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 19-JAN-2010, entry version 81. 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. 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASS RP SPECTROMETRY. RC TISSUE=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 THR-79, AND MASS RP SPECTROMETRY. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in RT naive and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-126 AND RP SER-129, AND MASS SPECTROMETRY. 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-129 AND SER-205, RP AND MASS SPECTROMETRY. RC TISSUE=Macrophage; 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 [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 169-229 IN COMPLEX WITH RP VAMP8; STX8 AND VTI1B. RX MEDLINE=21671743; 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 -!- SUBUNIT: Part of the SNARE core complex containing VAMP8, STX8 and CC VTI1B. Found in a complex with VAMP8 and VTI1B in the liver. Forms CC a SNARE complex with VTI1B, STX8 and VAMP8 which functions in the CC homotypic fusion of late endosomes. Interacts with VPS11, VPS16, CC VPS18 and VPS33A (By similarity). CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Single-pass type IV CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the syntaxin family. CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF056323; AAC15971.1; -; mRNA. DR IPI; IPI00118217; -. DR UniGene; Mm.248042; -. DR PDB; 1GL2; X-ray; 1.90 A; B=169-228. DR PDBsum; 1GL2; -. DR SMR; O70439; 8-126, 14-199. DR IntAct; O70439; 2. DR STRING; O70439; -. DR PhosphoSite; O70439; -. DR PRIDE; O70439; -. DR Ensembl; ENSMUST00000020174; ENSMUSP00000020174; ENSMUSG00000019998; Mus musculus. DR MGI; MGI:1858210; Stx7. DR eggNOG; roNOG10770; -. DR HOGENOM; HBG444570; -. DR HOVERGEN; O70439; -. DR InParanoid; O70439; -. DR PhylomeDB; O70439; -. DR ArrayExpress; O70439; -. DR Bgee; O70439; -. DR CleanEx; MM_STX7; -. DR Genevestigator; O70439; -. DR GermOnline; ENSMUSG00000019998; Mus musculus. DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro. 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 Pfam; PF00804; Syntaxin; 1. DR SMART; SM00503; SynN; 1. DR SMART; SM00397; t_SNARE; 1. DR PROSITE; PS00914; SYNTAXIN; 1. DR PROSITE; PS50192; T_SNARE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Coiled coil; Endosome; Iron; Membrane; KW Phosphoprotein; Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 261 Syntaxin-7. FT /FTId=PRO_0000210214. FT TOPO_DOM 2 238 Cytoplasmic (Potential). FT TRANSMEM 239 259 Anchor for type IV membrane protein FT (Potential). FT TOPO_DOM 260 261 Vesicular (Potential). FT DOMAIN 165 227 t-SNARE coiled-coil homology. FT COILED 47 68 Potential. FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 3 3 Phosphotyrosine (By similarity). FT MOD_RES 45 45 Phosphoserine. FT MOD_RES 79 79 Phosphothreonine. FT MOD_RES 125 125 Phosphoserine. FT MOD_RES 126 126 Phosphoserine. FT MOD_RES 129 129 Phosphoserine. FT MOD_RES 205 205 Phosphoserine. FT HELIX 170 226 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 //