ID   STX7_MOUSE              Reviewed;         261 AA.
AC   O70439;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-SEP-2015, entry version 122.
DE   RecName: Full=Syntaxin-7;
GN   Name=Stx7; Synonyms=Syn7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adipocyte;
RA   Tellam J., Piper R.C., Smith C., James D.E.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION IN A COMPLEX WITH VAMP8 AND VTI1B.
RX   PubMed=15363411; DOI=10.1016/j.devcel.2004.08.002;
RA   Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F.,
RA   Hong W.;
RT   "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic
RT   acinar cells.";
RL   Dev. Cell 7:359-371(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-126 AND
RP   SER-129, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-79; SER-126;
RP   SER-129 AND SER-205, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-79 AND SER-129,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
RC   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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 169-229 IN COMPLEX WITH
RP   VAMP8; STX8 AND VTI1B.
RX   PubMed=11786915; DOI=10.1038/nsb746;
RA   Antonin W., Fasshauer D., Becker S., Jahn R., Schneider T.R.;
RT   "Crystal structure of the endosomal SNARE complex reveals common
RT   structural principles of all SNAREs.";
RL   Nat. Struct. Biol. 9:107-111(2002).
CC   -!- FUNCTION: May be involved in protein trafficking from the plasma
CC       membrane to the early endosome (EE) as well as in homotypic fusion
CC       of endocytic organelles. Mediates the endocytic trafficking from
CC       early endosomes to late endosomes and lysosomes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with VPS11, VPS16 and VPS18. Interacts with
CC       VPS33A (By similarity). Forms a SNARE complex with VTI1B, STX8 and
CC       VAMP8 which functions in the homotypic fusion of late endosomes.
CC       Component of the SNARE complex composed of STX7, STX8, VAMP7 and
CC       VTI1B that is required for heterotypic fusion of late endosomes
CC       with lysosomes. {ECO:0000250, ECO:0000269|PubMed:11786915,
CC       ECO:0000269|PubMed:15363411}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250};
CC       Single-pass type IV membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00202}.
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DR   EMBL; AF056323; AAC15971.1; -; mRNA.
DR   CCDS; CCDS23749.1; -.
DR   UniGene; Mm.248042; -.
DR   PDB; 1GL2; X-ray; 1.90 A; B=169-228.
DR   PDBsum; 1GL2; -.
DR   ProteinModelPortal; O70439; -.
DR   SMR; O70439; 10-259.
DR   IntAct; O70439; 6.
DR   MINT; MINT-1870254; -.
DR   STRING; 10090.ENSMUSP00000020174; -.
DR   PhosphoSite; O70439; -.
DR   MaxQB; O70439; -.
DR   PaxDb; O70439; -.
DR   PRIDE; O70439; -.
DR   MGI; MGI:1858210; Stx7.
DR   eggNOG; COG5325; -.
DR   HOGENOM; HOG000188453; -.
DR   HOVERGEN; HBG053083; -.
DR   InParanoid; O70439; -.
DR   PhylomeDB; O70439; -.
DR   ChiTaRS; Stx7; mouse.
DR   EvolutionaryTrace; O70439; -.
DR   PRO; PR:O70439; -.
DR   Proteomes; UP000000589; Unplaced.
DR   CleanEx; MM_STX7; -.
DR   GO; GO:0042582; C:azurophil granule; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0001772; C:immunological synapse; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005770; C:late endosome; ISO:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR   GO; GO:0005764; C:lysosome; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0070820; C:tertiary granule; ISO:MGI.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0019869; F:chloride channel inhibitor activity; 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:0019905; F:syntaxin binding; ISO:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0070925; P:organelle assembly; ISO:MGI.
DR   GO; GO:0051640; P:organelle localization; ISO:MGI.
DR   GO; GO:1902685; P:positive regulation of receptor localization to synapse; ISO:MGI.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISO:MGI.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF05739; SNARE; 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   3D-structure; Acetylation; Coiled coil; Complete proteome; Endosome;
KW   Iron; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:O15400}.
FT   CHAIN         2    261       Syntaxin-7.
FT                                /FTId=PRO_0000210214.
FT   TOPO_DOM      2    238       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    239    259       Helical; Anchor for type IV membrane
FT                                protein. {ECO:0000255}.
FT   TOPO_DOM    260    261       Vesicular. {ECO:0000255}.
FT   DOMAIN      165    227       t-SNARE coiled-coil homology.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00202}.
FT   COILED       47     68       {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000250|UniProtKB:O15400}.
FT   MOD_RES      45     45       Phosphoserine.
FT                                {ECO:0000244|PubMed:19144319,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES      79     79       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19144319,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     125    125       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355}.
FT   MOD_RES     126    126       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:19144319}.
FT   MOD_RES     129    129       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:19144319,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     205    205       Phosphoserine.
FT                                {ECO:0000244|PubMed:19144319}.
FT   HELIX       170    226       {ECO:0000244|PDB:1GL2}.
SQ   SEQUENCE   261 AA;  29821 MW;  62F4E4B33F247ADB CRC64;
     MSYTPGIGGD SAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ LLQQKQQYTN
     QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS LTNFQKAQRQ AAEREKEFVA
     RVRASSRVSG GFPEDSSKEK NLVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA
     DIMDINEIFK DLGMMIHEQG DMIDSIEANV ESAEVHVQQA NQQLSRAADY QRKSRKTLCI
     IIFILVVRIV IICLIVWGLK G
//