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STX7_BOVIN
ID   STX7_BOVIN              Reviewed;         261 AA.
AC   Q3ZBT5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Syntaxin-7;
GN   Name=STX7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in protein trafficking from the plasma
CC       membrane to the early endosome (EE) as well as in homotypic fusion of
CC       endocytic organelles. Mediates the endocytic trafficking from early
CC       endosomes to late endosomes and lysosomes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms a SNARE complex with VTI1B, STX8 and VAMP8 which
CC       functions in the homotypic fusion of late endosomes. Component of the
CC       SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required
CC       for heterotypic fusion of late endosomes with lysosomes. Interacts with
CC       VPS11, VPS16 and VPS18. Interacts with VPS33A (By similarity).
CC       Interacts with TPC1 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:O70439}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-
CC       pass type IV membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; BC103116; AAI03117.1; -; mRNA.
DR   RefSeq; NP_001071332.1; NM_001077864.1.
DR   AlphaFoldDB; Q3ZBT5; -.
DR   SMR; Q3ZBT5; -.
DR   STRING; 9913.ENSBTAP00000022780; -.
DR   PaxDb; Q3ZBT5; -.
DR   PRIDE; Q3ZBT5; -.
DR   Ensembl; ENSBTAT00000022780; ENSBTAP00000022780; ENSBTAG00000017139.
DR   GeneID; 507031; -.
DR   KEGG; bta:507031; -.
DR   CTD; 8417; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017139; -.
DR   VGNC; VGNC:35443; STX7.
DR   eggNOG; KOG0811; Eukaryota.
DR   GeneTree; ENSGT01000000214440; -.
DR   HOGENOM; CLU_059257_1_1_1; -.
DR   InParanoid; Q3ZBT5; -.
DR   OMA; HMENGLN; -.
DR   OrthoDB; 1204812at2759; -.
DR   TreeFam; TF315607; -.
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000017139; Expressed in nasopharynx and 104 other tissues.
DR   ExpressionAtlas; Q3ZBT5; baseline and differential.
DR   GO; GO:0042582; C:azurophil granule; IEA:Ensembl.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0070820; C:tertiary granule; IEA:Ensembl.
DR   GO; GO:0019869; F:chloride channel inhibitor activity; IEA:Ensembl.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0070925; P:organelle assembly; IEA:Ensembl.
DR   GO; GO:1902685; P:positive regulation of receptor localization to synapse; IEA:Ensembl.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   CDD; cd00179; SynN; 1.
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   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Endosome; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   CHAIN           2..261
FT                   /note="Syntaxin-7"
FT                   /id="PRO_0000284073"
FT   TOPO_DOM        2..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..261
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          165..227
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          129..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          47..69
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         4
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         79
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O70439"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70439"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15400"
SQ   SEQUENCE   261 AA;  29656 MW;  953C8660A2472F88 CRC64;
     MSYTPGVGGD PAQLAQRISS NIQKITQCSA EIQRTLNQLG TPQDSPELRQ QLQQKQQYTN
     QLAKETDKYI KEFGSLPTTP SDQRQRKIQK DRLVAEFTAS LTNFQKVQRQ AAEREKEFVA
     RVRASSRVSG GFPEESSKER NLVSWESQTQ PQAQLQDEEI TEDDLRLIQE RESSIRQLEA
     DIMDINEIFK DLGMMIHEQG DVIDSIEANV ENAEVHVQQA NQQLSRAADY QRKSRKTLCI
     IIFILVIGVV IIGLIIWGVK G
 
 
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