VAMP2_XENLA
ID VAMP2_XENLA Reviewed; 114 AA.
AC P47193; Q5D065;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Vesicle-associated membrane protein 2;
DE Short=VAMP-2;
DE AltName: Full=SYBII;
DE AltName: Full=Synaptobrevin-2;
GN Name=vamp2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang X.-H., Poo M.-M.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-114.
RC TISSUE=Embryo;
RX PubMed=7601005; DOI=10.1242/dev.121.6.1927;
RA Knecht A.K., Good P.J., Dawid I.B., Harland R.M.;
RT "Dorsal-ventral patterning and differentiation of noggin-induced neural
RT tissue in the absence of mesoderm.";
RL Development 121:1927-1935(1995).
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 {ECO:0000250|UniProtKB:P63027, ECO:0000250|UniProtKB:P63044,
CC 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}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF035017; AAB88138.1; -; mRNA.
DR EMBL; BC060344; AAH60344.1; -; mRNA.
DR EMBL; BC123114; AAI23115.1; -; mRNA.
DR EMBL; U16801; AAA81376.1; -; mRNA.
DR RefSeq; NP_001080944.1; NM_001087475.1.
DR AlphaFoldDB; P47193; -.
DR BMRB; P47193; -.
DR SMR; P47193; -.
DR MaxQB; P47193; -.
DR DNASU; 394287; -.
DR GeneID; 394287; -.
DR KEGG; xla:394287; -.
DR CTD; 394287; -.
DR Xenbase; XB-GENE-5788238; vamp2.L.
DR OrthoDB; 1606985at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 394287; Expressed in brain and 20 other tissues.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
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 Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..114
FT /note="Vesicle-associated membrane protein 2"
FT /id="PRO_0000206727"
FT TOPO_DOM 2..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..111
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..114
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 29..89
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 114 AA; 12473 MW; AEF2EDDCDF2D1DBF CRC64;
MSAPAAGPPA AAPGDGAPQG PPNLTSNRRL QQTQAQVDEV VDIMRVNVDK VLERDTKLSE
LDDRADALQA GASQFETSAA KLKRKYWWKN MKMMIIMGVI CAIILIIIIV YFST
