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Protein

Vesicle-associated membrane protein 8

Gene

Vamp8

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

Functioni

SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Plays also a role in regulated enzyme secretion in pancreatic acinar cells (PubMed:15363411). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity).By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

  • autophagosome maturation Source: UniProtKB
  • mucus secretion Source: UniProtKB
  • negative regulation of secretion by cell Source: MGI
  • positive regulation of histamine secretion by mast cell Source: MGI
  • positive regulation of pancreatic amylase secretion Source: MGI
  • protein transport Source: UniProtKB-KW
  • regulation of endocytosis Source: MGI
  • regulation of protein localization to plasma membrane Source: MGI
  • SNARE complex assembly Source: BHF-UCL
  • vesicle fusion Source: MGI
  • viral entry into host cell Source: MGI
  • zymogen granule exocytosis Source: MGI
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-associated membrane protein 81 Publication
Short name:
VAMP-81 Publication
Alternative name(s):
Endobrevin1 Publication
Short name:
EdbBy similarity
Gene namesi
Name:Vamp8Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1336882. Vamp8.

Subcellular locationi

  • Lysosome membrane By similarity; Single-pass type IV membrane protein Curated
  • Late endosome membrane By similarity; Single-pass type IV membrane protein Curated
  • Early endosome membrane By similarity; Single-pass type IV membrane protein Curated
  • Cell membrane 1 Publication; Single-pass type IV membrane protein Curated

  • Note: Perinuclear vesicular structures of the early and late endosomes, coated pits, and trans-Golgi (By similarity). Sub-tight junctional domain in retinal pigment epithelium cells (By similarity). Midbody region during cytokinesis (By similarity). Lumenal oriented, apical membranes of nephric tubular cell (By similarity). Cycles through the apical but not through the basolateral plasma membrane (By similarity). Apical region of acinar cells; in zymogen granule membranes (PubMed:9614193).By similarity1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7575CytoplasmicSequence analysisAdd
BLAST
Transmembranei76 – 9621Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini97 – 1015VesicularSequence analysis

GO - Cellular componenti

  • azurophil granule membrane Source: MGI
  • basolateral plasma membrane Source: MGI
  • cell surface Source: BHF-UCL
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • early endosome Source: MGI
  • early endosome membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • late endosome membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • membrane Source: MGI
  • mitochondrion Source: MGI
  • mucin granule Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • plasma membrane Source: MGI
  • recycling endosome Source: MGI
  • secretory granule Source: MGI
  • secretory granule membrane Source: MGI
  • SNARE complex Source: UniProtKB
  • vesicle Source: MGI
  • zymogen granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241K → A: Blocks internalization from cell surface; when associated with A-27. 1 Publication
Mutagenesisi27 – 271M → A: Blocks internalization from cell surface; when associated with A-24. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 101101Vesicle-associated membrane protein 8PRO_0000206737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei18 – 181PhosphoserineBy similarity
Modified residuei28 – 281PhosphothreonineBy similarity
Modified residuei48 – 481PhosphothreonineBy similarity
Modified residuei54 – 541PhosphothreonineCombined sources
Modified residuei55 – 551PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO70404.
MaxQBiO70404.
PaxDbiO70404.
PeptideAtlasiO70404.
PRIDEiO70404.

PTM databases

iPTMnetiO70404.
PhosphoSiteiO70404.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO70404.
CleanExiMM_VAMP8.

Interactioni

Subunit structurei

Forms a SNARE complex composed of VAMP8, SNAP29 and STX17 involved in fusion of autophagosome with lysosome (By similarity). Found in a number of SNARE complexes with NAPA, SNAP23, SNAP25, STX1A, STX4, STX7, STX8 and VTI1B (PubMed:15363411). Interacts with CALM (PubMed:22118466). SNARE complex formation and binding by CALM are mutually exclusive processes for VAMP8 (PubMed:22118466).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei33 – 331Interaction with STX8By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PicalmO550124EBI-1812572,EBI-915601From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204497. 2 interactions.
IntActiO70404. 4 interactions.
MINTiMINT-1870074.
STRINGi10090.ENSMUSP00000059501.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 3722Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZYMX-ray2.03A/B/C11-41[»]
ProteinModelPortaliO70404.
SMRiO70404. Positions 12-64.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 7261v-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

eggNOGiKOG0860. Eukaryota.
COG5143. LUCA.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiO70404.
KOiK08512.
OrthoDBiEOG75B87Z.
PhylomeDBiO70404.
TreeFamiTF320419.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFiPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS50892. V_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O70404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEASGSAGN DRVRNLQSEV EGVKNIMTQN VERILSRGEN LDHLRNKTED
60 70 80 90 100
LEATSEHFKT TSQKVARKFW WKNVKMIVII CVIVLIIVIL IILFATGTIP

T
Length:101
Mass (Da):11,451
Last modified:August 1, 1998 - v1
Checksum:i0A2FDB6B69E06C3E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361S → A (PubMed:16141072).Curated
Sequence conflicti36 – 361S → A (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39514.1.
RefSeqiNP_058074.2. NM_016794.3.
UniGeneiMm.1838.

Genome annotation databases

GeneIDi22320.
KEGGimmu:22320.
UCSCiuc009cin.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39514.1.
RefSeqiNP_058074.2. NM_016794.3.
UniGeneiMm.1838.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZYMX-ray2.03A/B/C11-41[»]
ProteinModelPortaliO70404.
SMRiO70404. Positions 12-64.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204497. 2 interactions.
IntActiO70404. 4 interactions.
MINTiMINT-1870074.
STRINGi10090.ENSMUSP00000059501.

PTM databases

iPTMnetiO70404.
PhosphoSiteiO70404.

Proteomic databases

EPDiO70404.
MaxQBiO70404.
PaxDbiO70404.
PeptideAtlasiO70404.
PRIDEiO70404.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi22320.
KEGGimmu:22320.
UCSCiuc009cin.2. mouse.

Organism-specific databases

CTDi8673.
MGIiMGI:1336882. Vamp8.

Phylogenomic databases

eggNOGiKOG0860. Eukaryota.
COG5143. LUCA.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiO70404.
KOiK08512.
OrthoDBiEOG75B87Z.
PhylomeDBiO70404.
TreeFamiTF320419.

Miscellaneous databases

PROiO70404.
SOURCEiSearch...

Gene expression databases

BgeeiO70404.
CleanExiMM_VAMP8.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFiPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54 AND SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Pancreas and Spleen.
  9. "The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM."
    Miller S.E., Sahlender D.A., Graham S.C., Honing S., Robinson M.S., Peden A.A., Owen D.J.
    Cell 147:1118-1131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 11-41 IN COMPLEX WITH PICALM, INTERACTION WITH PICALM, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-24 AND MET-27.

Entry informationi

Entry nameiVAMP8_MOUSE
AccessioniPrimary (citable) accession number: O70404
Secondary accession number(s): Q9CRA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 124 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

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.