VAMP7_HUMAN
ID VAMP7_HUMAN Reviewed; 220 AA.
AC P51809; Q53GY7; Q7Z409; Q9H4A7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Vesicle-associated membrane protein 7;
DE Short=VAMP-7;
DE AltName: Full=Synaptobrevin-like protein 1;
DE AltName: Full=Tetanus-insensitive VAMP;
DE Short=Ti-VAMP;
GN Name=VAMP7; Synonyms=SYBL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8640232; DOI=10.1038/ng0696-227;
RA D'Esposito M., Ciccodicola A., Gianfrancesco F., Esposito T., Flagiello L.,
RA Mazzarella R., Schlessinger D., D'Urso M.;
RT "A synaptobrevin-like gene in the Xq28 pseudoautosomal region undergoes X
RT inactivation.";
RL Nat. Genet. 13:227-229(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10655549; DOI=10.1093/hmg/9.3.395;
RA Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F.,
RA Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A.,
RA Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A., Cocchia S.,
RA Mercadante G., Pannone E., Archidiacono N., Rocchi M., Schlessinger D.,
RA D'Urso M.;
RT "Differentially regulated and evolved genes in the fully sequenced Xq/Yq
RT pseudoautosomal region.";
RL Hum. Mol. Genet. 9:395-401(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12853575; DOI=10.1073/pnas.1431910100;
RA Martinez-Arca S., Rudge R., Vacca M., Camonis J., Daviet L.,
RA Formstecher E., Hamburger A., Filippini F., D'Esposito M., Galli T.;
RT "A dual mechanism controlling the localization and function of exocytic v-
RT SNARE.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9011-9016(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA D'Esposito M., Filippini F., Rossi V., D'Urso M.;
RT "Alternative splicing of SYBL1 gene.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-10; 126-137 AND 143-150, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [9]
RP FUNCTION.
RX PubMed=10888671; DOI=10.1091/mbc.11.7.2327;
RA Ward D.M., Pevsner J., Scullion M.A., Vaughn M., Kaplan J.;
RT "Syntaxin 7 and VAMP-7 are soluble N-ethylmaleimide-sensitive factor
RT attachment protein receptors required for late endosome-lysosome and
RT homotypic lysosome fusion in alveolar macrophages.";
RL Mol. Biol. Cell 11:2327-2333(2000).
RN [10]
RP FUNCTION.
RX PubMed=16677249; DOI=10.1111/j.1398-9995.2006.01089.x;
RA Logan M.R., Lacy P., Odemuyiwa S.O., Steward M., Davoine F., Kita H.,
RA Moqbel R.;
RT "A critical role for vesicle-associated membrane protein-7 in exocytosis
RT from human eosinophils and neutrophils.";
RL Allergy 61:777-784(2006).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [12]
RP FUNCTION.
RX PubMed=18042464; DOI=10.1016/j.bbrc.2007.11.079;
RA Marcet-Palacios M., Odemuyiwa S.O., Coughlin J.J., Garofoli D., Ewen C.,
RA Davidson C.E., Ghaffari M., Kane K.P., Lacy P., Logan M.R., Befus A.D.,
RA Bleackley R.C., Moqbel R.;
RT "Vesicle-associated membrane protein 7 (VAMP-7) is essential for target
RT cell killing in a natural killer cell line.";
RL Biochem. Biophys. Res. Commun. 366:617-623(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP INTERACTION WITH PICALM.
RX PubMed=23741335; DOI=10.1371/journal.pone.0064514;
RA Sahlender D.A., Kozik P., Miller S.E., Peden A.A., Robinson M.S.;
RT "Uncoupling the functions of CALM in VAMP sorting and clathrin-coated pit
RT formation.";
RL PLoS ONE 8:E64514-E64514(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP INTERACTION WITH RAB21.
RX PubMed=25648148; DOI=10.15252/embr.201439464;
RA Jean S., Cox S., Nassari S., Kiger A.A.;
RT "Starvation-induced MTMR13 and RAB21 activity regulates VAMP8 to promote
RT autophagosome-lysosome fusion.";
RL EMBO Rep. 16:297-311(2015).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP STRUCTURE BY NMR OF 1-118.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the longin domain of synaptobrevin-like protein 1.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane during transport of proteins from the early
CC endosome to the lysosome. Required for heterotypic fusion of late
CC endosomes with lysosomes and homotypic lysosomal fusion. Required for
CC calcium regulated lysosomal exocytosis. Involved in the export of
CC chylomicrons from the endoplasmic reticulum to the cis Golgi. Required
CC for exocytosis of mediators during eosinophil and neutrophil
CC degranulation, and target cell killing by natural killer cells.
CC Required for focal exocytosis of late endocytic vesicles during
CC phagosome formation. {ECO:0000269|PubMed:10888671,
CC ECO:0000269|PubMed:16677249, ECO:0000269|PubMed:18042464}.
CC -!- SUBUNIT: Component of the SNARE complex composed of STX4, SNAP23 and
CC VAMP7 that binds SYT7 during lysosomal exocytosis. Component of the
CC SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required
CC for heterotypic fusion of late endosomes with lysosomes. May interact
CC with STX17 (By similarity). Interacts with PICALM (PubMed:23741335).
CC Interacts with RAB21 (PubMed:25648148). {ECO:0000250,
CC ECO:0000269|PubMed:23741335, ECO:0000269|PubMed:25648148}.
CC -!- INTERACTION:
CC P51809; P52594: AGFG1; NbExp=7; IntAct=EBI-1052205, EBI-996560;
CC P51809; Q5SQN1: SNAP47; NbExp=4; IntAct=EBI-1052205, EBI-10244848;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
CC Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}. Late endosome membrane
CC {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
CC Lysosome membrane {ECO:0000269|PubMed:17897319}; Single-pass type IV
CC membrane protein {ECO:0000269|PubMed:17897319}. Endoplasmic reticulum
CC membrane {ECO:0000250}; Single-pass type IV membrane protein
CC {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250};
CC Single-pass type IV membrane protein {ECO:0000250}. Synapse,
CC synaptosome {ECO:0000250}. Note=In immature neurons expression is
CC localized in vesicular structures in axons and dendrites while in
CC mature neurons it is localized to the somatodendritic region.
CC Colocalizes with LAMP1 in kidney cells. Localization to the endoplasmic
CC reticulum membrane was observed in the intestine but not in liver or
CC kidney (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Ti-VAMPa/VAMP7a;
CC IsoId=P51809-1; Sequence=Displayed;
CC Name=2; Synonyms=Ti-VAMPb/VAMP7b;
CC IsoId=P51809-2; Sequence=VSP_017509;
CC Name=3; Synonyms=Ti-VAMPc/VAMP7c;
CC IsoId=P51809-3; Sequence=VSP_017508;
CC -!- TISSUE SPECIFICITY: Detected in all tissues tested.
CC -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC pseudoautosomal region 2 (PAR2) of X and Y chromosomes.
CC -!- MISCELLANEOUS: Loss-of-function mutant (antisense inhibition) displays
CC impaired granzyme B release and target cell killing by natural killer
CC cells.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BI547528; Type=Miscellaneous discrepancy; Note=Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; X92396; CAA63133.1; -; mRNA.
DR EMBL; AJ271736; CAB96816.1; -; Genomic_DNA.
DR EMBL; AJ549301; CAD70593.2; -; mRNA.
DR EMBL; AJ295938; CAC16891.1; -; mRNA.
DR EMBL; AK222794; BAD96514.1; -; mRNA.
DR EMBL; BC056141; AAH56141.1; -; mRNA.
DR EMBL; BI547528; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS14770.4; -. [P51809-1]
DR CCDS; CCDS48199.1; -. [P51809-3]
DR CCDS; CCDS55548.1; -. [P51809-2]
DR RefSeq; NP_001138621.1; NM_001145149.2. [P51809-3]
DR RefSeq; NP_001172112.1; NM_001185183.1. [P51809-2]
DR RefSeq; NP_005629.1; NM_005638.5. [P51809-1]
DR PDB; 2DMW; NMR; -; A=1-118.
DR PDBsum; 2DMW; -.
DR AlphaFoldDB; P51809; -.
DR BMRB; P51809; -.
DR SMR; P51809; -.
DR BioGRID; 112712; 101.
DR CORUM; P51809; -.
DR IntAct; P51809; 52.
DR MINT; P51809; -.
DR STRING; 9606.ENSP00000262640; -.
DR iPTMnet; P51809; -.
DR MetOSite; P51809; -.
DR PhosphoSitePlus; P51809; -.
DR SwissPalm; P51809; -.
DR BioMuta; VAMP7; -.
DR DMDM; 1723133; -.
DR EPD; P51809; -.
DR jPOST; P51809; -.
DR MassIVE; P51809; -.
DR MaxQB; P51809; -.
DR PaxDb; P51809; -.
DR PeptideAtlas; P51809; -.
DR PRIDE; P51809; -.
DR ProteomicsDB; 56403; -. [P51809-1]
DR ProteomicsDB; 56404; -. [P51809-2]
DR ProteomicsDB; 56405; -. [P51809-3]
DR Antibodypedia; 31441; 232 antibodies from 35 providers.
DR DNASU; 6845; -.
DR Ensembl; ENST00000262640.11; ENSP00000262640.6; ENSG00000124333.16. [P51809-2]
DR Ensembl; ENST00000286448.12; ENSP00000286448.6; ENSG00000124333.16. [P51809-1]
DR Ensembl; ENST00000460621.6; ENSP00000427822.1; ENSG00000124333.16. [P51809-3]
DR GeneID; 6845; -.
DR KEGG; hsa:6845; -.
DR MANE-Select; ENST00000286448.12; ENSP00000286448.6; NM_005638.6; NP_005629.1.
DR UCSC; uc004fnr.4; human. [P51809-1]
DR CTD; 6845; -.
DR DisGeNET; 6845; -.
DR GeneCards; VAMP7; -.
DR HGNC; HGNC:11486; VAMP7.
DR HPA; ENSG00000124333; Low tissue specificity.
DR MalaCards; VAMP7; -.
DR MIM; 300053; gene.
DR neXtProt; NX_P51809; -.
DR OpenTargets; ENSG00000124333; -.
DR Orphanet; 251510; 46,XY partial gonadal dysgenesis.
DR PharmGKB; PA162408786; -.
DR VEuPathDB; HostDB:ENSG00000124333; -.
DR eggNOG; KOG0859; Eukaryota.
DR GeneTree; ENSGT00510000047733; -.
DR HOGENOM; CLU_064620_1_1_1; -.
DR InParanoid; P51809; -.
DR OMA; NTKLMIM; -.
DR PhylomeDB; P51809; -.
DR TreeFam; TF323448; -.
DR PathwayCommons; P51809; -.
DR Reactome; R-HSA-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9020591; Interleukin-12 signaling.
DR SignaLink; P51809; -.
DR BioGRID-ORCS; 6845; 8 hits in 588 CRISPR screens.
DR ChiTaRS; VAMP7; human.
DR EvolutionaryTrace; P51809; -.
DR GeneWiki; SYBL1; -.
DR GenomeRNAi; 6845; -.
DR Pharos; P51809; Tbio.
DR PRO; PR:P51809; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51809; protein.
DR Bgee; ENSG00000124333; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; P51809; baseline and differential.
DR Genevisible; P51809; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0035577; C:azurophil granule membrane; IDA:UniProtKB.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
DR GO; GO:0031143; C:pseudopodium; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
DR GO; GO:0043308; P:eosinophil degranulation; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0043320; P:natural killer cell degranulation; IMP:UniProtKB.
DR GO; GO:0043312; P:neutrophil degranulation; IMP:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006906; P:vesicle fusion; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
DR CDD; cd14824; Longin; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR042855; V_SNARE_CC.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum;
KW Endosome; Exocytosis; Golgi apparatus; Lysosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Signal-anchor; Synapse; Synaptosome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..220
FT /note="Vesicle-associated membrane protein 7"
FT /id="PRO_0000206761"
FT TOPO_DOM 2..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..220
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 7..110
FT /note="Longin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT DOMAIN 125..185
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT MOD_RES 2
FT /note="N-acetylalanine; partial"
FT /evidence="ECO:0000269|Ref.8"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70280"
FT VAR_SEQ 28..68
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12853575"
FT /id="VSP_017508"
FT VAR_SEQ 145..220
FT /note="DLVAQRGERLELLIDKTENLVDSSVTFKTTSRNLARAMCMKNLKLTIIIIIV
FT SIVFIYIIVSPLCGGFTWPSCVKK -> VCHLQNYQQKSCSSHVYEEPQAHYYHHHRIN
FT CVHLYHCFTSLWWIYMAKLCEEIGKKKLPLTKDMREQGVKSNPCDSSLSHTDRWYLPVS
FT STLFSLFKILFHASRFIFVLSTSLFL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_017509"
FT CONFLICT 98
FT /note="L -> P (in Ref. 5; BAD96514)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2DMW"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:2DMW"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2DMW"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:2DMW"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2DMW"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2DMW"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2DMW"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:2DMW"
FT HELIX 72..89
FT /evidence="ECO:0007829|PDB:2DMW"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:2DMW"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:2DMW"
SQ SEQUENCE 220 AA; 24935 MW; 9C1AA5C590375CEF CRC64;
MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY LFHYICQDRI
VYLCITDDDF ERSRAFNFLN EIKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN
KGLDKVMETQ AQVDELKGIM VRNIDLVAQR GERLELLIDK TENLVDSSVT FKTTSRNLAR
AMCMKNLKLT IIIIIVSIVF IYIIVSPLCG GFTWPSCVKK
