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UniProtKB/Swiss-Prot entry P51809


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name VAMP7_HUMAN
Primary accession number P51809
Secondary accession numbers Q53GY7 Q7Z409 Q9H4A7
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 86)
Name and origin of the protein
Protein name Vesicle-associated membrane protein 7
Synonyms VAMP-7
Synaptobrevin-like protein 1
Tetanus-insensitive VAMP
Ti-VAMP
Gene name
Name: VAMP7
Synonyms: SYBL1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1038/ng0696-227; PubMed=8640232 [NCBI, ExPASy, EBI, Israel, Japan]
D'Esposito M., Ciccodicola A., Gianfrancesco F., Esposito T., Flagiello L., Mazzarella R., Schlessinger D., D'Urso M.;
"A synaptobrevin-like gene in the Xq28 pseudoautosomal region undergoes X inactivation.";
Nat. Genet. 13:227-229(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/hmg/9.3.395; PubMed=10655549 [NCBI, ExPASy, EBI, Israel, Japan]
Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F., Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A., Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A., Cocchia S., Mercadante G., Pannone E., Archidiacono N., Rocchi M., Schlessinger D., D'Urso M.;
"Differentially regulated and evolved genes in the fully sequenced Xq/Yq pseudoautosomal region.";
Hum. Mol. Genet. 9:395-401(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Brain;
DOI=10.1073/pnas.1431910100; PubMed=12853575 [NCBI, ExPASy, EBI, Israel, Japan]
Martinez-Arca S., Rudge R., Vacca M., Camonis J., Daviet L., Formstecher E., Hamburger A., Filippini F., D'Esposito M., Galli T.;
"A dual mechansim controlling the localization and function of exocytic v-SNARE.";
Proc. Natl. Acad. Sci. U.S.A. 100:9011-9016(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
D'Esposito M., Filippini F., Rossi V., D'Urso M.;
"Alternative splicing of SYBL1 gene.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-10; 126-137 AND 143-150, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[9]
FUNCTION.
PubMed=10888671 [NCBI, ExPASy, EBI, Israel, Japan]
Ward D.M., Pevsner J., Scullion M.A., Vaughn M., Kaplan J.;
"Syntaxin 7 and VAMP-7 are soluble N-ethylmaleimide-sensitive factor attachment protein receptors required for late endosome-lysosome and homotypic lysosome fusion in alveolar macrophages.";
Mol. Biol. Cell 11:2327-2333(2000).
[10]
FUNCTION.
DOI=10.1111/j.1398-9995.2006.01089.x; PubMed=16677249 [NCBI, ExPASy, EBI, Israel, Japan]
Logan M.R., Lacy P., Odemuyiwa S.O., Steward M., Davoine F., Kita H., Moqbel R.;
"A critical role for vesicle-associated membrane protein-7 in exocytosis from human eosinophils and neutrophils.";
Allergy 61:777-784(2006).
[11]
FUNCTION.
DOI=10.1016/j.bbrc.2007.11.079; PubMed=18042464 [NCBI, ExPASy, EBI, Israel, Japan]
Marcet-Palacios M., Odemuyiwa S.O., Coughlin J.J., Garofoli D., Ewen C., Davidson C.E., Ghaffari M., Kane K.P., Lacy P., Logan M.R., Befus A.D., Bleackley R.C., Moqbel R.;
"Vesicle-associated membrane protein 7 (VAMP-7) is essential for target cell killing in a natural killer cell line.";
Biochem. Biophys. Res. Commun. 366:617-623(2008).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[13]
STRUCTURE BY NMR OF 1-118.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the longin domain of synaptobrevin-like protein 1.";
Submitted (OCT-2006) to the PDB data bank.
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 (By similarity).
  • INTERACTION:
    P52594:AGFG1; NbExp=5; IntAct=EBI-1052205, EBI-996560;
  • SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein (By similarity). Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein (By similarity). Late endosome membrane; Single-pass type IV membrane protein (By similarity). Lysosome membrane; Single-pass type IV membrane protein (By similarity). Endoplasmic reticulum membrane; Single-pass type IV membrane protein (By similarity). Cytoplasmic vesicle, phagosome membrane; Single-pass type IV membrane protein (By similarity).
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsTi-VAMPa/VAMP7a
    Isoform IDP51809-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsTi-VAMPb/VAMP7b
    Isoform IDP51809-2
    Features which should be applied to build the isoform sequence: VSP_017509.
    Name3
    SynonymsTi-VAMPc/VAMP7c
    Isoform IDP51809-3
    Features which should be applied to build the isoform sequence: VSP_017508.
  • TISSUE SPECIFICITY: Detected in all tissues tested.
  • MISCELLANEOUS: The gene encoding for this protein is located in the pseudoautosomal region 2 (PAR2) of X and Y chromosomes.
  • MISCELLANEOUS: Loss-of-function mutant (antisense inhibition) displays impaired granzyme B release and target cell killing by natural killer cells.
  • 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
X92396; CAA63133.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271736; CAB96816.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ549301; CAD70593.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ295938; CAC16891.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222794; BAD96514.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC056141; AAH56141.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00013236; -.
IPI00020887; -.
IPI00401804; -.
RefSeq NP_001138621.1; -.
NP_005629.1; -.
UniGene Hs.24167
3D structure databases
PDB
2DMW; NMR; -; A=1-118.[ExPASy / RCSB / EBI]
2VX8; X-ray; 2.20 A; A/B/C/D=1-120.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2DMW; -.
2VX8; -.
ModBase P51809.
Protein-protein interaction databases
IntAct P51809; 3.
PTM databases
PhosphoSite P51809; -.
Enzyme and pathway databases
Reactome REACT_11123; Membrane Trafficking.
Organism-specific databases
GeneCards GC0XP154764; -.
H-InvDB HIX0028460; -.
HIX0077340; -.
HGNC HGNC:11486; VAMP7.
GenAtlas VAMP7.
MIM 300053; gene. [NCBI / EBI]
PharmGKB PA36268; -.
Gene expression databases
ArrayExpress P51809; -.
Bgee P51809; -.
CleanEx HS_VAMP7; -.
GermOnline ENSG00000124333; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from sequence or structural similarity 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 sequence or structural similarity from UniProtKB).
GO:0005765; Cellular component: lysosomal membrane (inferred from sequence or structural similarity 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 sequence or structural similarity from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0017156; Biological process: calcium ion-dependent exocytosis (inferred from sequence or structural similarity from UniProtKB).
GO:0008333; Biological process: endosome to lysosome transport (inferred from direct assay from UniProtKB).
GO:0043308; Biological process: eosinophil degranulation (inferred from sequence or structural similarity from UniProtKB).
GO:0006888; Biological process: ER to Golgi vesicle-mediated transport (inferred from sequence or structural similarity from UniProtKB).
GO:0043312; Biological process: neutrophil degranulation (inferred from sequence or structural similarity from UniProtKB).
GO:0006911; Biological process: phagocytosis, engulfment (inferred from sequence or structural similarity 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 P51809; -.
Genome annotation databases
Ensembl ENSG00000124333; Homo sapiens. [Contig view]
GeneID 6845; -.
KEGG hsa:6845; -.
Phylogenomic databases
HOVERGEN P51809; -.
OMA P51809; WIYMAKL.
Other
NextBio 26723; -.
SOURCE VAMP7; Homo sapiens.
ProtoNet P51809.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum; Endosome; Exocytosis; Golgi apparatus; Lysosome; Membrane; Protein transport; Signal-anchor; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   220  219     Vesicle-associated membrane protein 7. PRO_0000206761
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; partial. 
VAR_SEQ   28    68        Missing (in isoform 3). VSP_017508
VAR_SEQ   145   220        DLVAQRGERLELLIDKTENLVDSSVTFKTTSRNLARAMCM KNLKLTIIIIIVSIVFIYIIVSPLCGGFTWPSCVKK -> VCHLQNYQQKSCSSHVYEEPQAHYYHHHRINCVHLYHCFT SLWWIYMAKLCEEIGKKKLPLTKDMREQGVKSNPCDSSLS HTDRWYLPVSSTLFSLFKILFHASRFIFVLSTSLFL (in isoform 2). VSP_017509
CONFLICT   98    98        L -> P (in Ref. 5; BAD96514). 
Sequence information
Length: 220 AA [This is the length of the unprocessed precursor] Molecular weight: 24935 Da [This is the MW of the unprocessed precursor] CRC64: 9C1AA5C590375CEF [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 ERSRAFNFLN EIKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN 

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

       190        200        210        220 
AMCMKNLKLT IIIIIVSIVF IYIIVSPLCG GFTWPSCVKK 

P51809 in FASTA format

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