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STX2_MOUSE
ID   STX2_MOUSE              Reviewed;         289 AA.
AC   Q00262;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 146.
DE   RecName: Full=Syntaxin-2;
DE   AltName: Full=Epimorphin;
GN   Name=Stx2; Synonyms=Epim;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1581962; DOI=10.1016/0092-8674(92)90448-l;
RA   Hirai Y., Takebe K., Takashina M., Kobayashi S., Takeichi M.;
RT   "Epimorphin: a mesenchymal protein essential for epithelial
RT   morphogenesis.";
RL   Cell 69:471-481(1992).
RN   [2]
RP   FUNCTION.
RX   PubMed=7957204; DOI=10.1111/j.1432-1033.1994.1133b.x;
RA   Hirai Y.;
RT   "Sodium-dodecyl-sulfate-resistant complex formation of epimorphin monomers
RT   and interaction of the 150-kDa complex with the cell surface.";
RL   Eur. J. Biochem. 225:1133-1139(1994).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH SYT6 AND SYT8.
RX   PubMed=15774481; DOI=10.1074/jbc.m412920200;
RA   Hutt D.M., Baltz J.M., Ngsee J.K.;
RT   "Synaptotagmin VI and VIII and syntaxin 2 are essential for the mouse sperm
RT   acrosome reaction.";
RL   J. Biol. Chem. 280:20197-20203(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Essential for epithelial morphogenesis. May mediate Ca(2+)-
CC       regulation of exocytosis acrosomal reaction in sperm.
CC       {ECO:0000269|PubMed:15774481, ECO:0000269|PubMed:7957204}.
CC   -!- SUBUNIT: Interacts with SYT6 and SYT8; the interaction is Ca(2+)-
CC       dependent. {ECO:0000269|PubMed:15774481}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; D10475; BAA01278.1; -; mRNA.
DR   CCDS; CCDS19692.1; -.
DR   PIR; A38216; S51193.
DR   AlphaFoldDB; Q00262; -.
DR   SMR; Q00262; -.
DR   STRING; 10090.ENSMUSP00000031378; -.
DR   iPTMnet; Q00262; -.
DR   PhosphoSitePlus; Q00262; -.
DR   EPD; Q00262; -.
DR   jPOST; Q00262; -.
DR   MaxQB; Q00262; -.
DR   PaxDb; Q00262; -.
DR   PeptideAtlas; Q00262; -.
DR   PRIDE; Q00262; -.
DR   ProteomicsDB; 254608; -.
DR   MGI; MGI:108059; Stx2.
DR   eggNOG; KOG0810; Eukaryota.
DR   InParanoid; Q00262; -.
DR   PhylomeDB; Q00262; -.
DR   ChiTaRS; Stx2; mouse.
DR   PRO; PR:Q00262; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q00262; protein.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0030496; C:midbody; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:HGNC-UCL.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR   GO; GO:0005198; F:structural molecule activity; ISO:MGI.
DR   GO; GO:0007340; P:acrosome reaction; IDA:HGNC-UCL.
DR   GO; GO:0030154; P:cell differentiation; IDA:MGI.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR   GO; GO:1903575; P:cornified envelope assembly; ISO:MGI.
DR   GO; GO:0048546; P:digestive tract morphogenesis; ISO:MGI.
DR   GO; GO:0007566; P:embryo implantation; IC:MGI.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISO:MGI.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0030033; P:microvillus assembly; ISO:MGI.
DR   GO; GO:0061952; P:midbody abscission; ISO:MGI.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
DR   GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
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; IPR028671; STX2.
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   PANTHER; PTHR19957:SF36; PTHR19957:SF36; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 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; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..289
FT                   /note="Syntaxin-2"
FT                   /id="PRO_0000210197"
FT   TOPO_DOM        1..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..289
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          192..254
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   COILED          68..101
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   289 AA;  33178 MW;  9D82330D0F5CA2F4 CRC64;
     MRDRLPDLTA CRTNDDGDTA VVIVEKDHFM DGFFHQVEEI RSSIARIAQH VEDVKKNHSI
     ILSAPNPEGK IKEELEDLDK EIKKTANRIR GKLKSIEQSC DQDENGNRTS VDLRIRRTQH
     SVLSRKFVDV MTEYNEAQIL FRERSKGRIQ RQLEITGRTT TDDELEEMLE SGKPSIFISD
     IISDSQITRQ ALNEIESRHK DIMKLETSIR ELHEMFMDMA MFVETQGEMV NNIERNVVNS
     VDYVEHAKEE TKKAIKYQSK ARRKKWIIAA VAVAVIAVLA LIIGLSVGK
 
 
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