VAMP4_HUMAN
ID VAMP4_HUMAN Reviewed; 141 AA.
AC O75379; A2IDD8; Q96IY9; Q96J20; Q9UEL7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Vesicle-associated membrane protein 4;
DE Short=VAMP-4;
GN Name=VAMP4;
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] (ISOFORM 1).
RC TISSUE=B-cell;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Rhodes S.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, and Urinary bladder;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP INTERACTION WITH BAIAP3.
RX PubMed=28626000; DOI=10.1083/jcb.201702099;
RA Zhang X., Jiang S., Mitok K.A., Li L., Attie A.D., Martin T.F.J.;
RT "BAIAP3, a C2 domain-containing Munc13 protein, controls the fate of dense-
RT core vesicles in neuroendocrine cells.";
RL J. Cell Biol. 216:2151-2166(2017).
CC -!- FUNCTION: Involved in the pathway that functions to remove an inhibitor
CC (probably synaptotagmin-4) of calcium-triggered exocytosis during the
CC maturation of secretory granules. May be a marker for this sorting
CC pathway that is critical for remodeling the secretory response of
CC granule.
CC -!- SUBUNIT: Identified in a complex containing STX6, STX12, VAMP4 and
CC VTI1A (By similarity). Interacts with BAIAP3; this interaction is
CC increased in the presence of calcium (PubMed:28626000).
CC {ECO:0000250|UniProtKB:O70480, ECO:0000269|PubMed:28626000}.
CC -!- INTERACTION:
CC O75379; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-744953, EBI-7054139;
CC O75379; Q13520: AQP6; NbExp=3; IntAct=EBI-744953, EBI-13059134;
CC O75379; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-744953, EBI-11343438;
CC O75379; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-744953, EBI-1045797;
CC O75379; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-744953, EBI-18013275;
CC O75379; P00387: CYB5R3; NbExp=3; IntAct=EBI-744953, EBI-1046040;
CC O75379; Q15125: EBP; NbExp=3; IntAct=EBI-744953, EBI-3915253;
CC O75379; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-744953, EBI-18535450;
CC O75379; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-744953, EBI-781551;
CC O75379; P34910-2: EVI2B; NbExp=3; IntAct=EBI-744953, EBI-17640610;
CC O75379; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-744953, EBI-18304435;
CC O75379; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-744953, EBI-18938272;
CC O75379; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-744953, EBI-13345167;
CC O75379; Q8TED1: GPX8; NbExp=3; IntAct=EBI-744953, EBI-11721746;
CC O75379; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-744953, EBI-749265;
CC O75379; Q5T700: LDLRAD1; NbExp=3; IntAct=EBI-744953, EBI-10173166;
CC O75379; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-744953, EBI-17490413;
CC O75379; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-744953, EBI-11956541;
CC O75379; O14880: MGST3; NbExp=3; IntAct=EBI-744953, EBI-724754;
CC O75379; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-744953, EBI-3923617;
CC O75379; O14684: PTGES; NbExp=3; IntAct=EBI-744953, EBI-11161398;
CC O75379; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-744953, EBI-7545592;
CC O75379; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-744953, EBI-10192441;
CC O75379; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-744953, EBI-3920694;
CC O75379; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-744953, EBI-2855401;
CC O75379; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-744953, EBI-18159983;
CC O75379; Q5SQN1: SNAP47; NbExp=2; IntAct=EBI-744953, EBI-10244848;
CC O75379; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-744953, EBI-17280858;
CC O75379; P27105: STOM; NbExp=3; IntAct=EBI-744953, EBI-1211440;
CC O75379; O14662-5: STX16; NbExp=3; IntAct=EBI-744953, EBI-9089968;
CC O75379; Q16623: STX1A; NbExp=3; IntAct=EBI-744953, EBI-712466;
CC O75379; Q12846: STX4; NbExp=7; IntAct=EBI-744953, EBI-744942;
CC O75379; O43752: STX6; NbExp=2; IntAct=EBI-744953, EBI-2695795;
CC O75379; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-744953, EBI-8032987;
CC O75379; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-744953, EBI-6448756;
CC O75379; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-744953, EBI-6269551;
CC O75379; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-744953, EBI-726044;
CC O75379; Q9Y320: TMX2; NbExp=3; IntAct=EBI-744953, EBI-6447886;
CC O75379-2; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-10187996, EBI-747430;
CC O75379-2; Q53GS7: GLE1; NbExp=3; IntAct=EBI-10187996, EBI-1955541;
CC O75379-2; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-10187996, EBI-749265;
CC O75379-2; O95721: SNAP29; NbExp=3; IntAct=EBI-10187996, EBI-490676;
CC O75379-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10187996, EBI-5235340;
CC O75379-2; Q12846: STX4; NbExp=4; IntAct=EBI-10187996, EBI-744942;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
CC Note=Associated with trans Golgi network (TGN) and newly formed
CC immature secretory granules (ISG). Not found on the mature secretory
CC organelles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75379-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75379-2; Sequence=VSP_006326;
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF044310; AAC24032.1; -; mRNA.
DR EMBL; AL035296; CAA22896.1; -; mRNA.
DR EMBL; Z98751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90904.1; -; Genomic_DNA.
DR EMBL; BC005974; AAH05974.1; -; mRNA.
DR EMBL; BC007019; AAH07019.1; -; mRNA.
DR EMBL; BC031264; AAH31264.1; -; mRNA.
DR CCDS; CCDS1298.1; -. [O75379-1]
DR CCDS; CCDS53430.1; -. [O75379-2]
DR RefSeq; NP_001172056.1; NM_001185127.1. [O75379-2]
DR RefSeq; NP_003753.2; NM_003762.4. [O75379-1]
DR AlphaFoldDB; O75379; -.
DR SMR; O75379; -.
DR BioGRID; 114222; 131.
DR CORUM; O75379; -.
DR DIP; DIP-44226N; -.
DR IntAct; O75379; 94.
DR MINT; O75379; -.
DR STRING; 9606.ENSP00000236192; -.
DR iPTMnet; O75379; -.
DR PhosphoSitePlus; O75379; -.
DR SwissPalm; O75379; -.
DR BioMuta; VAMP4; -.
DR CPTAC; CPTAC-1035; -.
DR EPD; O75379; -.
DR jPOST; O75379; -.
DR MassIVE; O75379; -.
DR MaxQB; O75379; -.
DR PaxDb; O75379; -.
DR PeptideAtlas; O75379; -.
DR PRIDE; O75379; -.
DR ProteomicsDB; 49950; -. [O75379-1]
DR ProteomicsDB; 49951; -. [O75379-2]
DR Antibodypedia; 34381; 262 antibodies from 26 providers.
DR DNASU; 8674; -.
DR Ensembl; ENST00000236192.12; ENSP00000236192.7; ENSG00000117533.15. [O75379-1]
DR Ensembl; ENST00000367740.2; ENSP00000356714.2; ENSG00000117533.15. [O75379-2]
DR Ensembl; ENST00000474047.5; ENSP00000435933.1; ENSG00000117533.15. [O75379-1]
DR GeneID; 8674; -.
DR KEGG; hsa:8674; -.
DR MANE-Select; ENST00000236192.12; ENSP00000236192.7; NM_003762.5; NP_003753.2.
DR UCSC; uc001ghy.3; human. [O75379-1]
DR CTD; 8674; -.
DR DisGeNET; 8674; -.
DR GeneCards; VAMP4; -.
DR HGNC; HGNC:12645; VAMP4.
DR HPA; ENSG00000117533; Low tissue specificity.
DR MIM; 606909; gene.
DR neXtProt; NX_O75379; -.
DR OpenTargets; ENSG00000117533; -.
DR PharmGKB; PA37269; -.
DR VEuPathDB; HostDB:ENSG00000117533; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000155005; -.
DR HOGENOM; CLU_149550_0_0_1; -.
DR InParanoid; O75379; -.
DR OMA; WWRGCKV; -.
DR PhylomeDB; O75379; -.
DR TreeFam; TF313666; -.
DR PathwayCommons; O75379; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; O75379; -.
DR SIGNOR; O75379; -.
DR BioGRID-ORCS; 8674; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; VAMP4; human.
DR GeneWiki; VAMP4; -.
DR GenomeRNAi; 8674; -.
DR Pharos; O75379; Tbio.
DR PRO; PR:O75379; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75379; protein.
DR Bgee; ENSG00000117533; Expressed in endothelial cell and 211 other tissues.
DR ExpressionAtlas; O75379; baseline and differential.
DR Genevisible; O75379; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0090161; P:Golgi ribbon formation; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:0035493; P:SNARE complex assembly; IDA:BHF-UCL.
DR GO; GO:0016189; P:synaptic vesicle to endosome fusion; IEA:Ensembl.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR042855; V_SNARE_CC.
DR InterPro; IPR042887; VAMP4.
DR PANTHER; PTHR46897; PTHR46897; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..141
FT /note="Vesicle-associated membrane protein 4"
FT /id="PRO_0000206731"
FT TOPO_DOM 1..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..141
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 52..112
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70480"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006326"
FT CONFLICT 68
FT /note="Q -> P (in Ref. 1; AAC24032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 16397 MW; 556CC682D26CF91E CRC64;
MPPKFKRHLN DDDVTGSVKS ERRNLLEDDS DEEEDFFLRG PSGPRFGPRN DKIKHVQNQV
DEVIDVMQEN ITKVIERGER LDELQDKSES LSDNATAFSN RSKQLRRQMW WRGCKIKAIM
ALVAAILLLV IIILIVMKYR T
