VAMP7_BOVIN
ID VAMP7_BOVIN Reviewed; 220 AA.
AC Q17QI5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Vesicle-associated membrane protein 7;
DE Short=VAMP-7;
DE AltName: Full=Synaptobrevin-like protein 1;
GN Name=VAMP7; Synonyms=SYBL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC Interacts with RAB21 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P51809}.
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:0000250}; Single-pass type IV membrane protein
CC {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000250}; Single-pass type IV membrane protein
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Note=In immature
CC neurons expression is localized in vesicular structures in axons and
CC dendrites while in mature neurons it is localized to the
CC somatodendritic region. Colocalizes with LAMP1 in kidney cells.
CC Localization to the endoplasmic reticulum membrane was observed in the
CC intestine but not in liver or kidney (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC118341; AAI18342.1; -; mRNA.
DR RefSeq; NP_001069770.1; NM_001076302.1.
DR AlphaFoldDB; Q17QI5; -.
DR BMRB; Q17QI5; -.
DR SMR; Q17QI5; -.
DR PRIDE; Q17QI5; -.
DR GeneID; 613984; -.
DR KEGG; bta:613984; -.
DR CTD; 6845; -.
DR InParanoid; Q17QI5; -.
DR OrthoDB; 1211929at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS: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:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0043308; P:eosinophil degranulation; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0043312; P:neutrophil degranulation; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006906; P:vesicle fusion; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS: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 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasmic vesicle; 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:0000250|UniProtKB:P51809"
FT CHAIN 2..220
FT /note="Vesicle-associated membrane protein 7"
FT /id="PRO_0000284056"
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"
FT /evidence="ECO:0000250|UniProtKB:P51809"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51809"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70280"
SQ SEQUENCE 220 AA; 24962 MW; 2DEB4AC581C74A83 CRC64;
MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY LFHYICQDRI
VYLCITDDDF ERSRAFNFLN EIKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN
KGLDKVMETQ AQVDELKGIM VRNIDLVAQR GERLELLIDK TENLVDSSVT FKTTSRNLAR
AMCMKNLKLT IIIIIISVVF IYIIVSPLCG GFTWPNCVKK
