ID VAM2_MOUSE STANDARD; PRT; 115 AA. AC Q64357; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Vesicle-associated membrane protein 2 (VAMP-2) (Synaptobrevin 2). GN VAMP2 OR SYB2. OS Mus musculus (Mouse), and OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090, 10116; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Rat; RX MEDLINE=89291844; PubMed=2472388; RA Elferink L.A., Trimble W.S., Scheller R.H.; RT "Two vesicle-associated membrane protein genes are differentially RT expressed in the rat central nervous system."; RL J. Biol. Chem. 264:11061-11064(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RX MEDLINE=98104125; PubMed=9430681; RA Martin L.B., Shewan A., Millar C.A., Gould G.W., James D.E.; RT "Vesicle-associated membrane protein 2 plays a specific role in the RT insulin-dependent trafficking of the facilitative glucose transporter RT GLUT4 in 3T3-L1 adipocytes."; RL J. Biol. Chem. 273:1444-1452(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-96 IN COMPLEX WITH STX1A RP AND SNAP25. RC SPECIES=Rat; RX MEDLINE=98430524; PubMed=9759724; RA Sutton R.B., Fasshauer D., Jahn R., Brunger A.T.; RT "Crystal structure of a SNARE complex involved in synaptic exocytosis RT at 2.4 A resolution."; RL Nature 395:347-353(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 29-93 IN COMPLEX WITH STX1A; RP CPLX1 AND SNAP25, AND NMR ANALYSIS. RC SPECIES=Rat; RX MEDLINE=21822661; PubMed=11832227; RA Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., RA Suedhof T.C., Rizo J.; RT "Three-dimensional structure of the complexin/SNARE complex."; RL Neuron 33:397-409(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 28-89 IN COMPLEX WITH STX1A RP AND SNAP25. RC SPECIES=Rat; RX MEDLINE=22499607; PubMed=12496247; RA Ernst J.A., Brunger A.T.; RT "High resolution structure, stability, and synaptotagmin binding of a RT truncated neuronal SNARE complex."; RL J. Biol. Chem. 278:8630-8636(2003). CC -!- FUNCTION: Involved in the targeting and/or fusion of transport CC vesicles to their target membrane. CC -!- SUBUNIT: Interacts with VAPA and VAPB (By similarity). Part of the CC SNARE core complex containing SNAP25, VAMP2 and STX1A. This CC complex binds to CPLX1. CC -!- SUBCELLULAR LOCATION: Type IV membrane protein. Neuronal synaptic CC vesicles. CC -!- TISSUE SPECIFICITY: Nervous system specific. A higher level CC expression is seen in the brain as compared to the spinal cord. CC -!- SIMILARITY: Belongs to the synaptobrevin family. CC -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M24105; AAA42321.1; -. DR EMBL; U60150; AAB03463.1; -. DR PIR; B34288; B34288. DR PDB; 1KIL; 13-MAR-02. DR PDB; 1N7S; 27-DEC-02. DR PDB; 1SFC; 29-DEC-99. DR MGD; MGI:1313277; Vamp2. DR InterPro; IPR001388; Synaptobrevin. DR Pfam; PF00957; synaptobrevin; 1. DR PRINTS; PR00219; SYNAPTOBREVN. DR ProDom; PD001229; Synaptobrevin; 1. DR PROSITE; PS00417; SYNAPTOBREVIN; 1. DR PROSITE; PS50892; V_SNARE; 1. KW Synapse; Synaptosome; Transmembrane; Coiled coil; Acetylation; KW Polymorphism; Multigene family; 3D-structure. FT INIT_MET 0 0 BY SIMILARITY. FT DOMAIN 1 93 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 94 113 ANCHOR FOR TYPE IV MEMBRANE PROTEIN FT (POTENTIAL). FT DOMAIN 114 115 VESICULAR (POTENTIAL). FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT DOMAIN 30 90 V-SNARE COILED-COIL HOMOLOGY. FT VARIANT 110 110 I -> II. FT VARIANT 111 111 V -> I. SQ SEQUENCE 115 AA; 12559 MW; EA400D6291ABF0BC CRC64; SATAATVPPA APAGEGGPPA PPPNLTSNRR LQQTQAQVDE VVDIMRVNVD KVLERDQKLS ELDDRADALQ AGASQFETSA AKLKRKYWWK NLKMMIILGV ICAIILIIII VYFST //