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SNC1_YEAST
ID   SNC1_YEAST              Reviewed;         117 AA.
AC   P31109; D6VPI8;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Synaptobrevin homolog 1;
GN   Name=SNC1; OrderedLocusNames=YAL030W;
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=1316605; DOI=10.1073/pnas.89.10.4338;
RA   Gerst J.E., Rodgers L., Riggs M., Wigler M.;
RT   "SNC1, a yeast homolog of the synaptic vesicle-associated membrane
RT   protein/synaptobrevin gene family: genetic interactions with the RAS and
RT   CAP genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:4338-4342(1992).
RN   [2]
RP   ERRATUM OF PUBMED:1316605.
RA   Gerst J.E., Rodgers L., Riggs M., Wigler M.;
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7287-7287(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-63, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [6]
RP   PALMITOYLATION AT CYS-95.
RX   PubMed=15973437; DOI=10.1038/sj.emboj.7600724;
RA   Valdez-Taubas J., Pelham H.R.B.;
RT   "Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its
RT   ubiquitination and degradation.";
RL   EMBO J. 24:2524-2532(2005).
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: SNC1 and SNC2 are vesicle-targeting proteins essential for
CC       normal secretory traffic between the Golgi and the plasma membrane.
CC       They may also be involved in vesicle fusion.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Single-pass type IV membrane
CC       protein. Note=Post-Golgi vesicle membrane. {ECO:0000305}.
CC   -!- PTM: Palmitoylated by SWF1. {ECO:0000269|PubMed:15973437}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; M91157; AAA35069.1; -; Genomic_DNA.
DR   EMBL; U12980; AAC05002.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06958.1; -; Genomic_DNA.
DR   PIR; S31250; S31250.
DR   RefSeq; NP_009372.1; NM_001178175.1.
DR   PDB; 3B5N; X-ray; 1.60 A; A/E/I=27-86.
DR   PDBsum; 3B5N; -.
DR   AlphaFoldDB; P31109; -.
DR   BMRB; P31109; -.
DR   SMR; P31109; -.
DR   BioGRID; 31736; 76.
DR   ComplexPortal; CPX-1365; Vesicular SNARE complex SSO1-SEC9-SNC1.
DR   ComplexPortal; CPX-1369; Vesicular SNARE complex SSO2-SEC9-SNC1.
DR   ComplexPortal; CPX-5322; Endosomal SNARE complex TLG2-VTI1-TLG1-SNC1.
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-5464; Vesicular SNARE complex SSO1-SPO20-SNC1.
DR   DIP; DIP-2495N; -.
DR   IntAct; P31109; 4.
DR   STRING; 4932.YAL030W; -.
DR   iPTMnet; P31109; -.
DR   SwissPalm; P31109; -.
DR   MaxQB; P31109; -.
DR   PaxDb; P31109; -.
DR   PRIDE; P31109; -.
DR   EnsemblFungi; YAL030W_mRNA; YAL030W; YAL030W.
DR   GeneID; 851203; -.
DR   KEGG; sce:YAL030W; -.
DR   SGD; S000000028; SNC1.
DR   VEuPathDB; FungiDB:YAL030W; -.
DR   eggNOG; KOG0860; Eukaryota.
DR   GeneTree; ENSGT00940000155005; -.
DR   HOGENOM; CLU_064620_2_1_1; -.
DR   InParanoid; P31109; -.
DR   OMA; NIDNMTR; -.
DR   BioCyc; YEAST:G3O-28841-MON; -.
DR   Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-SCE-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   EvolutionaryTrace; P31109; -.
DR   PRO; PR:P31109; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P31109; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005933; C:cellular bud; HDA:SGD.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005768; C:endosome; IDA:SGD.
DR   GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR   GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0005628; C:prospore membrane; IC:ComplexPortal.
DR   GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR   GO; GO:0030658; C:transport vesicle membrane; IDA:SGD.
DR   GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR   GO; GO:0000149; F:SNARE binding; IPI:CAFA.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0031321; P:ascospore-type prospore assembly; IC:ComplexPortal.
DR   GO; GO:0006897; P:endocytosis; IMP:SGD.
DR   GO; GO:0006887; P:exocytosis; IMP:SGD.
DR   GO; GO:0006895; P:Golgi to endosome transport; IC:ComplexPortal.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:SGD.
DR   GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IC:ComplexPortal.
DR   GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IC:ComplexPortal.
DR   GO; GO:0035493; P:SNARE complex assembly; IMP:CAFA.
DR   GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR   GO; GO:0099500; P:vesicle fusion to plasma membrane; IC:ComplexPortal.
DR   GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IC:ComplexPortal.
DR   DisProt; DP00113; -.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR016444; Synaptobrevin/VAMP.
DR   InterPro; IPR042855; V_SNARE_CC.
DR   PANTHER; PTHR45701; PTHR45701; 1.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Isopeptide bond; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   CHAIN           1..117
FT                   /note="Synaptobrevin homolog 1"
FT                   /id="PRO_0000206744"
FT   TOPO_DOM        1..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..111
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..117
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..88
FT                   /note="v-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           95
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:15973437"
FT   CROSSLNK        63
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   HELIX           27..85
FT                   /evidence="ECO:0007829|PDB:3B5N"
SQ   SEQUENCE   117 AA;  13201 MW;  662C3DB5C8D44A94 CRC64;
     MSSSTPFDPY ALSEHDEERP QNVQSKSRTA ELQAEIDDTV GIMRDNINKV AERGERLTSI
     EDKADNLAVS AQGFKRGANR VRKAMWYKDL KMKMCLALVI IILLVVIIVP IAVHFSR
 
 
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