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O70404 (VAMP8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vesicle-associated membrane protein 8
Short name=VAMP-8
Alternative name(s):
Endobrevin
Short name=Edb
Gene names
Name:Vamp8
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the targeting and/or fusion of transport vesicles to their target membrane. Plays a role in regulated enzyme secretion in pancreatic acinar cells. Involved for dense-granule secretion in platelets. Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells. Involved in the homotypic fusion of early and late endosomes By similarity. Ref.6

Subunit structure

Found in a number of SNARE complexes with NAPA, SNAP23, SNAP25, STX1A, STX4, STX7, STX8 and VTI1B By similarity. Interacts with STX8 By similarity.

Subcellular location

Membrane; Single-pass type IV membrane protein Probable Ref.6.

Tissue specificity

Expressed abundantly in the kidney, less in the liver, brain, kidney, heart, lung, pancreas and placenta. Ref.2 Ref.6

Sequence similarities

Belongs to the synaptobrevin family.

Contains 1 v-SNARE coiled-coil homology domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 101101Vesicle-associated membrane protein 8
PRO_0000206737

Regions

Topological domain1 – 7575Cytoplasmic Potential
Transmembrane76 – 9621Helical; Anchor for type IV membrane protein; Potential
Topological domain97 – 1015Vesicular Potential
Domain12 – 7261v-SNARE coiled-coil homology

Sites

Site331Interaction with STX8 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue181Phosphoserine Ref.7

Experimental info

Sequence conflict361S → A Ref.4
Sequence conflict361S → A Ref.5

Sequences

Sequence LengthMass (Da)Tools
O70404 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 0A2FDB6B69E06C3E

FASTA10111,451
        10         20         30         40         50         60 
MEEASGSAGN DRVRNLQSEV EGVKNIMTQN VERILSRGEN LDHLRNKTED LEATSEHFKT 

        70         80         90        100 
TSQKVARKFW WKNVKMIVII CVIVLIIVIL IILFATGTIP T

« Hide

References

« Hide 'large scale' references
[1]"Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome."
Wong S.H., Zhang T., Xu Y., Subramaniam V.N., Griffiths G., Hong W.
Mol. Biol. Cell 9:1549-1563(1998) [PubMed: 9614193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Seven novel mammalian SNARE proteins localize to distinct membrane compartments."
Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C., Prekeris R., Yoo J.-S., Scheller R.H.
J. Biol. Chem. 273:10317-10324(1998) [PubMed: 9553086] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Embryo.
[3]Lu L., Bui T.D., Hong W.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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. expand/collapse author list , 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(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[5]"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(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
[6]"A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells."
Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F., Hong W.
Dev. Cell 7:359-371(2004) [PubMed: 15363411] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION IN COMPLEXES WITH SNAP23; VTI1B; STX4 AND STX7.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF053724 mRNA. Translation: AAC06371.1.
AF045661 mRNA. Translation: AAC23665.1.
AF247556 Genomic DNA. Translation: AAK48423.1.
AK002268 mRNA. Translation: BAB21977.1.
AK013279 mRNA. Translation: BAB28766.1.
BC012668 mRNA. Translation: AAH12668.1.
IPIIPI00453589.
RefSeqNP_058074.2. NM_016794.3.
UniGeneMm.1838.

3D structure databases

ProteinModelPortalO70404.
SMRO70404. Positions 12-64.
ModBaseSearch...

Protein-protein interaction databases

IntActO70404. 1 interaction.
STRINGO70404.

PTM databases

PhosphoSiteO70404.

Proteomic databases

PRIDEO70404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059983; ENSMUSP00000059501; ENSMUSG00000050732.
GeneID22320.
KEGGmmu:22320.
UCSCuc009cin.2. mouse.

Organism-specific databases

CTD8673.
MGIMGI:1336882. Vamp8.

Phylogenomic databases

eggNOGroNOG17274.
HOGENOMHBG386095.
HOVERGENHBG006675.
InParanoidO70404.
OrthoDBEOG4FBHVK.
PhylomeDBO70404.

Gene expression databases

ArrayExpressO70404.
BgeeO70404.
CleanExMM_VAMP8.
GenevestigatorO70404.
GermOnlineENSMUSG00000050732. Mus musculus.

Family and domain databases

InterProIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin_met/fun.
[Graphical view]
KOK08512.
PfamPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSPR00219. SYNAPTOBREVN.
PROSITEPS00417. SYNAPTOBREVIN. False negative.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302537.
SOURCESearch...

Entry information

Entry nameVAMP8_MOUSE
AccessionPrimary (citable) accession number: O70404
Secondary accession number(s): Q9CRA3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: August 1, 1998
Last modified: November 16, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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