STX7_MOUSE
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 25-MAY-2022, entry version 152.
DE RecName: Full=Syntaxin-7;
GN Name=Stx7; Synonyms=Syn7;
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].
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., Hong W.;
RT "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar
RT 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 SER-129, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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; SER-129
RP AND SER-205, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, 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).
RN [7]
RP INTERACTION WITH TPC1.
RX PubMed=28855648; DOI=10.1038/s41598-017-10607-4;
RA Castonguay J., Orth J.H.C., Mueller T., Sleman F., Grimm C.,
RA Wahl-Schott C., Biel M., Mallmann R.T., Bildl W., Schulte U., Klugbauer N.;
RT "The two-pore channel TPC1 is required for efficient protein processing
RT through early and recycling endosomes.";
RL Sci. Rep. 7:10038-10038(2017).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 169-229 IN COMPLEX WITH VAMP8;
RP 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 structural
RT 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 of
CC endocytic organelles. Mediates the endocytic trafficking from early
CC endosomes to late endosomes and lysosomes (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VPS11, VPS16 and VPS18. Interacts with VPS33A
CC (By similarity). 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 TPC1 (PubMed:28855648). {ECO:0000250, ECO:0000269|PubMed:11786915,
CC ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:28855648}.
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; AF056323; AAC15971.1; -; mRNA.
DR CCDS; CCDS23749.1; -.
DR PDB; 1GL2; X-ray; 1.90 A; B=169-228.
DR PDBsum; 1GL2; -.
DR AlphaFoldDB; O70439; -.
DR SMR; O70439; -.
DR CORUM; O70439; -.
DR IntAct; O70439; 5.
DR MINT; O70439; -.
DR STRING; 10090.ENSMUSP00000020174; -.
DR iPTMnet; O70439; -.
DR PhosphoSitePlus; O70439; -.
DR SwissPalm; O70439; -.
DR CPTAC; non-CPTAC-3880; -.
DR EPD; O70439; -.
DR jPOST; O70439; -.
DR MaxQB; O70439; -.
DR PaxDb; O70439; -.
DR PeptideAtlas; O70439; -.
DR PRIDE; O70439; -.
DR ProteomicsDB; 258667; -.
DR TopDownProteomics; O70439; -.
DR MGI; MGI:1858210; Stx7.
DR eggNOG; KOG0811; Eukaryota.
DR InParanoid; O70439; -.
DR PhylomeDB; O70439; -.
DR ChiTaRS; Stx7; mouse.
DR EvolutionaryTrace; O70439; -.
DR PRO; PR:O70439; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70439; protein.
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; IDA: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:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; 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; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; 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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; 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; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Endosome; Iron; Membrane;
KW Phosphoprotein; 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_0000210214"
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 128..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..68
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:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15400"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT HELIX 170..226
FT /evidence="ECO:0007829|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
