VAMP7_RAT
ID VAMP7_RAT Reviewed; 220 AA.
AC Q9JHW5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10777677; DOI=10.1006/bbrc.2000.2591;
RA Hibi T., Hirashima N., Nakanishi M.;
RT "Rat basophilic leukemia cells express syntaxin-3 and VAMP-7 in granule
RT membranes.";
RL Biochem. Biophys. Res. Commun. 271:36-41(2000).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9553086; DOI=10.1074/jbc.273.17.10317;
RA Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C., Prekeris R.,
RA Yoo J.-S., Scheller R.H.;
RT "Seven novel mammalian SNARE proteins localize to distinct membrane
RT compartments.";
RL J. Biol. Chem. 273:10317-10324(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10459012; DOI=10.1083/jcb.146.4.765;
RA Advani R.J., Yang B., Prekeris R., Lee K.C., Klumperman J., Scheller R.H.;
RT "VAMP-7 mediates vesicular transport from endosomes to lysosomes.";
RL J. Cell Biol. 146:765-776(1999).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10559389; DOI=10.1523/jneurosci.19-22-09803.1999;
RA Coco S., Raposo G., Martinez S., Fontaine J.-J., Takamori S., Zahraoui A.,
RA Jahn R., Matteoli M., Louvard D., Galli T.;
RT "Subcellular localization of tetanus neurotoxin-insensitive vesicle-
RT associated membrane protein (VAMP)/VAMP7 in neuronal cells: evidence for a
RT novel membrane compartment.";
RL J. Neurosci. 19:9803-9812(1999).
RN [5]
RP FUNCTION, AND SNARE COMPLEX CHARACTERIZATION.
RX PubMed=15133481; DOI=10.1038/sj.embor.7400150;
RA Pryor P.R., Mullock B.M., Bright N.A., Lindsay M.R., Gray S.R.,
RA Richardson S.C.W., Stewart A., James D.E., Piper R.C., Luzio J.P.;
RT "Combinatorial SNARE complexes with VAMP7 or VAMP8 define different late
RT endocytic fusion events.";
RL EMBO Rep. 5:590-595(2004).
RN [6]
RP FUNCTION, AND SNARE COMPLEX CHARACTERIZATION.
RX PubMed=14993220; DOI=10.1074/jbc.m400798200;
RA Rao S.K., Huynh C., Proux-Gillardeaux V., Galli T., Andrews N.W.;
RT "Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal
RT exocytosis.";
RL J. Biol. Chem. 279:20471-20479(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16495485; DOI=10.1242/jcs.02803;
RA Siddiqi S.A., Mahan J., Siddiqi S., Gorelick F.S., Mansbach C.M. II;
RT "Vesicle-associated membrane protein 7 is expressed in intestinal ER.";
RL J. Cell Sci. 119:943-950(2006).
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:10459012,
CC ECO:0000269|PubMed:14993220, ECO:0000269|PubMed:15133481,
CC ECO:0000269|PubMed:16495485}.
CC -!- SUBUNIT: May interact with STX17 (By similarity). Component of the
CC SNARE complex composed of STX4, SNAP23 and VAMP7 that binds SYT7 during
CC lysosomal exocytosis. Component of the SNARE complex composed of STX7,
CC STX8, VAMP7 and VTI1B that is required for heterotypic fusion of late
CC endosomes with lysosomes. Interacts with PICALM (By similarity).
CC Interacts with RAB21 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P51809}.
CC -!- INTERACTION:
CC Q9JHW5; Q96NW4: ANKRD27; Xeno; NbExp=4; IntAct=EBI-919936, EBI-6125599;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane;
CC Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi
CC network membrane; Single-pass type IV membrane protein. Late endosome
CC membrane; Single-pass type IV membrane protein. Lysosome membrane;
CC Single-pass type IV membrane protein. Endoplasmic reticulum membrane;
CC Single-pass type IV membrane protein. Cytoplasmic vesicle, phagosome
CC 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.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, liver, lung, spleen and
CC thymus. Not expressed in heart and skeletal muscle.
CC {ECO:0000269|PubMed:10459012, ECO:0000269|PubMed:10559389,
CC ECO:0000269|PubMed:16495485, ECO:0000269|PubMed:9553086}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF281632; AAF88059.1; -; mRNA.
DR PIR; JC7258; JC7258.
DR RefSeq; NP_445983.1; NM_053531.1.
DR RefSeq; XP_006249078.1; XM_006249016.3.
DR AlphaFoldDB; Q9JHW5; -.
DR SMR; Q9JHW5; -.
DR BioGRID; 250111; 1.
DR CORUM; Q9JHW5; -.
DR DIP; DIP-37175N; -.
DR IntAct; Q9JHW5; 8.
DR MINT; Q9JHW5; -.
DR STRING; 10116.ENSRNOP00000011065; -.
DR PhosphoSitePlus; Q9JHW5; -.
DR SwissPalm; Q9JHW5; -.
DR jPOST; Q9JHW5; -.
DR PaxDb; Q9JHW5; -.
DR PRIDE; Q9JHW5; -.
DR Ensembl; ENSRNOT00000011065; ENSRNOP00000011065; ENSRNOG00000008372.
DR GeneID; 85491; -.
DR KEGG; rno:85491; -.
DR UCSC; RGD:621558; rat.
DR CTD; 6845; -.
DR RGD; 621558; Vamp7.
DR eggNOG; KOG0859; Eukaryota.
DR GeneTree; ENSGT00510000047733; -.
DR HOGENOM; CLU_064620_1_1_1; -.
DR InParanoid; Q9JHW5; -.
DR OMA; NTKLMIM; -.
DR OrthoDB; 1211929at2759; -.
DR PhylomeDB; Q9JHW5; -.
DR TreeFam; TF323448; -.
DR Reactome; R-RNO-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q9JHW5; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000008372; Expressed in liver and 19 other tissues.
DR Genevisible; Q9JHW5; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0035577; C:azurophil granule membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0031091; C:platelet alpha granule; ISO:RGD.
DR GO; GO:0031143; C:pseudopodium; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0030667; C:secretory granule membrane; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0030133; C:transport vesicle; ISO:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IPI:RGD.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
DR GO; GO:0043308; P:eosinophil degranulation; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:RGD.
DR GO; GO:0043320; P:natural killer cell degranulation; ISO:RGD.
DR GO; GO:0043312; P:neutrophil degranulation; IDA:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IDA:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; ISO:RGD.
DR GO; GO:1900483; P:regulation of protein targeting to vacuolar membrane; ISO:RGD.
DR GO; GO:0035493; P:SNARE complex assembly; ISO:RGD.
DR GO; GO:0034197; P:triglyceride transport; IMP:RGD.
DR GO; GO:0006906; P:vesicle fusion; IDA:UniProtKB.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IDA:RGD.
DR GO; GO:0047496; P:vesicle transport along microtubule; 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 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_0000316088"
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; 24776 MW; 527D818A23224A54 CRC64;
MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY LFHYICQDRI
VYLCITDDDF ERSRAFGFLN EVKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN
QSLDRVTETQ AQVDELKGIM VRNIDLVAQR GERLELLIDK TENLVDSSVT FKTTSRNLAR
AMCVKNVKLT AIIVVVSIVF IYIIVSPLCG GFTWPSCVKK
