[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1006/bbrc.2000.2591; PubMed=10777677 [NCBI, ExPASy, EBI, Israel, Japan] Hibi T., Hirashima N., Nakanishi M.; "Rat basophilic leukemia cells express syntaxin-3 and VAMP-7 in granule membranes."; Biochem. Biophys. Res. Commun. 271:36-41(2000).
[2]	SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1074/jbc.273.17.10317; PubMed=9553086 [NCBI, ExPASy, EBI, Israel, Japan] Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C., Prekeris R., Yoo J.-S., Scheller R.H.; "Seven novel mammalian SNARE proteins localize to distinct membrane compartments."; J. Biol. Chem. 273:10317-10324(1998).
[3]	FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1083/jcb.146.4.765; PubMed=10459012 [NCBI, ExPASy, EBI, Israel, Japan] Advani R.J., Yang B., Prekeris R., Lee K.C., Klumperman J., Scheller R.H.; "VAMP-7 mediates vesicular transport from endosomes to lysosomes."; J. Cell Biol. 146:765-776(1999).
[4]	SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. PubMed=10559389 [NCBI, ExPASy, EBI, Israel, Japan] Coco S., Raposo G., Martinez S., Fontaine J.-J., Takamori S., Zahraoui A., Jahn R., Matteoli M., Louvard D., Galli T.; "Subcellular localization of tetanus neurotoxin-insensitive vesicle-associated membrane protein (VAMP)/VAMP7 in neuronal cells: evidence for a novel membrane compartment."; J. Neurosci. 19:9803-9812(1999).
[5]	FUNCTION, AND SNARE COMPLEX CHARACTERIZATION. DOI=10.1038/sj.embor.7400150; PubMed=15133481 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Combinatorial SNARE complexes with VAMP7 or VAMP8 define different late endocytic fusion events."; EMBO Rep. 5:590-595(2004).
[6]	FUNCTION, AND SNARE COMPLEX CHARACTERIZATION. DOI=10.1074/jbc.M400798200; PubMed=14993220 [NCBI, ExPASy, EBI, Israel, Japan] Rao S.K., Huynh C., Proux-Gillardeaux V., Galli T., Andrews N.W.; "Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis."; J. Biol. Chem. 279:20471-20479(2004).
[7]	FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1242/jcs.02803; PubMed=16495485 [NCBI, ExPASy, EBI, Israel, Japan] Siddiqi S.A., Mahan J., Siddiqi S., Gorelick F.S., Mansbach C.M. II; "Vesicle-associated membrane protein 7 is expressed in intestinal ER."; J. Cell Sci. 119:943-950(2006).

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.
SUBUNIT: 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 vesicle, secretory vesicle membrane; Single-pass type IV membrane protein. Golgi apparatus, trans-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 vesicle, phagosome 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.
TISSUE SPECIFICITY: Expressed in brain, kidney, liver, lung, spleen and thymus. Not expressed in heart and skeletal muscle.
SIMILARITY: Belongs to the synaptobrevin family.
SIMILARITY: Contains 1 longin domain.
SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF281632; AAF88059.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00199984; -.

JC7258; JC7258.

NP_445983.1; -.

3D structure databases

HSSP

Q9WUF4; 1GL2. [HSSP ENTRY / PDB]

SMR

Q9JHW5; 1-122.

ModBase

Q9JHW5.

Organism-specific databases

RGD

621558; Vamp7.

Gene expression databases

ArrayExpress

Q9JHW5; -.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from direct assay from UniProtKB).
GO:0005794;	Cellular component: Golgi apparatus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031902;	Cellular component: late endosome membrane (inferred from direct assay from UniProtKB).
GO:0005765;	Cellular component: lysosomal membrane (inferred from direct assay from UniProtKB).
GO:0030670;	Cellular component: phagocytic vesicle membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0030667;	Cellular component: secretory granule membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031201;	Cellular component: SNARE complex (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0017156;	Biological process: calcium ion-dependent exocytosis (inferred from direct assay from UniProtKB).
GO:0008333;	Biological process: endosome to lysosome transport (inferred from direct assay from UniProtKB).
GO:0043308;	Biological process: eosinophil degranulation (inferred from direct assay from UniProtKB).
GO:0006888;	Biological process: ER to Golgi vesicle-mediated transport (inferred from direct assay from UniProtKB).
GO:0043312;	Biological process: neutrophil degranulation (inferred from direct assay from UniProtKB).
GO:0006911;	Biological process: phagocytosis, engulfment (inferred from direct assay from UniProtKB).
GO:0015031;	Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006906;	Biological process: vesicle fusion (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR010908; Longin.
IPR001388; Synaptobrevin.
Graphical view of domain structure.

Pfam

PF00957; Synaptobrevin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00219; SYNAPTOBREVN.

ProDom

PD001229; Synaptobrevin; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS50859; LONGIN; 1.
PS00417; SYNAPTOBREVIN; 1.
PS50892; V_SNARE; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q9JHW5; -.

Genome annotation databases

Ensembl

ENSRNOG00000008372; Rattus norvegicus. [Contig view]

GeneID

85491; -.

KEGG

rno:85491; -.

Phylogenomic databases

HOVERGEN

Q9JHW5; -.

OMA

Q9JHW5; FLCMAND.

Other

617580; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Coiled coil; Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Exocytosis; Golgi apparatus; Lysosome; Membrane; Protein transport; Signal-anchor; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 220`	`219`	`Vesicle-associated membrane protein 7.`	`PRO_0000316088`
`TOPO_DOM`	`2 188`	`187`	`Cytoplasmic (Potential).`
`TRANSMEM`	`189 209`	`21`	`Anchor for type IV membrane protein (Potential).`
`TOPO_DOM`	`210 220`	`11`	`Vesicular (Potential).`
`DOMAIN`	`7 110`	`104`	`Longin.`
`DOMAIN`	`125 185`	`61`	`v-SNARE coiled-coil homology.`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`

Sequence information

Length: 220 AA [This is the length of the unprocessed precursor]

Molecular weight: 24776 Da [This is the MW of the unprocessed precursor]

CRC64: 527D818A23224A54 [This is a checksum on the sequence]

        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

Q9JHW5 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools