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Protein

Vesicle-associated membrane protein 3

Gene

Vamp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network.By similarity

GO - Molecular functioni

  1. SNAP receptor activity Source: GO_Central
  2. SNARE binding Source: GO_Central

GO - Biological processi

  1. calcium ion-dependent exocytosis Source: MGI
  2. Golgi to plasma membrane protein transport Source: MGI
  3. negative regulation of secretion by cell Source: MGI
  4. neurotransmitter secretion Source: GO_Central
  5. positive regulation of receptor recycling Source: UniProtKB
  6. retrograde transport, endosome to Golgi Source: UniProtKB
  7. SNARE complex assembly Source: BHF-UCL
  8. substrate adhesion-dependent cell spreading Source: UniProtKB
  9. vesicle fusion Source: GO_Central
  10. vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-associated membrane protein 3
Short name:
VAMP-3
Alternative name(s):
Cellubrevin
Short name:
CEB
Synaptobrevin-3
Gene namesi
Name:Vamp3
Synonyms:Syb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1321389. Vamp3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8181CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei82 – 10221Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini103 – 1031VesicularSequence Analysis

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. cell junction Source: UniProtKB-KW
  3. cell surface Source: BHF-UCL
  4. clathrin-coated vesicle Source: MGI
  5. clathrin-coated vesicle membrane Source: Ensembl
  6. cytoplasmic vesicle Source: MGI
  7. cytosol Source: UniProtKB
  8. integral component of membrane Source: UniProtKB-KW
  9. intracellular Source: MGI
  10. intracellular membrane-bounded organelle Source: MGI
  11. neuron projection Source: UniProtKB-SubCell
  12. plasma membrane Source: UniProtKB
  13. recycling endosome Source: MGI
  14. secretory granule Source: MGI
  15. SNARE complex Source: MGI
  16. synaptic vesicle Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Membrane, Synapse, Synaptosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 103103Vesicle-associated membrane protein 3PRO_0000206729Add
BLAST

Proteomic databases

MaxQBiP63024.
PaxDbiP63024.
PRIDEiP63024.

PTM databases

PhosphoSiteiP63024.

Expressioni

Gene expression databases

BgeeiP63024.
CleanExiMM_VAMP3.
GenevestigatoriP63024.

Interactioni

Subunit structurei

Interacts with BVES (via the C-terminus cytoplasmic tail). Interacts with BCAP31; involved in VAMP3 export from the endoplasmic reticulum.2 Publications

Protein-protein interaction databases

BioGridi204496. 3 interactions.
IntActiP63024. 3 interactions.
MINTiMINT-4139722.

Structurei

3D structure databases

ProteinModelPortaliP63024.
SMRiP63024. Positions 15-79.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 7861v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the synaptobrevin family.Curated
Contains 1 v-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5143.
GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiP63024.
KOiK13505.
OMAiFTHACAF.
OrthoDBiEOG7MSMRJ.
PhylomeDBiP63024.
TreeFamiTF313666.

Family and domain databases

InterProiIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFiPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTGVPSGSS AATGSNRRLQ QTQNQVDEVV DIMRVNVDKV LERDQKLSEL
60 70 80 90 100
DDRADALQAG ASQFETSAAK LKRKYWWKNC KMWAIGISVL VIIVIIIIVW

CVS
Length:103
Mass (Da):11,480
Last modified:August 31, 2004 - v1
Checksum:iEB502BBE5D0F5981
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60961 mRNA. Translation: AAB03490.1.
AF308434, AF308433 Genomic DNA. Translation: AAG42468.1.
AK051272 mRNA. Translation: BAC34586.1.
AK051691 mRNA. Translation: BAC34723.1.
AK165947 mRNA. Translation: BAE38479.1.
AK168413 mRNA. Translation: BAE40328.1.
AK169056 mRNA. Translation: BAE40844.1.
AK169087 mRNA. Translation: BAE40871.1.
BC060045 mRNA. Translation: AAH60045.1.
CCDSiCCDS18979.1.
RefSeqiNP_033524.1. NM_009498.4.
UniGeneiMm.273930.

Genome annotation databases

EnsembliENSMUST00000030797; ENSMUSP00000030797; ENSMUSG00000028955.
GeneIDi22319.
KEGGimmu:22319.
UCSCiuc008vyj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60961 mRNA. Translation: AAB03490.1.
AF308434, AF308433 Genomic DNA. Translation: AAG42468.1.
AK051272 mRNA. Translation: BAC34586.1.
AK051691 mRNA. Translation: BAC34723.1.
AK165947 mRNA. Translation: BAE38479.1.
AK168413 mRNA. Translation: BAE40328.1.
AK169056 mRNA. Translation: BAE40844.1.
AK169087 mRNA. Translation: BAE40871.1.
BC060045 mRNA. Translation: AAH60045.1.
CCDSiCCDS18979.1.
RefSeqiNP_033524.1. NM_009498.4.
UniGeneiMm.273930.

3D structure databases

ProteinModelPortaliP63024.
SMRiP63024. Positions 15-79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204496. 3 interactions.
IntActiP63024. 3 interactions.
MINTiMINT-4139722.

PTM databases

PhosphoSiteiP63024.

Proteomic databases

MaxQBiP63024.
PaxDbiP63024.
PRIDEiP63024.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030797; ENSMUSP00000030797; ENSMUSG00000028955.
GeneIDi22319.
KEGGimmu:22319.
UCSCiuc008vyj.1. mouse.

Organism-specific databases

CTDi9341.
MGIiMGI:1321389. Vamp3.

Phylogenomic databases

eggNOGiCOG5143.
GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiP63024.
KOiK13505.
OMAiFTHACAF.
OrthoDBiEOG7MSMRJ.
PhylomeDBiP63024.
TreeFamiTF313666.

Miscellaneous databases

ChiTaRSiVamp3. mouse.
NextBioi302533.
PROiP63024.
SOURCEiSearch...

Gene expression databases

BgeeiP63024.
CleanExiMM_VAMP3.
GenevestigatoriP63024.

Family and domain databases

InterProiIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFiPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Martin S., Tellam J.T., Livington C., Slot J.W., Gould G.W., James D.E.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "VAMP3 null mice display normal constitutive, insulin- and exercise-regulated vesicle trafficking."
    Yang C.M., Mora S., Ryder J.W., Coker K.J., Hansen P., Allen L.A., Pessin J.E.
    Mol. Cell. Biol. 21:1573-1580(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6x129SV/J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Heart, Liver, Lung and Spinal ganglion.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31."
    Annaert W.G., Becker B., Kistner U., Reth M., Jahn R.
    J. Cell Biol. 139:1397-1410(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCAP31.
  6. "Identification of a novel Bves function: regulation of vesicular transport."
    Hager H.A., Roberts R.J., Cross E.E., Proux-Gillardeaux V., Bader D.M.
    EMBO J. 29:532-545(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BVES.

Entry informationi

Entry nameiVAMP3_MOUSE
AccessioniPrimary (citable) accession number: P63024
Secondary accession number(s): Q3TH70, Q64271
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: April 1, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.