VAMP5_HUMAN
ID VAMP5_HUMAN Reviewed; 116 AA.
AC O95183; Q9P0T2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Vesicle-associated membrane protein 5;
DE Short=VAMP-5;
DE AltName: Full=Myobrevin;
GN Name=VAMP5; ORFNames=HSPC191;
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].
RX PubMed=9725904; DOI=10.1091/mbc.9.9.2423;
RA Zeng Q., Subramaniam V.N., Wong S.H., Tang B.L., Parton R.G., Rea S.,
RA James D.E., Hong W.;
RT "A novel synaptobrevin/VAMP homologous protein (VAMP5) is increased during
RT in vitro myogenesis and present in the plasma membrane.";
RL Mol. Biol. Cell 9:2423-2437(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-49, AND
RP IDENTIFICATION BY 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 [5]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE
RP X.
RX PubMed=28770820; DOI=10.1038/ncomms14130;
RA Zhang S., Masuyer G., Zhang J., Shen Y., Lundin D., Henriksson L.,
RA Miyashita S.I., Martinez-Carranza M., Dong M., Stenmark P.;
RT "Identification and characterization of a novel botulinum neurotoxin.";
RL Nat. Commun. 8:14130-14130(2017).
CC -!- FUNCTION: May participate in trafficking events that are associated
CC with myogenesis, such as myoblast fusion and/or GLUT4 trafficking.
CC -!- INTERACTION:
CC O95183; O95870: ABHD16A; NbExp=3; IntAct=EBI-10191195, EBI-348517;
CC O95183; Q13520: AQP6; NbExp=3; IntAct=EBI-10191195, EBI-13059134;
CC O95183; P07307-3: ASGR2; NbExp=3; IntAct=EBI-10191195, EBI-12808270;
CC O95183; O75787: ATP6AP2; NbExp=3; IntAct=EBI-10191195, EBI-2512037;
CC O95183; Q13323: BIK; NbExp=3; IntAct=EBI-10191195, EBI-700794;
CC O95183; P19397: CD53; NbExp=3; IntAct=EBI-10191195, EBI-6657396;
CC O95183; O00501: CLDN5; NbExp=3; IntAct=EBI-10191195, EBI-18400628;
CC O95183; O95471: CLDN7; NbExp=3; IntAct=EBI-10191195, EBI-740744;
CC O95183; P21964: COMT; NbExp=3; IntAct=EBI-10191195, EBI-372265;
CC O95183; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-10191195, EBI-18013275;
CC O95183; P55060: CSE1L; NbExp=2; IntAct=EBI-10191195, EBI-286709;
CC O95183; P00387: CYB5R3; NbExp=3; IntAct=EBI-10191195, EBI-1046040;
CC O95183; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-10191195, EBI-18535450;
CC O95183; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-10191195, EBI-781551;
CC O95183; P60508: ERVFRD-1; NbExp=3; IntAct=EBI-10191195, EBI-17973325;
CC O95183; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10191195, EBI-18304435;
CC O95183; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-10191195, EBI-12142257;
CC O95183; P48165: GJA8; NbExp=3; IntAct=EBI-10191195, EBI-17458373;
CC O95183; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-10191195, EBI-3917143;
CC O95183; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-10191195, EBI-13345167;
CC O95183; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10191195, EBI-11721746;
CC O95183; Q96HH9: GRAMD2B; NbExp=3; IntAct=EBI-10191195, EBI-2832937;
CC O95183; P31937: HIBADH; NbExp=3; IntAct=EBI-10191195, EBI-11427100;
CC O95183; Q13651: IL10RA; NbExp=3; IntAct=EBI-10191195, EBI-1031656;
CC O95183; P26951: IL3RA; NbExp=3; IntAct=EBI-10191195, EBI-1757512;
CC O95183; P16871: IL7R; NbExp=3; IntAct=EBI-10191195, EBI-80490;
CC O95183; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-10191195, EBI-10266796;
CC O95183; P43628: KIR2DL3; NbExp=3; IntAct=EBI-10191195, EBI-8632435;
CC O95183; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-10191195, EBI-17272405;
CC O95183; P26715: KLRC1; NbExp=3; IntAct=EBI-10191195, EBI-9018187;
CC O95183; Q08380: LGALS3BP; NbExp=2; IntAct=EBI-10191195, EBI-354956;
CC O95183; Q8N386: LRRC25; NbExp=3; IntAct=EBI-10191195, EBI-11304917;
CC O95183; P15941-11: MUC1; NbExp=3; IntAct=EBI-10191195, EBI-17263240;
CC O95183; Q6IBW4-4: NCAPH2; NbExp=3; IntAct=EBI-10191195, EBI-10247000;
CC O95183; Q96RD7: PANX1; NbExp=3; IntAct=EBI-10191195, EBI-7037612;
CC O95183; P15151: PVR; NbExp=3; IntAct=EBI-10191195, EBI-3919694;
CC O95183; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-10191195, EBI-7545592;
CC O95183; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-10191195, EBI-10192441;
CC O95183; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10191195, EBI-3920694;
CC O95183; A0A0S2Z4U3: SDC3; NbExp=3; IntAct=EBI-10191195, EBI-10204280;
CC O95183; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-10191195, EBI-2855401;
CC O95183; Q15849: SLC14A2; NbExp=3; IntAct=EBI-10191195, EBI-1573290;
CC O95183; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-10191195, EBI-17595455;
CC O95183; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-10191195, EBI-12898013;
CC O95183; A8K287: SNAP23; NbExp=3; IntAct=EBI-10191195, EBI-10188497;
CC O95183; O95721: SNAP29; NbExp=9; IntAct=EBI-10191195, EBI-490676;
CC O95183; Q99523: SORT1; NbExp=3; IntAct=EBI-10191195, EBI-1057058;
CC O95183; O43278-2: SPINT1; NbExp=3; IntAct=EBI-10191195, EBI-12078338;
CC O95183; O14662: STX16; NbExp=4; IntAct=EBI-10191195, EBI-2853548;
CC O95183; O14662-5: STX16; NbExp=3; IntAct=EBI-10191195, EBI-9089968;
CC O95183; Q16623: STX1A; NbExp=3; IntAct=EBI-10191195, EBI-712466;
CC O95183; P61266: STX1B; NbExp=3; IntAct=EBI-10191195, EBI-9071709;
CC O95183; P32856-2: STX2; NbExp=3; IntAct=EBI-10191195, EBI-11956649;
CC O95183; Q12846: STX4; NbExp=7; IntAct=EBI-10191195, EBI-744942;
CC O95183; Q13190: STX5; NbExp=4; IntAct=EBI-10191195, EBI-714206;
CC O95183; Q9UNK0: STX8; NbExp=4; IntAct=EBI-10191195, EBI-727240;
CC O95183; Q9NYW4: TAS2R5; NbExp=3; IntAct=EBI-10191195, EBI-17933167;
CC O95183; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-10191195, EBI-13351685;
CC O95183; Q8N6Q1: TMCO5A; NbExp=3; IntAct=EBI-10191195, EBI-12821895;
CC O95183; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-10191195, EBI-2821497;
CC O95183; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-10191195, EBI-7238458;
CC O95183; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-10191195, EBI-8638294;
CC O95183; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-10191195, EBI-3923061;
CC O95183; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-10191195, EBI-18178701;
CC O95183; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-10191195, EBI-2548832;
CC O95183; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-10191195, EBI-12345267;
CC O95183; Q9Y320: TMX2; NbExp=3; IntAct=EBI-10191195, EBI-6447886;
CC O95183; Q9Y279: VSIG4; NbExp=3; IntAct=EBI-10191195, EBI-903131;
CC O95183; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-10191195, EBI-12837904;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}. Endomembrane system {ECO:0000305};
CC Single-pass type IV membrane protein {ECO:0000305}. Golgi apparatus,
CC trans-Golgi network membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}. Note=Associated with the plasma
CC membrane as well as intracellular perinuclear and peripheral vesicular
CC structures of myotubes. Associated with the trans-Golgi, but not with
CC the cis-Golgi apparatus (By similarity). {ECO:0000250}.
CC -!- INDUCTION: During myogenesis.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type X (BoNT/X) which hydrolyzes the 40-Arg-|-Ser-41 bond
CC and probably inhibits neurotransmitter release (PubMed:28770820). It
CC remains unknown whether BoNT/X is ever produced, or what organisms it
CC targets. {ECO:0000269|PubMed:28770820}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF054825; AAC97473.1; -; mRNA.
DR EMBL; AF077197; AAD26992.1; -; mRNA.
DR EMBL; AF151025; AAF36111.1; -; mRNA.
DR EMBL; BC017891; AAH17891.1; -; mRNA.
DR CCDS; CCDS1980.1; -.
DR RefSeq; NP_006625.1; NM_006634.2.
DR AlphaFoldDB; O95183; -.
DR SMR; O95183; -.
DR BioGRID; 116007; 168.
DR IntAct; O95183; 135.
DR MINT; O95183; -.
DR STRING; 9606.ENSP00000305647; -.
DR iPTMnet; O95183; -.
DR MetOSite; O95183; -.
DR PhosphoSitePlus; O95183; -.
DR SwissPalm; O95183; -.
DR BioMuta; VAMP5; -.
DR EPD; O95183; -.
DR jPOST; O95183; -.
DR MassIVE; O95183; -.
DR PaxDb; O95183; -.
DR PeptideAtlas; O95183; -.
DR PRIDE; O95183; -.
DR ProteomicsDB; 50693; -.
DR Antibodypedia; 31895; 175 antibodies from 25 providers.
DR DNASU; 10791; -.
DR Ensembl; ENST00000306384.5; ENSP00000305647.4; ENSG00000168899.5.
DR GeneID; 10791; -.
DR KEGG; hsa:10791; -.
DR MANE-Select; ENST00000306384.5; ENSP00000305647.4; NM_006634.3; NP_006625.1.
DR CTD; 10791; -.
DR DisGeNET; 10791; -.
DR GeneCards; VAMP5; -.
DR HGNC; HGNC:12646; VAMP5.
DR HPA; ENSG00000168899; Low tissue specificity.
DR MIM; 607029; gene.
DR neXtProt; NX_O95183; -.
DR OpenTargets; ENSG00000168899; -.
DR PharmGKB; PA37270; -.
DR VEuPathDB; HostDB:ENSG00000168899; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00730000111371; -.
DR HOGENOM; CLU_064620_4_2_1; -.
DR InParanoid; O95183; -.
DR OMA; VRCRIYL; -.
DR OrthoDB; 1607213at2759; -.
DR PhylomeDB; O95183; -.
DR TreeFam; TF313666; -.
DR PathwayCommons; O95183; -.
DR SignaLink; O95183; -.
DR BioGRID-ORCS; 10791; 8 hits in 1081 CRISPR screens.
DR ChiTaRS; VAMP5; human.
DR GenomeRNAi; 10791; -.
DR Pharos; O95183; Tbio.
DR PRO; PR:O95183; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95183; protein.
DR Bgee; ENSG00000168899; Expressed in right lung and 173 other tissues.
DR ExpressionAtlas; O95183; baseline and differential.
DR Genevisible; O95183; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0031301; C:integral component of organelle membrane; ISS:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR CDD; cd15872; R-SNARE_VAMP5; 1.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR042855; V_SNARE_CC.
DR InterPro; IPR042166; Vamp5.
DR InterPro; IPR042581; VAMP5_R-SNARE.
DR PANTHER; PTHR47462; PTHR47462; 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 Cell membrane; Coiled coil; Developmental protein; Differentiation;
KW Golgi apparatus; Membrane; Myogenesis; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..116
FT /note="Vesicle-associated membrane protein 5"
FT /id="PRO_0000206733"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..116
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 5..65
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 96..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 40..41
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type X (BoNT/X)"
FT /evidence="ECO:0000269|PubMed:28770820"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2P8"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CONFLICT 17
FT /note="T -> M (in Ref. 2; AAF36111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 12805 MW; 32A1F3B808A6016C CRC64;
MAGIELERCQ QQANEVTEIM RNNFGKVLER GVKLAELQQR SDQLLDMSST FNKTTQNLAQ
KKCWENIRYR ICVGLVVVGV LLIILIVLLV VFLPQSSDSS SAPRTQDAGI ASGPGN
