VAMP8_HUMAN
ID VAMP8_HUMAN Reviewed; 100 AA.
AC Q9BV40; O60625; Q53SP9; Q6IB09;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Vesicle-associated membrane protein 8 {ECO:0000303|PubMed:12130530};
DE Short=VAMP-8 {ECO:0000303|PubMed:12130530};
DE AltName: Full=Endobrevin {ECO:0000303|PubMed:9614193};
DE Short=EDB {ECO:0000303|PubMed:9614193};
GN Name=VAMP8 {ECO:0000303|PubMed:12130530};
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], AND SUBCELLULAR LOCATION.
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 [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 15-24 AND 38-59, FUNCTION IN SECRETION, IDENTIFICATION
RP IN A COMPLEX WITH STX1A AND SNAP23, AND TISSUE SPECIFICITY.
RX PubMed=12130530; DOI=10.1182/blood.v100.3.1081;
RA Polgar J., Chung S.H., Reed G.L.;
RT "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in
RT human platelets and are required for granule secretion.";
RL Blood 100:1081-1083(2002).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [8]
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 [9]
RP FUNCTION IN AUTOPHAGY, AND INTERACTION WITH SNAP29 AND 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-18; THR-28; THR-48;
RP THR-54 AND SER-55, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [11]
RP INTERACTION WITH RAB21 AND SBF2, AND SUBCELLULAR LOCATION.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [13]
RP INTERACTION WITH STX17.
RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
RA Miao G., Zhang Y., Chen D., Zhang H.;
RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
RL Mol. Cell 0:0-0(2019).
RN [14]
RP INTERACTION WITH STX17.
RX PubMed=33422265; DOI=10.1016/j.devcel.2020.12.010;
RA Miao G., Zhao H., Li Y., Ji M., Chen Y., Shi Y., Bi Y., Wang P., Zhang H.;
RT "ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated
RT assembly of the SNARE complex required for autolysosome formation.";
RL Dev. Cell 56:427-442(2020).
RN [15]
RP FUNCTION, AND INTERACTION WITH TRIM6.
RX PubMed=31694946; DOI=10.1128/jvi.01454-19;
RA van Tol S., Atkins C., Bharaj P., Johnson K.N., Hage A., Freiberg A.N.,
RA Rajsbaum R.;
RT "VAMP8 Contributes to the TRIM6-Mediated Type I Interferon Antiviral
RT Response during West Nile Virus Infection.";
RL J. Virol. 94:0-0(2020).
RN [16]
RP STEAROYLATION AT LYS-64 AND LYS-68 (MICROBIAL INFECTION), AND MUTAGENESIS
RP OF 64-LYS--LYS-68 AND LYS-72.
RX PubMed=30061757; DOI=10.1038/s41564-018-0215-6;
RA Liu W., Zhou Y., Peng T., Zhou P., Ding X., Li Z., Zhong H., Xu Y.,
RA Chen S., Hang H.C., Shao F.;
RT "Nepsilon-fatty acylation of multiple membrane-associated proteins by
RT Shigella IcsB effector to modulate host function.";
RL Nat. Microbiol. 3:996-1009(2018).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 11-74 IN COMPLEX WITH STX17 AND
RP SNAP29, AND FUNCTION.
RX PubMed=25686604; DOI=10.1038/nature14147;
RA Diao J., Liu R., Rong Y., Zhao M., Zhang J., Lai Y., Zhou Q., Wilz L.M.,
RA Li J., Vivona S., Pfuetzner R.A., Brunger A.T., Zhong Q.;
RT "ATG14 promotes membrane tethering and fusion of autophagosomes to
RT endolysosomes.";
RL Nature 520:563-566(2015).
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 (PubMed:23217709, PubMed:25686604). Also required for
CC dense-granule secretion in platelets (PubMed:12130530). Also plays a
CC role in regulated enzyme secretion in pancreatic acinar cells (By
CC similarity). Involved in the abscission of the midbody during cell
CC division, which leads to completely separate daughter cells (By
CC similarity). Involved in the homotypic fusion of early and late
CC endosomes (By similarity). Participates also in the activation of type
CC I interferon antiviral response through a TRIM6-dependent mechanism
CC (PubMed:31694946). {ECO:0000250|UniProtKB:Q9WUF4,
CC ECO:0000269|PubMed:12130530, ECO:0000269|PubMed:23217709,
CC ECO:0000269|PubMed:25686604, ECO:0000269|PubMed:31694946}.
CC -!- SUBUNIT: Forms a SNARE complex composed of VAMP8, SNAP29 and STX17
CC involved in fusion of autophagosome with lysosome (PubMed:25686604).
CC Found in a number of SNARE complexes with NAPA, SNAP23, SNAP25, STX1A,
CC STX4, STX7, STX8 and VTI1B (PubMed:12130530). Interacts with PICALM (By
CC similarity). SNARE complex formation and binding by PICALM are mutually
CC exclusive processes for VAMP8 (By similarity). Interacts with
CC SBF2/MTMR13 (PubMed:25648148). Interacts with RAB21 (in GTP-bound form)
CC in response to starvation; the interaction probably regulates VAMP8
CC endolysosomal trafficking (PubMed:25648148). Interacts with STX17; this
CC interaction is increased in the absence of TMEM39A (PubMed:31806350,
CC PubMed:33422265). Interacts with TRIM6 (PubMed:31694946).
CC {ECO:0000250|UniProtKB:O70404, ECO:0000269|PubMed:12130530,
CC ECO:0000269|PubMed:25648148, ECO:0000269|PubMed:25686604,
CC ECO:0000269|PubMed:31694946, ECO:0000269|PubMed:31806350,
CC ECO:0000269|PubMed:33422265}.
CC -!- SUBUNIT: (Microbial infection) The interaction with STX17 is decreased
CC in presence of SARS coronavirus-2/SARS-CoV-2 ORF3A protein.
CC {ECO:0000269|PubMed:33422265}.
CC -!- INTERACTION:
CC Q9BV40; O95721: SNAP29; NbExp=6; IntAct=EBI-727028, EBI-490676;
CC Q9BV40; P56962: STX17; NbExp=11; IntAct=EBI-727028, EBI-2797775;
CC Q9BV40; O15400: STX7; NbExp=2; IntAct=EBI-727028, EBI-3221827;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:25686604};
CC Single-pass type IV membrane protein {ECO:0000305}. Early endosome
CC membrane {ECO:0000269|PubMed:25648148, ECO:0000269|PubMed:9614193};
CC Single-pass type IV membrane protein {ECO:0000305}. Late endosome
CC membrane {ECO:0000269|PubMed:25648148}; Single-pass type IV membrane
CC protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:O70404};
CC Single-pass type IV membrane protein {ECO:0000305}. Zymogen granule
CC membrane {ECO:0000250|UniProtKB:O70404}; Single-pass type IV membrane
CC protein {ECO:0000305}. Note=Perinuclear vesicular structures of the
CC early and late endosomes, coated pits, and trans-Golgi (By similarity).
CC Sub-tight junctional domain in retinal pigment epithelium cells.
CC Midbody region during cytokinesis. Lumenal oriented, apical membranes
CC of nephric tubular cell (By similarity). Cycles through the apical but
CC not through the basolateral plasma membrane (By similarity). Apical
CC region of acinar cells; in zymogen granule membranes (By similarity).
CC {ECO:0000250|UniProtKB:Q9WUF4}.
CC -!- TISSUE SPECIFICITY: Platelets. {ECO:0000269|PubMed:12130530}.
CC -!- PTM: (Microbial infection) Stearoylated By S.flexneri N-epsilon-fatty
CC acyltransferase IcsB, thereby disrupting the host actin cytoskeleton.
CC {ECO:0000269|PubMed:30061757}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF053233; AAC08434.1; -; mRNA.
DR EMBL; BT006700; AAP35346.1; -; mRNA.
DR EMBL; CR456995; CAG33276.1; -; mRNA.
DR EMBL; AC016753; AAY24341.1; -; Genomic_DNA.
DR EMBL; BC001634; AAH01634.1; -; mRNA.
DR CCDS; CCDS1979.1; -.
DR RefSeq; NP_003752.2; NM_003761.4.
DR PDB; 4WY4; X-ray; 1.40 A; A=11-74.
DR PDB; 7BV6; X-ray; 3.05 A; A/E/I/M/Q/U=8-75.
DR PDBsum; 4WY4; -.
DR PDBsum; 7BV6; -.
DR AlphaFoldDB; Q9BV40; -.
DR SMR; Q9BV40; -.
DR BioGRID; 114221; 89.
DR CORUM; Q9BV40; -.
DR DIP; DIP-40358N; -.
DR IntAct; Q9BV40; 32.
DR MINT; Q9BV40; -.
DR STRING; 9606.ENSP00000263864; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; Q9BV40; -.
DR MetOSite; Q9BV40; -.
DR PhosphoSitePlus; Q9BV40; -.
DR BioMuta; VAMP8; -.
DR DMDM; 55976764; -.
DR EPD; Q9BV40; -.
DR jPOST; Q9BV40; -.
DR MassIVE; Q9BV40; -.
DR MaxQB; Q9BV40; -.
DR PaxDb; Q9BV40; -.
DR PeptideAtlas; Q9BV40; -.
DR PRIDE; Q9BV40; -.
DR ProteomicsDB; 79166; -.
DR TopDownProteomics; Q9BV40; -.
DR Antibodypedia; 1528; 189 antibodies from 32 providers.
DR DNASU; 8673; -.
DR Ensembl; ENST00000263864.10; ENSP00000263864.5; ENSG00000118640.11.
DR GeneID; 8673; -.
DR KEGG; hsa:8673; -.
DR MANE-Select; ENST00000263864.10; ENSP00000263864.5; NM_003761.5; NP_003752.2.
DR UCSC; uc002spt.5; human.
DR CTD; 8673; -.
DR DisGeNET; 8673; -.
DR GeneCards; VAMP8; -.
DR HGNC; HGNC:12647; VAMP8.
DR HPA; ENSG00000118640; Low tissue specificity.
DR MIM; 603177; gene.
DR neXtProt; NX_Q9BV40; -.
DR OpenTargets; ENSG00000118640; -.
DR PharmGKB; PA37271; -.
DR VEuPathDB; HostDB:ENSG00000118640; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000160325; -.
DR HOGENOM; CLU_064620_5_0_1; -.
DR InParanoid; Q9BV40; -.
DR OMA; KQTSHKV; -.
DR OrthoDB; 1614157at2759; -.
DR PhylomeDB; Q9BV40; -.
DR TreeFam; TF320419; -.
DR PathwayCommons; Q9BV40; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
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-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q9BV40; -.
DR SIGNOR; Q9BV40; -.
DR BioGRID-ORCS; 8673; 7 hits in 1078 CRISPR screens.
DR ChiTaRS; VAMP8; human.
DR GeneWiki; Vesicle-associated_membrane_protein_8; -.
DR GenomeRNAi; 8673; -.
DR Pharos; Q9BV40; Tbio.
DR PRO; PR:Q9BV40; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BV40; protein.
DR Bgee; ENSG00000118640; Expressed in palpebral conjunctiva and 198 other tissues.
DR ExpressionAtlas; Q9BV40; baseline and differential.
DR Genevisible; Q9BV40; HS.
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:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; TAS:ProtInc.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IDA:UniProtKB.
DR GO; GO:0098594; C:mucin granule; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0019869; F:chloride channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IMP:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; IDA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0070254; P:mucus secretion; IMP:UniProtKB.
DR GO; GO:1903531; P:negative regulation of secretion by cell; IDA: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:1903076; P:regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0035493; P:SNARE complex assembly; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0046718; P:viral entry into host cell; 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; PS00417; SYNAPTOBREVIN; 1.
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; Direct protein sequencing; Endosome;
KW Lipoprotein; Lysosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..100
FT /note="Vesicle-associated membrane protein 8"
FT /id="PRO_0000206736"
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..100
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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 64
FT /note="(Microbial infection) N6-stearoyl lysine"
FT /evidence="ECO:0000269|PubMed:30061757"
FT LIPID 68
FT /note="(Microbial infection) N6-stearoyl lysine"
FT /evidence="ECO:0000269|PubMed:30061757"
FT MUTAGEN 64..68
FT /note="KVARK->RVARR: Abolished stearoylation in response to
FT S.flexneri infection."
FT /evidence="ECO:0000269|PubMed:30061757"
FT MUTAGEN 72
FT /note="K->R: Does not affect stearoylation in response to
FT S.flexneri infection."
FT /evidence="ECO:0000269|PubMed:30061757"
FT CONFLICT 12
FT /note="R -> L (in Ref. 1; AAC08434)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="C -> R (in Ref. 3; CAG33276)"
FT /evidence="ECO:0000305"
FT HELIX 12..72
FT /evidence="ECO:0007829|PDB:4WY4"
SQ SEQUENCE 100 AA; 11438 MW; 018B986442BBD9B6 CRC64;
MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT
TSQKVARKFW WKNVKMIVLI CVIVFIIILF IVLFATGAFS
