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STX8_YEAST
ID   STX8_YEAST              Reviewed;         255 AA.
AC   P31377; D6VPK4;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Syntaxin-8;
DE   AltName: Full=SNARE protein related to mammalian syntaxin 8;
DE   AltName: Full=ULP1-interacting protein 2;
GN   Name=SYN8; Synonyms=UIP2; OrderedLocusNames=YAL014C; ORFNames=FUN34;
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH PEP12; VTI1 AND SNC.
RC   STRAIN=ATCC 201389 / BY4742;
RX   PubMed=12453154; DOI=10.1034/j.1600-0854.2002.31207.x;
RA   Lewis M.J., Pelham H.R.B.;
RT   "A new yeast endosomal SNARE related to mammalian syntaxin 8.";
RL   Traffic 3:922-929(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RA   Burri L., Hofmann K., Lithgow T.;
RT   "Re-sequencing of the UIP2 gene reveals a frame-correction and a new Qc-
RT   SNARE in the endosome of Saccharomyces cerevisiae.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8458570; DOI=10.1139/g93-005;
RA   Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA   Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT   "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT   kb region between the LTE1 and SPO7 genes.";
RL   Genome 36:32-42(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8144453; DOI=10.1128/jb.176.7.1872-1880.1994;
RA   Barton A.B., Kaback D.B.;
RT   "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae:
RT   analysis of the genes in the FUN38-MAK16-SPO7 region.";
RL   J. Bacteriol. 176:1872-1880(1994).
RN   [5]
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   [6]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Dolinski K.J., Cherry J.M.;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   [8]
RP   PALMITOYLATION AT CYS-238.
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   [9]
RP   PALMITOYLATION.
RX   PubMed=16751107; DOI=10.1016/j.cell.2006.03.042;
RA   Roth A.F., Wan J., Bailey A.O., Sun B., Kuchar J.A., Green W.N.,
RA   Phinney B.S., Yates J.R. III, Davis N.G.;
RT   "Global analysis of protein palmitoylation in yeast.";
RL   Cell 125:1003-1013(2006).
CC   -!- FUNCTION: t-SNARE which may play a role in determining the specificity
CC       of membrane fusion, protein transport and vesicle trafficking within
CC       the Golgi/endosomal and plasma membrane/endosomal systems.
CC       {ECO:0000269|PubMed:12453154}.
CC   -!- SUBUNIT: Interacts with PEP12, VTI1 and the SNC SNARE complex proteins.
CC       {ECO:0000269|PubMed:12453154}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:12453154};
CC       Single-pass type IV membrane protein {ECO:0000269|PubMed:12453154}.
CC   -!- PTM: Palmitoylated by SWF1. {ECO:0000269|PubMed:15973437,
CC       ECO:0000269|PubMed:16751107}.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; AY205237; AAO46883.1; -; Genomic_DNA.
DR   EMBL; AY205236; AAO22142.1; -; Genomic_DNA.
DR   EMBL; L05146; AAC04943.2; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06974.1; -; Genomic_DNA.
DR   PIR; S36720; S36720.
DR   RefSeq; NP_009388.2; NM_001178159.1.
DR   AlphaFoldDB; P31377; -.
DR   SMR; P31377; -.
DR   BioGRID; 31752; 104.
DR   ComplexPortal; CPX-5421; Endosomal SNARE complex PEP12-VTI1-SYN8-YKT6.
DR   ComplexPortal; CPX-5424; Endosomal SNARE complex PEP12-VTI1-SYN8-SNC1.
DR   ComplexPortal; CPX-5461; Endosomal SNARE complex PEP12-VTI1-SYN8-SNC2.
DR   DIP; DIP-5642N; -.
DR   IntAct; P31377; 8.
DR   MINT; P31377; -.
DR   STRING; 4932.YAL014C; -.
DR   SwissPalm; P31377; -.
DR   MaxQB; P31377; -.
DR   PaxDb; P31377; -.
DR   PRIDE; P31377; -.
DR   EnsemblFungi; YAL014C_mRNA; YAL014C; YAL014C.
DR   GeneID; 851219; -.
DR   KEGG; sce:YAL014C; -.
DR   SGD; S000000012; SYN8.
DR   VEuPathDB; FungiDB:YAL014C; -.
DR   eggNOG; ENOG502RZK4; Eukaryota.
DR   HOGENOM; CLU_053570_2_1_1; -.
DR   InParanoid; P31377; -.
DR   OMA; MRQDQDL; -.
DR   BioCyc; YEAST:G3O-28826-MON; -.
DR   Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   PRO; PR:P31377; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P31377; 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; 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; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma 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:0006887; P:exocytosis; IBA:GO_Central.
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:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; PTHR19957; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Endosome; Lipoprotein; Membrane; Palmitate; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..255
FT                   /note="Syntaxin-8"
FT                   /id="PRO_0000210281"
FT   TOPO_DOM        1..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          164..228
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          110..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           238
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:15973437"
SQ   SEQUENCE   255 AA;  29049 MW;  7631FB672F8E55D6 CRC64;
     MDVLKLGYEL DQLSDLVEER TRLVSVLKLA PTSNDNVTLK RQLGSILELL QKCAPNDELI
     SRYNTILDKI PDTAVDKELY RFQQQVARNT DEVSKESLKK VRFKNDDELT VMYKDDDEQD
     EESPLPSTHT PYKDEPLQSQ LQSQSQPQPP QPMVSNQELF INQQQQLLEQ DSHLGALSQS
     IGRTHDISLD LNNEIVSQND SLLVDLENLI DNNGRNLNRA SRSMHGFNNS RFKDNGNCVI
     ILVLIVVLLL LLLVL
 
 
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