VAMP3_HUMAN
ID VAMP3_HUMAN Reviewed; 100 AA.
AC Q15836; Q9BRV4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Vesicle-associated membrane protein 3;
DE Short=VAMP-3;
DE AltName: Full=Cellubrevin {ECO:0000303|PubMed:9885218};
DE Short=CEB;
DE AltName: Full=Synaptobrevin-3;
GN Name=VAMP3; Synonyms=SYB3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9885218;
RA Bernstein A.M., Whiteheart S.W.;
RT "Identification of a cellubrevin/vesicle associated membrane protein 3
RT homologue in human platelets.";
RL Blood 93:571-579(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Urinary bladder;
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 [5]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP PROTEIN SEQUENCE OF 42-47 AND 60-64, AND PROTEOLYTIC CLEAVAGE (MICROBIAL
RP INFECTION) BY C.BOTULINUM NEUROTOXIN TYPES B; D AND F.
RX PubMed=22289120; DOI=10.1111/j.1348-0421.2012.00434.x;
RA Yamamoto H., Ida T., Tsutsuki H., Mori M., Matsumoto T., Kohda T.,
RA Mukamoto M., Goshima N., Kozaki S., Ihara H.;
RT "Specificity of botulinum protease for human VAMP family proteins.";
RL Microbiol. Immunol. 56:245-253(2012).
RN [7]
RP FUNCTION.
RX PubMed=18195106; DOI=10.1083/jcb.200707136;
RA Ganley I.G., Espinosa E., Pfeffer S.R.;
RT "A syntaxin 10-SNARE complex distinguishes two distinct transport routes
RT from endosomes to the trans-Golgi in human cells.";
RL J. Cell Biol. 180:159-172(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INTERACTION WITH PICALM.
RX PubMed=22118466; DOI=10.1016/j.cell.2011.10.038;
RA Miller S.E., Sahlender D.A., Graham S.C., Honing S., Robinson M.S.,
RA Peden A.A., Owen D.J.;
RT "The molecular basis for the endocytosis of small R-SNAREs by the clathrin
RT adaptor CALM.";
RL Cell 147:1118-1131(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP INTERACTION WITH BAIAP3.
RX PubMed=28626000; DOI=10.1083/jcb.201702099;
RA Zhang X., Jiang S., Mitok K.A., Li L., Attie A.D., Martin T.F.J.;
RT "BAIAP3, a C2 domain-containing Munc13 protein, controls the fate of dense-
RT core vesicles in neuroendocrine cells.";
RL J. Cell Biol. 216:2151-2166(2017).
RN [15]
RP SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-66; LYS-68 AND LYS-77, AND
RP MUTAGENESIS OF 66-LYS--LYS-68 AND LYS-77.
RX PubMed=23353890; DOI=10.1038/emboj.2013.1;
RA Yamazaki Y., Schoenherr C., Varshney G.K., Dogru M., Hallberg B.,
RA Palmer R.H.;
RT "Goliath family E3 ligases regulate the recycling endosome pathway via
RT VAMP3 ubiquitylation.";
RL EMBO J. 32:524-537(2013).
CC -!- FUNCTION: SNARE involved in vesicular transport from the late endosomes
CC to the trans-Golgi network. {ECO:0000269|PubMed:18195106}.
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 (PubMed:28626000). Interacts with
CC PICALM. {ECO:0000250|UniProtKB:P63024, ECO:0000269|PubMed:22118466,
CC ECO:0000269|PubMed:28626000}.
CC -!- INTERACTION:
CC Q15836; Q8IVF2-3: AHNAK2; NbExp=3; IntAct=EBI-722343, EBI-12078468;
CC Q15836; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-722343, EBI-11957045;
CC Q15836; Q13520: AQP6; NbExp=3; IntAct=EBI-722343, EBI-13059134;
CC Q15836; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-722343, EBI-11343438;
CC Q15836; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-722343, EBI-747430;
CC Q15836; Q13323: BIK; NbExp=3; IntAct=EBI-722343, EBI-700794;
CC Q15836; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-722343, EBI-11532900;
CC Q15836; Q8WZ55: BSND; NbExp=3; IntAct=EBI-722343, EBI-7996695;
CC Q15836; P11912: CD79A; NbExp=3; IntAct=EBI-722343, EBI-7797864;
CC Q15836; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-722343, EBI-752069;
CC Q15836; O95471: CLDN7; NbExp=3; IntAct=EBI-722343, EBI-740744;
CC Q15836; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-722343, EBI-17710733;
CC Q15836; P21964: COMT; NbExp=3; IntAct=EBI-722343, EBI-372265;
CC Q15836; Q15125: EBP; NbExp=3; IntAct=EBI-722343, EBI-3915253;
CC Q15836; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-722343, EBI-18535450;
CC Q15836; P54852: EMP3; NbExp=3; IntAct=EBI-722343, EBI-3907816;
CC Q15836; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-722343, EBI-781551;
CC Q15836; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-722343, EBI-18636064;
CC Q15836; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-722343, EBI-18304435;
CC Q15836; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-722343, EBI-18938272;
CC Q15836; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-722343, EBI-3917143;
CC Q15836; Q8TED1: GPX8; NbExp=3; IntAct=EBI-722343, EBI-11721746;
CC Q15836; Q92993: KAT5; NbExp=3; IntAct=EBI-722343, EBI-399080;
CC Q15836; O95279: KCNK5; NbExp=3; IntAct=EBI-722343, EBI-3934936;
CC Q15836; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-722343, EBI-2820517;
CC Q15836; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-722343, EBI-11742507;
CC Q15836; Q99735: MGST2; NbExp=3; IntAct=EBI-722343, EBI-11324706;
CC Q15836; O14880: MGST3; NbExp=3; IntAct=EBI-722343, EBI-724754;
CC Q15836; O14524-2: NEMP1; NbExp=3; IntAct=EBI-722343, EBI-10969203;
CC Q15836; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-722343, EBI-716063;
CC Q15836; Q53GL0: PLEKHO1; NbExp=3; IntAct=EBI-722343, EBI-949945;
CC Q15836; O14684: PTGES; NbExp=3; IntAct=EBI-722343, EBI-11161398;
CC Q15836; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-722343, EBI-10192441;
CC Q15836; Q96TC7: RMDN3; NbExp=3; IntAct=EBI-722343, EBI-1056589;
CC Q15836; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-722343, EBI-3920694;
CC Q15836; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-722343, EBI-17247926;
CC Q15836; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-722343, EBI-9090795;
CC Q15836; Q14973: SLC10A1; NbExp=3; IntAct=EBI-722343, EBI-3923031;
CC Q15836; O00161: SNAP23; NbExp=2; IntAct=EBI-722343, EBI-745000;
CC Q15836; O95721: SNAP29; NbExp=3; IntAct=EBI-722343, EBI-490676;
CC Q15836; Q16623: STX1A; NbExp=3; IntAct=EBI-722343, EBI-712466;
CC Q15836; P32856-2: STX2; NbExp=3; IntAct=EBI-722343, EBI-11956649;
CC Q15836; Q12846: STX4; NbExp=9; IntAct=EBI-722343, EBI-744942;
CC Q15836; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-722343, EBI-6448756;
CC Q15836; Q53R12: TM4SF20; NbExp=3; IntAct=EBI-722343, EBI-1805798;
CC Q15836; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-722343, EBI-10982110;
CC Q15836; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-722343, EBI-11722971;
CC Q15836; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-722343, EBI-18178701;
CC Q15836; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-722343, EBI-2548832;
CC Q15836; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-722343, EBI-11724433;
CC Q15836; Q9Y320: TMX2; NbExp=3; IntAct=EBI-722343, EBI-6447886;
CC Q15836; O43915: VEGFD; NbExp=4; IntAct=EBI-722343, EBI-11750035;
CC Q15836; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-722343, EBI-744988;
CC Q15836; P61981: YWHAG; NbExp=3; IntAct=EBI-722343, EBI-359832;
CC Q15836; O55012: Picalm; Xeno; NbExp=2; IntAct=EBI-722343, EBI-915601;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:23353890}; Single-pass type IV membrane protein
CC {ECO:0000255}. Recycling endosome membrane
CC {ECO:0000269|PubMed:23353890}; Single-pass type I membrane protein
CC {ECO:0000255}. Synapse, synaptosome {ECO:0000305}.
CC -!- PTM: Ubiquitinated by RNF167 at Lys-66, Lys-68 and Lys-77, regulating
CC the recycling endosome pathway. {ECO:0000269|PubMed:23353890}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type B (BoNT/B, botB) which hydrolyzes the 59-Gln-|-Phe-60
CC bond and probably inhibits neurotransmitter release (PubMed:22289120).
CC {ECO:0000269|PubMed:22289120}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type D (BoNT/D, botD) which hydrolyzes the 42-Lys-|-Leu-43
CC bond and probably inhibits neurotransmitter release (PubMed:22289120).
CC Note that humans are not known to be infected by C.botulinum type D.
CC {ECO:0000269|PubMed:22289120, ECO:0000305}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type F (BoNT/F, botF) which hydrolyzes the 41-Gln-|-Lys-42
CC bond and probably inhibits neurotransmitter release (PubMed:22289120).
CC {ECO:0000269|PubMed:22289120}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; U64520; AAB05814.1; -; mRNA.
DR EMBL; BT007327; AAP35991.1; -; mRNA.
DR EMBL; Z98884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003570; AAH03570.1; -; mRNA.
DR EMBL; BC005941; AAH05941.1; -; mRNA.
DR EMBL; BC007050; AAH07050.1; -; mRNA.
DR CCDS; CCDS88.1; -.
DR RefSeq; NP_004772.1; NM_004781.3.
DR AlphaFoldDB; Q15836; -.
DR SMR; Q15836; -.
DR BioGRID; 114747; 256.
DR CORUM; Q15836; -.
DR DIP; DIP-56422N; -.
DR IntAct; Q15836; 131.
DR MINT; Q15836; -.
DR STRING; 9606.ENSP00000054666; -.
DR TCDB; 1.F.1.1.5; the synaptosomal vesicle fusion pore (svf-pore) family.
DR GlyGen; Q15836; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15836; -.
DR MetOSite; Q15836; -.
DR PhosphoSitePlus; Q15836; -.
DR SwissPalm; Q15836; -.
DR BioMuta; VAMP3; -.
DR DMDM; 2501082; -.
DR EPD; Q15836; -.
DR jPOST; Q15836; -.
DR MassIVE; Q15836; -.
DR PaxDb; Q15836; -.
DR PeptideAtlas; Q15836; -.
DR PRIDE; Q15836; -.
DR ProteomicsDB; 60786; -.
DR TopDownProteomics; Q15836; -.
DR Antibodypedia; 27516; 269 antibodies from 31 providers.
DR DNASU; 9341; -.
DR Ensembl; ENST00000054666.11; ENSP00000054666.6; ENSG00000049245.13.
DR GeneID; 9341; -.
DR KEGG; hsa:9341; -.
DR MANE-Select; ENST00000054666.11; ENSP00000054666.6; NM_004781.4; NP_004772.1.
DR CTD; 9341; -.
DR DisGeNET; 9341; -.
DR GeneCards; VAMP3; -.
DR HGNC; HGNC:12644; VAMP3.
DR HPA; ENSG00000049245; Low tissue specificity.
DR MIM; 603657; gene.
DR neXtProt; NX_Q15836; -.
DR OpenTargets; ENSG00000049245; -.
DR PharmGKB; PA37268; -.
DR VEuPathDB; HostDB:ENSG00000049245; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000158192; -.
DR HOGENOM; CLU_064620_4_1_1; -.
DR InParanoid; Q15836; -.
DR OMA; MKMWGIL; -.
DR OrthoDB; 1606985at2759; -.
DR PhylomeDB; Q15836; -.
DR TreeFam; TF313666; -.
DR PathwayCommons; Q15836; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q15836; -.
DR SIGNOR; Q15836; -.
DR BioGRID-ORCS; 9341; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; VAMP3; human.
DR GeneWiki; VAMP3; -.
DR GenomeRNAi; 9341; -.
DR Pharos; Q15836; Tbio.
DR PRO; PR:Q15836; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15836; protein.
DR Bgee; ENSG00000049245; Expressed in inferior olivary complex and 208 other tissues.
DR ExpressionAtlas; Q15836; baseline and differential.
DR Genevisible; Q15836; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
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:0017156; P:calcium-ion regulated exocytosis; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; TAS:ProtInc.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:Ensembl.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:1903531; P:negative regulation of secretion by cell; IDA:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
DR GO; GO:0035493; P:SNARE complex assembly; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; TAS:ProtInc.
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 Acetylation; Coiled coil; Direct protein sequencing; Endosome;
KW Isopeptide bond; Membrane; Protein transport; Reference proteome; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..100
FT /note="Vesicle-associated membrane protein 3"
FT /id="PRO_0000206728"
FT TOPO_DOM 2..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..100
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 14..74
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT SITE 41..42
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type F (BoNT/F, botF)"
FT /evidence="ECO:0000269|PubMed:22289120"
FT SITE 42..43
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type D (BoNT/D, botD)"
FT /evidence="ECO:0000269|PubMed:22289120"
FT SITE 58..59
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type B (BoNT/B, botB)"
FT /evidence="ECO:0000269|PubMed:22289120"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CROSSLNK 66
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23353890"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23353890"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23353890"
FT MUTAGEN 66..68
FT /note="KLK->RLR: Abolished ubiquitination by RNF167; when
FT associated with R-77."
FT /evidence="ECO:0000269|PubMed:23353890"
FT MUTAGEN 77
FT /note="K->R: Abolished ubiquitination by RNF167; when
FT associated with 66-R--R-68."
FT /evidence="ECO:0000269|PubMed:23353890"
FT CONFLICT 77
FT /note="K -> E (in Ref. 3; AAH05941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 100 AA; 11309 MW; 347E9163157AFF42 CRC64;
MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF
ETSAAKLKRK YWWKNCKMWA IGITVLVIFI IIIIVWVVSS
