VAMP3_RAT
ID VAMP3_RAT Reviewed; 103 AA.
AC P63025; Q64271;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Vesicle-associated membrane protein 3;
DE Short=VAMP-3;
DE AltName: Full=Cellubrevin {ECO:0000303|PubMed:8332193};
DE Short=CEB;
DE AltName: Full=Synaptobrevin-3;
GN Name=Vamp3; Synonyms=Syb3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8332193; DOI=10.1038/364346a0;
RA McMahon H.T., Ushkaryov Y.A., Edelmann L., Link E., Binz T., Niemann H.,
RA Jahn R., Suedhof T.C.;
RT "Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a
RT putative synaptic vesicle fusion protein.";
RL Nature 364:346-349(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPES
RP D AND F AND BY C.TETANI TETANUS TOXIN.
RX PubMed=8175689; DOI=10.1016/s0021-9258(18)99941-2;
RA Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F.,
RA Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H.;
RT "Cleavage of members of the synaptobrevin/VAMP family by types D and F
RT botulinal neurotoxins and tetanus toxin.";
RL J. Biol. Chem. 269:12764-12772(1994).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: SNARE involved in vesicular transport from the late endosomes
CC to the trans-Golgi network. {ECO:0000250|UniProtKB:Q15836}.
CC -!- SUBUNIT: Interacts with BVES (via the C-terminus cytoplasmic tail).
CC Interacts with BCAP31; involved in VAMP3 export from the endoplasmic
CC reticulum (By similarity). Interacts with BAIAP3; this interaction is
CC increased in the presence of calcium (By similarity). Interacts with
CC PICALM (By similarity). {ECO:0000250|UniProtKB:P63024,
CC ECO:0000250|UniProtKB:Q15836}.
CC -!- INTERACTION:
CC P63025; Q9ES83: Bves; Xeno; NbExp=3; IntAct=EBI-7705696, EBI-7705661;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q15836}; Single-pass type IV membrane protein
CC {ECO:0000255}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q15836}; Single-pass type I membrane protein
CC {ECO:0000255}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q15836}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8332193}.
CC -!- PTM: Ubiquitinated by RNF167 at Lys-70, Lys-72 and Lys-81, regulating
CC the recycling endosome pathway. {ECO:0000250|UniProtKB:Q15836}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type D (BoNT/D, botD) which hydrolyzes the 46-Lys-|-Leu-47
CC bond and probably inhibits neurotransmitter release (PubMed:8175689).
CC {ECO:0000269|PubMed:8175689}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type F (BoNT/F, botF) which hydrolyzes the 45-Gln-|-Lys-46
CC bond and probably inhibits neurotransmitter release (PubMed:8175689).
CC {ECO:0000269|PubMed:8175689}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.tetani toxin
CC (tetX) which hydrolyzes the 63-Gln-|-Phe-64 bond and probably inhibits
CC neurotransmitter release (PubMed:8175689).
CC {ECO:0000269|PubMed:8175689}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; S63830; AAB27554.1; -; mRNA.
DR EMBL; BC088119; AAH88119.1; -; mRNA.
DR PIR; S35077; S35077.
DR RefSeq; NP_476438.1; NM_057097.2.
DR PDB; 5KJ7; X-ray; 3.50 A; A/G=14-76.
DR PDB; 5KJ8; X-ray; 4.10 A; A/G=14-76.
DR PDBsum; 5KJ7; -.
DR PDBsum; 5KJ8; -.
DR AlphaFoldDB; P63025; -.
DR BMRB; P63025; -.
DR SMR; P63025; -.
DR BioGRID; 248164; 2.
DR CORUM; P63025; -.
DR IntAct; P63025; 5.
DR MINT; P63025; -.
DR STRING; 10116.ENSRNOP00000048364; -.
DR iPTMnet; P63025; -.
DR PhosphoSitePlus; P63025; -.
DR SwissPalm; P63025; -.
DR jPOST; P63025; -.
DR PaxDb; P63025; -.
DR PRIDE; P63025; -.
DR GeneID; 29528; -.
DR KEGG; rno:29528; -.
DR UCSC; RGD:61880; rat.
DR CTD; 9341; -.
DR RGD; 61880; Vamp3.
DR VEuPathDB; HostDB:ENSRNOG00000030055; -.
DR eggNOG; KOG0860; Eukaryota.
DR HOGENOM; CLU_064620_4_1_1; -.
DR InParanoid; P63025; -.
DR OMA; IIISEWF; -.
DR OrthoDB; 1614157at2759; -.
DR PhylomeDB; P63025; -.
DR TreeFam; TF313666; -.
DR Reactome; R-RNO-1236974; ER-Phagosome pathway.
DR Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:P63025; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000030055; Expressed in duodenum and 19 other tissues.
DR Genevisible; P63025; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0043229; C:intracellular organelle; IDA:RGD.
DR GO; GO:0097708; C:intracellular vesicle; IDA:CACAO.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; IDA:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IPI:RGD.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0017075; F:syntaxin-1 binding; IPI:RGD.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:RGD.
DR GO; GO:1903531; P:negative regulation of secretion by cell; ISO:RGD.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0035493; P:SNARE complex assembly; ISO:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR016444; Synaptobrevin/VAMP.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45701; PTHR45701; 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 3D-structure; Coiled coil; Endosome; Isopeptide bond; Membrane;
KW Protein transport; Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..103
FT /note="Vesicle-associated membrane protein 3"
FT /id="PRO_0000206730"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 18..78
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 44..45
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type F (BoNT/F, botF)"
FT /evidence="ECO:0000269|PubMed:8175689"
FT SITE 46..47
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type D (BoNT/D, botD)"
FT /evidence="ECO:0000269|PubMed:8175689"
FT SITE 63..64
FT /note="(Microbial infection) Cleavage; by C.tetani toxin
FT (tetX)"
FT /evidence="ECO:0000269|PubMed:8175689"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15836"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15836"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15836"
FT HELIX 15..75
FT /evidence="ECO:0007829|PDB:5KJ7"
SQ SEQUENCE 103 AA; 11480 MW; EB502BBE5D0F5981 CRC64;
MSTGVPSGSS AATGSNRRLQ QTQNQVDEVV DIMRVNVDKV LERDQKLSEL DDRADALQAG
ASQFETSAAK LKRKYWWKNC KMWAIGISVL VIIVIIIIVW CVS
