ID   VAMP7_MOUSE             Reviewed;         220 AA.
AC   P70280;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 176.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9302271; DOI=10.1093/hmg/6.11.1917;
RA   D'Esposito M., Matarazzo M.R., Ciccodicola A., Strazzullo M.,
RA   Mazzarella R., Quaderi N.A., Fujiwara H., Ko M.S., Rowe L.B., Ricco A.,
RA   Archidiacono N., Rocchi M., Schlessinger D., D'Urso M.;
RT   "Differential expression pattern of XqPAR-linked genes SYBL1 and IL9R
RT   correlates with the structure and evolution of the region.";
RL   Hum. Mol. Genet. 6:1917-1923(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=10564831; DOI=10.1016/s0378-1119(99)00375-3;
RA   Matarazzo M.R., Cuccurese M., Strazzullo M., Vacca M., Curci A.,
RA   Miano M.G., Cocchia M., Mercadante G., Torino A., D'Urso M.,
RA   Ciccodicola A., D'Esposito M.;
RT   "Human and mouse SYBL1 gene structure and expression.";
RL   Gene 240:233-238(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Kidney, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15470500; DOI=10.1038/sj.emboj.7600427;
RA   Braun V., Fraisier V., Raposo G., Hurbain I., Sibarita J.-B., Chavrier P.,
RA   Galli T., Niedergang F.;
RT   "TI-VAMP/VAMP7 is required for optimal phagocytosis of opsonised particles
RT   in macrophages.";
RL   EMBO J. 23:4166-4176(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21998198; DOI=10.1091/mbc.e11-07-0592;
RA   Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B.,
RA   Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
RT   "The schizophrenia susceptibility factor dysbindin and its associated
RT   complex sort cargoes from cell bodies to the synapse.";
RL   Mol. Biol. Cell 22:4854-4867(2011).
RN   [9]
RP   INTERACTION WITH STX17.
RX   PubMed=23217709; DOI=10.1016/j.cell.2012.11.001;
RA   Itakura E., Kishi-Itakura C., Mizushima N.;
RT   "The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes
RT   for fusion with endosomes/lysosomes.";
RL   Cell 151:1256-1269(2012).
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:15470500}.
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 (By
CC       similarity). May interact with STX17. Interacts with PICALM (By
CC       similarity). Interacts with RAB21 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P51809}.
CC   -!- INTERACTION:
CC       P70280; O88384: Vti1b; NbExp=9; IntAct=EBI-6555653, EBI-775853;
CC       P70280; Q96NW4: ANKRD27; Xeno; NbExp=13; IntAct=EBI-6555653, EBI-6125599;
CC       P70280; P56962: STX17; Xeno; NbExp=2; IntAct=EBI-6555653, EBI-2797775;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane;
CC       Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi
CC       network membrane {ECO:0000250}; Single-pass type IV membrane protein
CC       {ECO:0000250}. Late endosome membrane; Single-pass type IV membrane
CC       protein. Lysosome membrane; Single-pass type IV membrane protein.
CC       Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV
CC       membrane protein {ECO:0000250}. Cytoplasmic vesicle, phagosome
CC       membrane; Single-pass type IV membrane protein. Synapse, synaptosome.
CC       Note=In immature neurons expression is localized in vesicular
CC       structures in axons and dendrites while in mature neurons it is
CC       localized to the somatodendritic region. Colocalizes with LAMP1 in
CC       kidney cells. Localization to the endoplasmic reticulum membrane was
CC       observed in the intestine but not in liver or kidney (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Loss-of-function mutant (antisense inhibition) displays
CC       impaired receptor-mediated phagocytosis.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; X96737; CAA65509.1; -; mRNA.
DR   EMBL; AJ133536; CAB94231.1; -; Genomic_DNA.
DR   EMBL; AJ133537; CAB94231.1; JOINED; Genomic_DNA.
DR   EMBL; AJ133538; CAB94231.1; JOINED; Genomic_DNA.
DR   EMBL; AJ133539; CAB94231.1; JOINED; Genomic_DNA.
DR   EMBL; AJ133540; CAB94231.1; JOINED; Genomic_DNA.
DR   EMBL; AJ133541; CAB94231.1; JOINED; Genomic_DNA.
DR   EMBL; AJ133542; CAB94231.1; JOINED; Genomic_DNA.
DR   EMBL; AK002825; BAB22386.1; -; mRNA.
DR   EMBL; AK011510; BAB27667.1; -; mRNA.
DR   EMBL; AK089035; BAC40712.1; -; mRNA.
DR   EMBL; AK165299; BAE38126.1; -; mRNA.
DR   EMBL; BC003764; AAH03764.1; -; mRNA.
DR   RefSeq; NP_001289067.1; NM_001302138.1.
DR   RefSeq; NP_035645.1; NM_011515.5.
DR   PDB; 2VX8; X-ray; 2.20 A; A/B/C/D=1-120.
DR   PDB; 4AFI; X-ray; 2.80 A; A/B=1-120.
DR   PDB; 4B93; X-ray; 2.00 A; A=1-187.
DR   PDBsum; 2VX8; -.
DR   PDBsum; 4AFI; -.
DR   PDBsum; 4B93; -.
DR   AlphaFoldDB; P70280; -.
DR   BMRB; P70280; -.
DR   SMR; P70280; -.
DR   BioGRID; 203595; 3.
DR   CORUM; P70280; -.
DR   DIP; DIP-46794N; -.
DR   IntAct; P70280; 12.
DR   MINT; P70280; -.
DR   STRING; 10090.ENSMUSP00000052262; -.
DR   iPTMnet; P70280; -.
DR   PhosphoSitePlus; P70280; -.
DR   SwissPalm; P70280; -.
DR   EPD; P70280; -.
DR   jPOST; P70280; -.
DR   MaxQB; P70280; -.
DR   PaxDb; 10090-ENSMUSP00000052262; -.
DR   PeptideAtlas; P70280; -.
DR   ProteomicsDB; 300113; -.
DR   Pumba; P70280; -.
DR   DNASU; 20955; -.
DR   GeneID; 20955; -.
DR   KEGG; mmu:20955; -.
DR   UCSC; uc009uym.2; mouse.
DR   AGR; MGI:1096399; -.
DR   CTD; 6845; -.
DR   MGI; MGI:1096399; Vamp7.
DR   VEuPathDB; HostDB:ENSMUSG00000051412; -.
DR   eggNOG; KOG0859; Eukaryota.
DR   HOGENOM; CLU_064620_1_1_1; -.
DR   InParanoid; P70280; -.
DR   OrthoDB; 664519at2759; -.
DR   PhylomeDB; P70280; -.
DR   TreeFam; TF323448; -.
DR   BioGRID-ORCS; 20955; 0 hits in 17 CRISPR screens.
DR   PRO; PR:P70280; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P70280; Protein.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0035577; C:azurophil granule membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0030175; C:filopodium; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR   GO; GO:0031143; C:pseudopodium; IDA:UniProtKB.
DR   GO; GO:0030141; C:secretory granule; ISO:MGI.
DR   GO; GO:0030667; C:secretory granule membrane; ISO:MGI.
DR   GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR   GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
DR   GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI.
DR   GO; GO:0043320; P:natural killer cell degranulation; ISO:MGI.
DR   GO; GO:0043312; P:neutrophil degranulation; ISS:UniProtKB.
DR   GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR   GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR   GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; ISO:MGI.
DR   GO; GO:1900483; P:regulation of protein targeting to vacuolar membrane; IMP:MGI.
DR   GO; GO:0035493; P:SNARE complex assembly; IDA:BHF-UCL.
DR   GO; GO:0034197; P:triglyceride transport; ISO:MGI.
DR   GO; GO:0006906; P:vesicle fusion; ISS:UniProtKB.
DR   GO; GO:0048280; P:vesicle fusion with Golgi apparatus; ISO:MGI.
DR   GO; GO:0047496; P:vesicle transport along microtubule; ISO:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR   CDD; cd14824; Longin; 1.
DR   CDD; cd15871; R-SNARE_VAMP7; 1.
DR   DisProt; DP02602; -.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 3.30.450.50; Longin domain; 1.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR010908; Longin_dom.
DR   InterPro; IPR001388; Synaptobrevin-like.
DR   InterPro; IPR042855; V_SNARE_CC.
DR   PANTHER; PTHR21136; SNARE PROTEINS; 1.
DR   PANTHER; PTHR21136:SF196; VESICLE-ASSOCIATED MEMBRANE PROTEIN 7; 1.
DR   Pfam; PF13774; Longin; 1.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   SMART; SM01270; Longin; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   SUPFAM; SSF64356; SNARE-like; 1.
DR   PROSITE; PS50859; LONGIN; 1.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
DR   Genevisible; P70280; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Cytoplasmic vesicle;
KW   Endoplasmic reticulum; Endosome; Exocytosis; Golgi apparatus; Lysosome;
KW   Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW   Signal-anchor; Synapse; Synaptosome; Transmembrane; Transmembrane helix;
KW   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_0000316087"
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:0007744|PubMed:19144319"
FT   STRAND          2..10
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   STRAND          13..23
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   HELIX           25..33
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   STRAND          38..47
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   STRAND          50..57
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   STRAND          60..67
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   HELIX           72..90
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   HELIX           91..95
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   TURN            99..102
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   HELIX           103..118
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   HELIX           130..134
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   TURN            135..138
FT                   /evidence="ECO:0007829|PDB:4B93"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:4B93"
SQ   SEQUENCE   220 AA;  24967 MW;  109DBA4BE5772B0C CRC64;
     MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY LFHYICQDRI
     VYLCITDDDF ERSRAFSFLN EVKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN
     KSLDKVMETQ AQVDELKGIM VRNIDLVAQR GERLELLIDK TENLVDSSVT FKTTSRNLAR
     AMCMKNIKLT IIIIIVSIVF IYIIVSLLCG GFTWPNCVKK
//