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 02-OCT-2024, entry version 184. 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=8; IntAct=EBI-727028, EBI-490676; CC Q9BV40; P56962: STX17; NbExp=11; IntAct=EBI-727028, EBI-2797775; CC Q9BV40; O15400: STX7; NbExp=5; 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}. 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; 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; 112. DR CORUM; Q9BV40; -. DR DIP; DIP-40358N; -. DR IntAct; Q9BV40; 53. 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 SwissPalm; Q9BV40; -. DR BioMuta; VAMP8; -. DR DMDM; 55976764; -. DR jPOST; Q9BV40; -. DR MassIVE; Q9BV40; -. DR PaxDb; 9606-ENSP00000263864; -. DR PeptideAtlas; Q9BV40; -. DR ProteomicsDB; 79166; -. DR Pumba; Q9BV40; -. DR TopDownProteomics; Q9BV40; -. DR Antibodypedia; 1528; 210 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 AGR; HGNC:12647; -. 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; VRKKMWW; -. DR OrthoDB; 664519at2759; -. 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; 9 hits in 1156 CRISPR screens. DR ChiTaRS; VAMP8; human. DR EvolutionaryTrace; Q9BV40; -. 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 200 other cell types or tissues. DR ExpressionAtlas; Q9BV40; baseline and differential. 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: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:0042589; C:zymogen granule membrane; IEA:UniProtKB-SubCell. 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:0046718; P:symbiont entry into host cell; IMP:MGI. DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central. DR CDD; cd15868; R-SNARE_VAMP8; 1. DR Gene3D; 1.20.5.110; -; 1. DR InterPro; IPR001388; Synaptobrevin-like. DR InterPro; IPR016444; Synaptobrevin/VAMP. DR InterPro; IPR042855; V_SNARE_CC. DR PANTHER; PTHR45701; SYNAPTOBREVIN FAMILY MEMBER; 1. DR PANTHER; PTHR45701:SF7; VESICLE-ASSOCIATED MEMBRANE PROTEIN 8; 1. DR Pfam; PF00957; Synaptobrevin; 1. DR PIRSF; PIRSF005409; Synaptobrevin_euk; 1. DR PRINTS; PR00219; SYNAPTOBREVN. DR SUPFAM; SSF58038; SNARE fusion complex; 1. 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 Proteomics identification; Reference proteome; Transmembrane; KW 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 //