VAMP3_MOUSE
ID VAMP3_MOUSE Reviewed; 103 AA.
AC P63024; Q3TH70; Q64271;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Vesicle-associated membrane protein 3;
DE Short=VAMP-3;
DE AltName: Full=Cellubrevin;
DE Short=CEB;
DE AltName: Full=Synaptobrevin-3;
GN Name=Vamp3; Synonyms=Syb3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Martin S., Tellam J.T., Livington C., Slot J.W., Gould G.W., James D.E.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6x129SV/J;
RX PubMed=11238894; DOI=10.1128/mcb.21.5.1573-1580.2001;
RA Yang C.M., Mora S., Ryder J.W., Coker K.J., Hansen P., Allen L.A.,
RA Pessin J.E.;
RT "VAMP3 null mice display normal constitutive, insulin- and exercise-
RT regulated vesicle trafficking.";
RL Mol. Cell. Biol. 21:1573-1580(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Liver, Lung, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 INTERACTION WITH BCAP31.
RX PubMed=9396746; DOI=10.1083/jcb.139.6.1397;
RA Annaert W.G., Becker B., Kistner U., Reth M., Jahn R.;
RT "Export of cellubrevin from the endoplasmic reticulum is controlled by
RT BAP31.";
RL J. Cell Biol. 139:1397-1410(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH BVES.
RX PubMed=20057356; DOI=10.1038/emboj.2009.379;
RA Hager H.A., Roberts R.J., Cross E.E., Proux-Gillardeaux V., Bader D.M.;
RT "Identification of a novel Bves function: regulation of vesicular
RT transport.";
RL EMBO J. 29:532-545(2010).
RN [8]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE
RP X.
RX PubMed=28770820; DOI=10.1038/ncomms14130;
RA Zhang S., Masuyer G., Zhang J., Shen Y., Lundin D., Henriksson L.,
RA Miyashita S.I., Martinez-Carranza M., Dong M., Stenmark P.;
RT "Identification and characterization of a novel botulinum neurotoxin.";
RL Nat. Commun. 8:14130-14130(2017).
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. Interacts with BAIAP3; this interaction is increased in the
CC presence of calcium (By similarity). Interacts with PICALM (By
CC similarity). {ECO:0000250|UniProtKB:Q15836,
CC ECO:0000269|PubMed:20057356, ECO:0000269|PubMed:9396746}.
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 -!- 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 X (BoNT/X) which hydrolyzes the 53-Arg-|-Ala-54 bond
CC and probably inhibits neurotransmitter release (PubMed:28770820). It
CC remains unknown whether BoNT/X is ever produced, or what organisms it
CC targets. {ECO:0000269|PubMed:28770820}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; U60961; AAB03490.1; -; mRNA.
DR EMBL; AF308434; AAG42468.1; -; Genomic_DNA.
DR EMBL; AF308433; AAG42468.1; JOINED; Genomic_DNA.
DR EMBL; AK051272; BAC34586.1; -; mRNA.
DR EMBL; AK051691; BAC34723.1; -; mRNA.
DR EMBL; AK165947; BAE38479.1; -; mRNA.
DR EMBL; AK168413; BAE40328.1; -; mRNA.
DR EMBL; AK169056; BAE40844.1; -; mRNA.
DR EMBL; AK169087; BAE40871.1; -; mRNA.
DR EMBL; BC060045; AAH60045.1; -; mRNA.
DR CCDS; CCDS18979.1; -.
DR RefSeq; NP_033524.1; NM_009498.4.
DR AlphaFoldDB; P63024; -.
DR BMRB; P63024; -.
DR SMR; P63024; -.
DR BioGRID; 204496; 7.
DR CORUM; P63024; -.
DR IntAct; P63024; 3.
DR STRING; 10090.ENSMUSP00000030797; -.
DR iPTMnet; P63024; -.
DR PhosphoSitePlus; P63024; -.
DR SwissPalm; P63024; -.
DR EPD; P63024; -.
DR jPOST; P63024; -.
DR MaxQB; P63024; -.
DR PaxDb; P63024; -.
DR PeptideAtlas; P63024; -.
DR PRIDE; P63024; -.
DR ProteomicsDB; 297908; -.
DR Antibodypedia; 27516; 269 antibodies from 31 providers.
DR DNASU; 22319; -.
DR Ensembl; ENSMUST00000030797; ENSMUSP00000030797; ENSMUSG00000028955.
DR GeneID; 22319; -.
DR KEGG; mmu:22319; -.
DR UCSC; uc008vyj.1; mouse.
DR CTD; 9341; -.
DR MGI; MGI:1321389; Vamp3.
DR VEuPathDB; HostDB:ENSMUSG00000028955; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000158192; -.
DR HOGENOM; CLU_064620_4_1_1; -.
DR InParanoid; P63024; -.
DR OMA; MKMWGIL; -.
DR PhylomeDB; P63024; -.
DR TreeFam; TF313666; -.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 22319; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Vamp3; mouse.
DR PRO; PR:P63024; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P63024; protein.
DR Bgee; ENSMUSG00000028955; Expressed in endothelial cell of lymphatic vessel and 259 other tissues.
DR Genevisible; P63024; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0097708; C:intracellular vesicle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0031201; C:SNARE complex; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IMP:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI.
DR GO; GO:1903531; P:negative regulation of secretion by cell; ISO:MGI.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0035493; P:SNARE complex assembly; IDA:BHF-UCL.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA: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 Coiled coil; Endosome; Isopeptide bond; Membrane; Protein transport;
KW 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_0000206729"
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 53..54
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type X (BoNT/X)"
FT /evidence="ECO:0000269|PubMed:28770820"
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"
SQ SEQUENCE 103 AA; 11480 MW; EB502BBE5D0F5981 CRC64;
MSTGVPSGSS AATGSNRRLQ QTQNQVDEVV DIMRVNVDKV LERDQKLSEL DDRADALQAG
ASQFETSAAK LKRKYWWKNC KMWAIGISVL VIIVIIIIVW CVS
