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Q9JHW5 (VAMP7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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 7

Short name=VAMP-7
Alternative name(s):
Synaptobrevin-like protein 1
Gene names
Name:Vamp7
Synonyms:Sybl1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation. Ref.3 Ref.5 Ref.6 Ref.7

Subunit structure

Component of the SNARE complex composed of STX4, SNAP23 and VAMP7 that binds SYT7 during lysosomal exocytosis. Component of the SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required for heterotypic fusion of late endosomes with lysosomes in liver cells.

Subcellular location

Cytoplasmic vesiclesecretory vesicle membrane; Single-pass type IV membrane protein. Golgi apparatustrans-Golgi network membrane; Single-pass type IV membrane protein. Late endosome membrane; Single-pass type IV membrane protein. Lysosome membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Cytoplasmic vesiclephagosome membrane; Single-pass type IV membrane protein By similarity. Note: In immature neurons expression is localized in vesicular structures in axons and dendrites while in mature neurons it is localized to the somatodendritic region. Colocalizes with Lamp1 in kidney cells. Localization to the endoplasmic reticulum membrane was observed in the intestine but not in liver or kidney. Ref.2 Ref.3 Ref.4 Ref.7

Tissue specificity

Expressed in brain, kidney, liver, lung, spleen and thymus. Not expressed in heart and skeletal muscle. Ref.2 Ref.3 Ref.4 Ref.7

Sequence similarities

Belongs to the synaptobrevin family.

Contains 1 longin domain.

Contains 1 v-SNARE coiled-coil homology domain.

Ontologies

Keywords
   Biological processExocytosis
Protein transport
Transport
   Cellular componentCytoplasmic vesicle
Endoplasmic reticulum
Endosome
Golgi apparatus
Lysosome
Membrane
   DomainCoiled coil
Signal-anchor
Transmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processER to Golgi vesicle-mediated transport

Inferred from direct assay Ref.7. Source: UniProtKB

calcium ion-dependent exocytosis

Inferred from direct assay Ref.6. Source: UniProtKB

endosome to lysosome transport

Inferred from direct assay Ref.5. Source: UniProtKB

eosinophil degranulation

Inferred from direct assay Ref.6. Source: UniProtKB

neutrophil degranulation

Inferred from direct assay Ref.6. Source: UniProtKB

phagocytosis, engulfment

Inferred from direct assay Ref.5. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

triglyceride transport

Inferred from mutant phenotype Ref.7. Source: RGD

vesicle fusion with Golgi apparatus

Inferred from direct assay. Source: RGD

   Cellular componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

SNARE complex

Inferred from direct assay Ref.5. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from direct assay Ref.7. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

late endosome membrane

Inferred from direct assay Ref.3. Source: UniProtKB

lysosomal membrane

Inferred from direct assay Ref.3. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionsyntaxin binding

Inferred from physical interaction Ref.5. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 220219Vesicle-associated membrane protein 7
PRO_0000316088

Regions

Topological domain2 – 188187Cytoplasmic Potential
Transmembrane189 – 20921Helical; Anchor for type IV membrane protein; Potential
Topological domain210 – 22011Vesicular Potential
Domain7 – 110104Longin
Domain125 – 18561v-SNARE coiled-coil homology

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1681Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JHW5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 527D818A23224A54

FASTA22024,776
        10         20         30         40         50         60 
MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY LFHYICQDRI 

        70         80         90        100        110        120 
VYLCITDDDF ERSRAFGFLN EVKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN 

       130        140        150        160        170        180 
QSLDRVTETQ AQVDELKGIM VRNIDLVAQR GERLELLIDK TENLVDSSVT FKTTSRNLAR 

       190        200        210        220 
AMCVKNVKLT AIIVVVSIVF IYIIVSPLCG GFTWPSCVKK 

« Hide

References

[1]"Rat basophilic leukemia cells express syntaxin-3 and VAMP-7 in granule membranes."
Hibi T., Hirashima N., Nakanishi M.
Biochem. Biophys. Res. Commun. 271:36-41(2000) [PubMed: 10777677] [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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"VAMP-7 mediates vesicular transport from endosomes to lysosomes."
Advani R.J., Yang B., Prekeris R., Lee K.C., Klumperman J., Scheller R.H.
J. Cell Biol. 146:765-776(1999) [PubMed: 10459012] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Subcellular localization of tetanus neurotoxin-insensitive vesicle-associated membrane protein (VAMP)/VAMP7 in neuronal cells: evidence for a novel membrane compartment."
Coco S., Raposo G., Martinez S., Fontaine J.-J., Takamori S., Zahraoui A., Jahn R., Matteoli M., Louvard D., Galli T.
J. Neurosci. 19:9803-9812(1999) [PubMed: 10559389] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"Combinatorial SNARE complexes with VAMP7 or VAMP8 define different late endocytic fusion events."
Pryor P.R., Mullock B.M., Bright N.A., Lindsay M.R., Gray S.R., Richardson S.C.W., Stewart A., James D.E., Piper R.C., Luzio J.P.
EMBO Rep. 5:590-595(2004) [PubMed: 15133481] [Abstract]
Cited for: FUNCTION, SNARE COMPLEX CHARACTERIZATION.
[6]"Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis."
Rao S.K., Huynh C., Proux-Gillardeaux V., Galli T., Andrews N.W.
J. Biol. Chem. 279:20471-20479(2004) [PubMed: 14993220] [Abstract]
Cited for: FUNCTION, SNARE COMPLEX CHARACTERIZATION.
[7]"Vesicle-associated membrane protein 7 is expressed in intestinal ER."
Siddiqi S.A., Mahan J., Siddiqi S., Gorelick F.S., Mansbach C.M. II
J. Cell Sci. 119:943-950(2006) [PubMed: 16495485] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF281632 mRNA. Translation: AAF88059.1.
IPIIPI00199984.
PIRJC7258.
RefSeqNP_445983.1. NM_053531.1.
UniGeneRn.34151.

3D structure databases

HSSPHSSP built from PDB template 1GL2 based on UniProtKB Q9WUF4.
ProteinModelPortalQ9JHW5.
SMRQ9JHW5. Positions 1-122.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9JHW5. 1 interaction.
STRINGQ9JHW5.

Proteomic databases

PRIDEQ9JHW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000011065; ENSRNOP00000011065; ENSRNOG00000008372.
GeneID85491.
KEGGrno:85491.

Organism-specific databases

CTD6845.
RGD621558. Vamp7.

Phylogenomic databases

eggNOGmaNOG08658.
GeneTreeENSGT00510000047733.
HOVERGENHBG006675.
InParanoidQ9JHW5.
OMALTFLCMA.
OrthoDBEOG49079V.
PhylomeDBQ9JHW5.

Gene expression databases

ArrayExpressQ9JHW5.
GenevestigatorQ9JHW5.

Family and domain databases

InterProIPR010908. Longin.
IPR011012. Longin-like.
IPR001388. Synaptobrevin.
[Graphical view]
Gene3DG3DSA:3.30.450.50. Longin. 1 hit.
KOK08515.
PfamPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSPR00219. SYNAPTOBREVN.
SUPFAMSSF64356. Longin_like. 1 hit.
PROSITEPS50859. LONGIN. 1 hit.
PS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio617580.

Entry information

Entry nameVAMP7_RAT
AccessionPrimary (citable) accession number: Q9JHW5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2000
Last modified: November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families