z28196; CAA82040.1; -; Genomic_DNA.
DR   EMBL; AY558393; AAS56719.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08970.1; -; Genomic_DNA.
DR   PIR; S38033; S38033.
DR   RefSeq; NP_012725.1; NM_001179762.1.
DR   PDB; 1H8M; NMR; -; A=1-140.
DR   PDB; 1IOU; NMR; -; A=1-140.
DR   PDB; 3BW6; X-ray; 2.50 A; A=1-140.
DR   PDBsum; 1H8M; -.
DR   PDBsum; 1IOU; -.
DR   PDBsum; 3BW6; -.
DR   AlphaFoldDB; P36015; -.
DR   SMR; P36015; -.
DR   BioGRID; 33925; 560.
DR   ComplexPortal; CPX-1855; Golgi SNARE complex SED5-GOS1-SFT1-YKT6.
DR   ComplexPortal; CPX-1887; Vacuolar SNARE complex VAM3-VTI1-VAM7-YKT6.
DR   ComplexPortal; CPX-5421; Endosomal SNARE complex PEP12-VTI1-SYN8-YKT6.
DR   ComplexPortal; CPX-5422; Endosomal SNARE complex PEP12-VTI1-TLG1-YKT6.
DR   DIP; DIP-2247N; -.
DR   IntAct; P36015; 28.
DR   MINT; P36015; -.
DR   STRING; 4932.YKL196C; -.
DR   CarbonylDB; P36015; -.
DR   iPTMnet; P36015; -.
DR   MaxQB; P36015; -.
DR   PaxDb; P36015; -.
DR   PRIDE; P36015; -.
DR   EnsemblFungi; YKL196C_mRNA; YKL196C; YKL196C.
DR   GeneID; 853638; -.
DR   KEGG; sce:YKL196C; -.
DR   SGD; S000001679; YKT6.
DR   VEuPathDB; FungiDB:YKL196C; -.
DR   eggNOG; KOG0861; Eukaryota.
DR   GeneTree; ENSGT00390000015164; -.
DR   HOGENOM; CLU_074848_0_1_1; -.
DR   InParanoid; P36015; -.
DR   OMA; ITDHEYP; -.
DR   BioCyc; YEAST:G3O-31958-MON; -.
DR   Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR   Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-SCE-6811438; Intra-Golgi traffic.
DR   EvolutionaryTrace; P36015; -.
DR   PRO; PR:P36015; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36015; protein.
DR   GO; GO:0000421; C:autophagosome membrane; IC:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR   GO; GO:0005768; C:endosome; IDA:SGD.
DR   GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR   GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:1990674; C:Golgi cis cisterna membrane; IC:ComplexPortal.
DR   GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR   GO; GO:0005774; C:vacuolar membrane; IC:ComplexPortal.
DR   GO; GO:0016409; F:palmitoyltransferase activity; IDA:SGD.
DR   GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR   GO; GO:0061911; P:amphisome-lysosome fusion; IC:ComplexPortal.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:ComplexPortal.
DR   GO; GO:0006895; P:Golgi to endosome transport; IC:ComplexPortal.
DR   GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IC:ComplexPortal.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IDA:ComplexPortal.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR   GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR   GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IC:ComplexPortal.
DR   CDD; cd14824; Longin; 1.
DR   CDD; cd15867; R-SNARE_YKT6; 1.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR010908; Longin_dom.
DR   InterPro; IPR045848; R-SNARE_YKT6.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR042855; V_SNARE_CC.
DR   Pfam; PF13774; Longin; 1.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   SMART; SM01270; Longin; 1.
DR   SUPFAM; SSF64356; SSF64356; 1.
DR   PROSITE; PS50859; LONGIN; 1.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Coiled coil; Lipoprotein; Membrane;
KW   Methylation; Palmitate; Phosphoprotein; Prenylation; Reference proteome;
KW   Transferase.
FT   CHAIN           1..197
FT                   /note="Synaptobrevin homolog YKT6"
FT                   /id="PRO_0000206781"
FT   PROPEP          198..200
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396675"
FT   DOMAIN          7..129
FT                   /note="Longin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT   DOMAIN          140..200
FT                   /note="v-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT   MOD_RES         158
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         197
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           196
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           197
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   STRAND          17..23
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:1H8M"
FT   TURN            30..34
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   HELIX           35..50
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   STRAND          64..70
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   STRAND          74..82
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   HELIX           87..104
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   HELIX           107..109
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   HELIX           124..131
FT                   /evidence="ECO:0007829|PDB:3BW6"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:1IOU"
SQ   SEQUENCE   200 AA;  22707 MW;  9BA0E47ED87B096D CRC64;
     MRIYYIGVFR SGGEKALELS EVKDLSQFGF FERSSVGQFM TFFAETVASR TGAGQRQSIE
     EGNYIGHVYA RSEGICGVLI TDKEYPVRPA YTLLNKILDE YLVAHPKEEW ADVTETNDAL
     KMKQLDTYIS KYQDPSQADA IMKVQQELDE TKIVLHKTIE NVLQRGEKLD NLVDKSESLT
     ASSKMFYKQA KKSNSCCIIM
 
 
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