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VAMP2_BOVIN
ID   VAMP2_BOVIN             Reviewed;         116 AA.
AC   P63026; P19065; Q9TRF2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Vesicle-associated membrane protein 2;
DE            Short=VAMP-2;
DE   AltName: Full=Synaptobrevin-2;
GN   Name=VAMP2; Synonyms=SYB2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2560644; DOI=10.1016/0896-6273(89)90193-1;
RA   Suedhof T.C., Baumert M., Perin M.S., Jahn R.;
RT   "A synaptic vesicle membrane protein is conserved from mammals to
RT   Drosophila.";
RL   Neuron 2:1475-1481(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 32-60 AND 68-83, AND ACETYLATION AT SER-2.
RX   PubMed=8455717; DOI=10.1038/362318a0;
RA   Soellner T., Whiteheart S.W., Brunner M., Erdjument-Bromage H.,
RA   Geromanos S., Tempst P., Rothman J.E.;
RT   "SNAP receptors implicated in vesicle targeting and fusion.";
RL   Nature 362:318-324(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 48-79.
RC   TISSUE=Brain;
RX   PubMed=8365494; DOI=10.1016/0014-5793(93)80281-x;
RA   Horikawa H.P., Saisu H., Ishizuka T., Sekine Y., Tsugita A., Odani S.,
RA   Abe T.;
RT   "A complex of rab3A, SNAP-25, VAMP/synaptobrevin-2 and syntaxins in brain
RT   presynaptic terminals.";
RL   FEBS Lett. 330:236-240(1993).
CC   -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC       to their target membrane (By similarity). Major SNARE protein of
CC       synaptic vesicles which mediates fusion of synaptic vesicles to release
CC       neurotransmitters. Essential for fast vesicular exocytosis and
CC       activity-dependent neurotransmitter release as well as fast endocytosis
CC       that mediates rapid reuse of synaptic vesicles (By similarity).
CC       Modulates the gating characteristics of the delayed rectifier voltage-
CC       dependent potassium channel KCNB1 (By similarity).
CC       {ECO:0000250|UniProtKB:P63027, ECO:0000250|UniProtKB:P63044,
CC       ECO:0000250|UniProtKB:P63045}.
CC   -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC       STX1A. This complex binds to CPLX1. Interacts with BVES and STX4 (By
CC       similarity). Interacts with VAPA and VAPB. Interacts with WDFY2, PRKCZ
CC       and PRKCI. Forms a complex with WDFY2 and PRKCZ (By similarity).
CC       Interacts (via N-terminus) with KCNB1 (via N-terminus and C-terminus);
CC       stimulates the channel inactivation rate of KCNB1 (By similarity).
CC       Interacts with SEPT8; the interaction inhibits interaction of VAMP2
CC       with SYP. Interacts with SYP; the interaction is inhibited by
CC       interaction with SEPT8 (By similarity). Interacts with PICALM.
CC       Interacts with alpha-synuclein/SNCA (By similarity). Interacts with
CC       STX3 (By similarity). {ECO:0000250|UniProtKB:P63027,
CC       ECO:0000250|UniProtKB:P63044, ECO:0000250|UniProtKB:P63045}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250|UniProtKB:P63027}; Single-pass type IV
CC       membrane protein {ECO:0000255}. Cell membrane
CC       {ECO:0000250|UniProtKB:P63045}. Note=Colocalizes with PRKCZ and WDFY2
CC       in intracellular vesicles. {ECO:0000250|UniProtKB:P63027}.
CC   -!- PTM: Phosphorylated by PRKCZ in vitro and this phosphorylation is
CC       increased in the presence of WDFY2. {ECO:0000250|UniProtKB:P63027}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; X76199; CAA53792.1; -; mRNA.
DR   PIR; JN0011; JN0011.
DR   RefSeq; NP_776908.1; NM_174483.2.
DR   AlphaFoldDB; P63026; -.
DR   BMRB; P63026; -.
DR   SMR; P63026; -.
DR   CORUM; P63026; -.
DR   STRING; 9913.ENSBTAP00000005078; -.
DR   iPTMnet; P63026; -.
DR   PaxDb; P63026; -.
DR   PeptideAtlas; P63026; -.
DR   Ensembl; ENSBTAT00000085421; ENSBTAP00000059351; ENSBTAG00000054934.
DR   GeneID; 282116; -.
DR   KEGG; bta:282116; -.
DR   CTD; 6844; -.
DR   VEuPathDB; HostDB:ENSBTAG00000054934; -.
DR   eggNOG; KOG0860; Eukaryota.
DR   GeneTree; ENSGT00940000158370; -.
DR   HOGENOM; CLU_064620_4_0_1; -.
DR   InParanoid; P63026; -.
DR   OMA; CQDTFAT; -.
DR   OrthoDB; 1606985at2759; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005901; C:caveola; IDA:AgBase.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031201; C:SNARE complex; IDA:AgBase.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IPI:AgBase.
DR   GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR   GO; GO:0017004; P:cytochrome complex assembly; IMP:AgBase.
DR   GO; GO:0043308; P:eosinophil degranulation; IEA:Ensembl.
DR   GO; GO:0031580; P:membrane raft distribution; IMP:AgBase.
DR   GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IMP:AgBase.
DR   GO; GO:0035493; P:SNARE complex assembly; IBA:GO_Central.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:UniProtKB.
DR   GO; GO:0042311; P:vasodilation; IMP:AgBase.
DR   GO; GO:0006906; P:vesicle fusion; IMP:AgBase.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR016444; Synaptobrevin/VAMP.
DR   InterPro; IPR042855; V_SNARE_CC.
DR   InterPro; IPR028717; VAMP2.
DR   PANTHER; PTHR45701; PTHR45701; 1.
DR   PANTHER; PTHR45701:SF5; PTHR45701:SF5; 1.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW   Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW   Synapse; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8455717"
FT   CHAIN           2..116
FT                   /note="Vesicle-associated membrane protein 2"
FT                   /id="PRO_0000206722"
FT   TOPO_DOM        2..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..114
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..116
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..91
FT                   /note="v-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..116
FT                   /note="Required for interaction with SEPT8"
FT                   /evidence="ECO:0000250|UniProtKB:P63045"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:8455717"
SQ   SEQUENCE   116 AA;  12649 MW;  98C679C4F6F1B5A8 CRC64;
     MSATAATAPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL
     SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFSS
 
 
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