VAMP2_MACMU
ID VAMP2_MACMU Reviewed; 116 AA.
AC Q9N0Y0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Vesicle-associated membrane protein 2;
DE Short=VAMP-2;
DE AltName: Full=Synaptobrevin-2;
GN Name=VAMP2; Synonyms=SYB2;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hippocampus;
RA Jensen M.J., Smith L.A.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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; AF240769; AAF64476.1; -; mRNA.
DR RefSeq; NP_001027992.1; NM_001032820.2.
DR AlphaFoldDB; Q9N0Y0; -.
DR BMRB; Q9N0Y0; -.
DR SMR; Q9N0Y0; -.
DR STRING; 9544.ENSMMUP00000024413; -.
DR Ensembl; ENSMMUT00000107313; ENSMMUP00000072536; ENSMMUG00000021798.
DR GeneID; 574134; -.
DR KEGG; mcc:574134; -.
DR CTD; 6844; -.
DR VEuPathDB; HostDB:ENSMMUG00000021798; -.
DR VGNC; VGNC:75942; PER1.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000159217; -.
DR InParanoid; Q9N0Y0; -.
DR OMA; CQDTFAT; -.
DR OrthoDB; 1606985at2759; -.
DR TreeFam; TF313666; -.
DR Proteomes; UP000006718; Chromosome 16.
DR Bgee; ENSMMUG00000021798; Expressed in primary visual cortex and 21 other tissues.
DR ExpressionAtlas; Q9N0Y0; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
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:0006906; P:vesicle fusion; ISS:UniProtKB.
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 3: Inferred from homology;
KW Acetylation; Cell membrane; Coiled coil; Cytoplasmic vesicle; Membrane;
KW Phosphoprotein; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63026"
FT CHAIN 2..116
FT /note="Vesicle-associated membrane protein 2"
FT /id="PRO_0000206724"
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:0000250|UniProtKB:P63026"
SQ SEQUENCE 116 AA; 12663 MW; 9CD679C4F6F1B5A8 CRC64;
MSATAATAPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL
SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST
