VAMP8_MOUSE
ID VAMP8_MOUSE Reviewed; 101 AA.
AC O70404; Q9CRA3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Vesicle-associated membrane protein 8 {ECO:0000303|PubMed:15363411};
DE Short=VAMP-8 {ECO:0000303|PubMed:15363411};
DE AltName: Full=Endobrevin {ECO:0000303|PubMed:15363411};
DE Short=Edb {ECO:0000250|UniProtKB:Q9BV40};
GN Name=Vamp8 {ECO:0000312|MGI:MGI:1336882};
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=9614193; DOI=10.1091/mbc.9.6.1549;
RA Wong S.H., Zhang T., Xu Y., Subramaniam V.N., Griffiths G., Hong W.;
RT "Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially
RT associated with the early endosome.";
RL Mol. Biol. Cell 9:1549-1563(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lu L., Bui T.D., Hong W.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND IDENTIFICATION IN
RP COMPLEXES WITH SNAP23; VTI1B; STX4 AND STX7.
RX PubMed=15363411; DOI=10.1016/j.devcel.2004.08.002;
RA Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F., Hong W.;
RT "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar
RT cells.";
RL Dev. Cell 7:359-371(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54 AND SER-55, AND
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Spleen;
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=27628032; DOI=10.1242/bio.018648;
RA Hubert V., Peschel A., Langer B., Groeger M., Rees A., Kain R.;
RT "LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and
RT for their fusion with lysosomes.";
RL Biol. Open 5:1516-1529(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 11-41 IN COMPLEX WITH PICALM,
RP INTERACTION WITH PICALM, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-24 AND MET-27.
RX PubMed=22118466; DOI=10.1016/j.cell.2011.10.038;
RA Miller S.E., Sahlender D.A., Graham S.C., Honing S., Robinson M.S.,
RA Peden A.A., Owen D.J.;
RT "The molecular basis for the endocytosis of small R-SNAREs by the clathrin
RT adaptor CALM.";
RL Cell 147:1118-1131(2011).
CC -!- FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment
CC protein receptors, are essential proteins for fusion of cellular
CC membranes. SNAREs localized on opposing membranes assemble to form a
CC trans-SNARE complex, an extended, parallel four alpha-helical bundle
CC that drives membrane fusion. VAMP8 is a SNARE involved in autophagy
CC through the direct control of autophagosome membrane fusion with the
CC lysososome membrane via its interaction with the STX17-SNAP29 binary t-
CC SNARE complex (By similarity). Also required for dense-granule
CC secretion in platelets (By similarity). Also plays a role in regulated
CC enzyme secretion in pancreatic acinar cells (PubMed:15363411). Involved
CC in the abscission of the midbody during cell division, which leads to
CC completely separate daughter cells (By similarity). Involved in the
CC homotypic fusion of early and late endosomes (By similarity).
CC Participates also in the activation of type I interferon antiviral
CC response through a TRIM6-dependent mechanism (By similarity).
CC {ECO:0000250|UniProtKB:Q9BV40, ECO:0000269|PubMed:15363411,
CC ECO:0000269|PubMed:22118466}.
CC -!- SUBUNIT: Forms a SNARE complex composed of VAMP8, SNAP29 and STX17
CC involved in fusion of autophagosome with lysosome (By similarity).
CC Found in a number of SNARE complexes with NAPA, SNAP23, SNAP25, STX1A,
CC STX4, STX7, STX8 and VTI1B (PubMed:15363411). Interacts with PICALM
CC (PubMed:22118466). SNARE complex formation and binding by PICALM are
CC mutually exclusive processes for VAMP8 (PubMed:22118466). Interacts
CC with SBF2/MTMR13 (By similarity). Interacts with RAB21 (in GTP-bound
CC form) in response to starvation; the interaction probably regulates
CC VAMP8 endolysosomal trafficking (By similarity). Interacts with STX17;
CC this interaction is increased in the absence of TMEM39A (By
CC similarity). Interacts with TRIM6 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BV40, ECO:0000269|PubMed:15363411,
CC ECO:0000269|PubMed:22118466}.
CC -!- INTERACTION:
CC O70404; O55012: Picalm; Xeno; NbExp=4; IntAct=EBI-1812572, EBI-915601;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:27628032};
CC Single-pass type IV membrane protein {ECO:0000305}. Late endosome
CC membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane
CC protein {ECO:0000305}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:22118466}; Single-pass
CC type IV membrane protein {ECO:0000305}. Zymogen granule membrane
CC {ECO:0000269|PubMed:15363411}; Single-pass type IV membrane protein
CC {ECO:0000305}. Note=Perinuclear vesicular structures of the early and
CC late endosomes, coated pits, and trans-Golgi (By similarity). Sub-tight
CC junctional domain in retinal pigment epithelium cells (By similarity).
CC Midbody region during cytokinesis (By similarity). Lumenal oriented,
CC apical membranes of nephric tubular cell (By similarity). Cycles
CC through the apical but not through the basolateral plasma membrane (By
CC similarity). Apical region of acinar cells; in zymogen granule
CC membranes (PubMed:15363411). {ECO:0000250|UniProtKB:Q9WUF4,
CC ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:9614193}.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the kidney, less in the
CC liver, brain, kidney, heart, lung, pancreas and placenta.
CC {ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:9553086}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF053724; AAC06371.1; -; mRNA.
DR EMBL; AF045661; AAC23665.1; -; mRNA.
DR EMBL; AF247556; AAK48423.1; -; Genomic_DNA.
DR EMBL; AK002268; BAB21977.1; -; mRNA.
DR EMBL; AK013279; BAB28766.1; -; mRNA.
DR EMBL; BC012668; AAH12668.1; -; mRNA.
DR CCDS; CCDS39514.1; -.
DR RefSeq; NP_058074.2; NM_016794.3.
DR PDB; 3ZYM; X-ray; 2.03 A; A/B/C=11-41.
DR PDBsum; 3ZYM; -.
DR AlphaFoldDB; O70404; -.
DR SMR; O70404; -.
DR BioGRID; 204497; 6.
DR CORUM; O70404; -.
DR IntAct; O70404; 3.
DR STRING; 10090.ENSMUSP00000059501; -.
DR iPTMnet; O70404; -.
DR PhosphoSitePlus; O70404; -.
DR EPD; O70404; -.
DR jPOST; O70404; -.
DR MaxQB; O70404; -.
DR PaxDb; O70404; -.
DR PeptideAtlas; O70404; -.
DR PRIDE; O70404; -.
DR ProteomicsDB; 298269; -.
DR DNASU; 22320; -.
DR GeneID; 22320; -.
DR KEGG; mmu:22320; -.
DR UCSC; uc009cin.2; mouse.
DR CTD; 8673; -.
DR MGI; MGI:1336882; Vamp8.
DR eggNOG; KOG0860; Eukaryota.
DR InParanoid; O70404; -.
DR OrthoDB; 1614157at2759; -.
DR PhylomeDB; O70404; -.
DR TreeFam; TF320419; -.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 22320; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Vamp8; mouse.
DR PRO; PR:O70404; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70404; protein.
DR GO; GO:0035577; C:azurophil granule membrane; ISO:MGI.
DR GO; GO:0045178; C:basal part of cell; IDA:MGI.
DR GO; GO:1990794; C:basolateral part of cell; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; TAS:MGI.
DR GO; GO:0031901; C:early endosome membrane; 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:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0098594; C:mucin granule; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0030667; C:secretory granule membrane; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0042588; C:zymogen granule; IDA:MGI.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0061025; P:membrane fusion; ISO:MGI.
DR GO; GO:0070254; P:mucus secretion; IMP:UniProtKB.
DR GO; GO:1903531; P:negative regulation of secretion by cell; ISO:MGI.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; ISO:MGI.
DR GO; GO:1902278; P:positive regulation of pancreatic amylase secretion; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:MGI.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0035493; P:SNARE complex assembly; IDA:BHF-UCL.
DR GO; GO:0006906; P:vesicle fusion; IMP:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR GO; GO:0070625; P:zymogen granule exocytosis; IMP:MGI.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR016444; Synaptobrevin/VAMP.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45701; PTHR45701; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antiviral defense; Autophagy; Cell membrane;
KW Coiled coil; Cytoplasmic vesicle; Endosome; Lysosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..101
FT /note="Vesicle-associated membrane protein 8"
FT /id="PRO_0000206737"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..101
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 12..72
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT SITE 33
FT /note="Interaction with STX8"
FT /evidence="ECO:0000250|UniProtKB:Q9WUF4"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 28
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV40"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MUTAGEN 24
FT /note="K->A: Blocks internalization from cell surface; when
FT associated with A-27."
FT /evidence="ECO:0000269|PubMed:22118466"
FT MUTAGEN 27
FT /note="M->A: Blocks internalization from cell surface; when
FT associated with A-24."
FT /evidence="ECO:0000269|PubMed:22118466"
FT CONFLICT 36
FT /note="S -> A (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT HELIX 16..37
FT /evidence="ECO:0007829|PDB:3ZYM"
SQ SEQUENCE 101 AA; 11451 MW; 0A2FDB6B69E06C3E CRC64;
MEEASGSAGN DRVRNLQSEV EGVKNIMTQN VERILSRGEN LDHLRNKTED LEATSEHFKT
TSQKVARKFW WKNVKMIVII CVIVLIIVIL IILFATGTIP T
