Full text data of VAMP8
VAMP8
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Vesicle-associated membrane protein 8; VAMP-8 (Endobrevin; EDB)
Vesicle-associated membrane protein 8; VAMP-8 (Endobrevin; EDB)
UniProt
Q9BV40
ID VAMP8_HUMAN Reviewed; 100 AA.
AC Q9BV40; O60625; Q53SP9; Q6IB09;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Vesicle-associated membrane protein 8;
DE Short=VAMP-8;
DE AltName: Full=Endobrevin;
DE Short=EDB;
GN Name=VAMP8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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
RT project: 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, AND
RP IDENTIFICATION IN A COMPLEX WITH STX1A AND SNAP23.
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
RT in 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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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, INTERACTION WITH SNAP29 AND STX17, AND
RP SUBCELLULAR LOCATION.
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
RT autophagosomes for fusion with endosomes/lysosomes.";
RL Cell 151:1256-1269(2012).
CC -!- FUNCTION: SNAREs, Soluble N-ethylmaleimide-sensitive factor-
CC attachment protein receptors, are essential proteins for fusion of
CC cellular membranes. SNAREs localized on opposing membranes
CC assemble to form a trans-SNARE complex, an extended, parallel four
CC alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE
CC involved in autophagy through the direct control of autophagosome
CC membrane fusion with the lysososome membrane. Also required for
CC dense-granule secretion in platelets. Plays also a role in
CC regulated enzyme secretion in pancreatic acinar cells. Involved in
CC the abscission of the midbody during cell division, which leads to
CC completely separate daughter cells. Involved in the homotypic
CC fusion of early and late endosomes.
CC -!- SUBUNIT: Forms a SNARE complex composed of VAMP8, SNAP29 and STX17
CC involved in fusion of autophagosome with lysosome. Binds tightly
CC to multiple syntaxins. Found in a number of SNARE complexes with
CC NAPA, SNAP23, SNAP25, STX1A, STX4, STX7, STX8 and VTI1B.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type IV
CC membrane protein (Probable). Late endosome membrane; Single-pass
CC type IV membrane protein (Probable). Note=Perinuclear vesicular
CC structures of the early and late endosomes, coated pits, and
CC trans-Golgi. Sub-tight junctional domain in retinal pigment
CC epithelium cells. Midbody region during cytokinesis. Lumenal
CC oriented, apical membranes of nephric tubular cell. Cycles through
CC the apical but not through the basolateral plasma membrane. Apical
CC region of acinar cells; in zymogen granule membranes (By
CC similarity).
CC -!- TISSUE SPECIFICITY: Platelets.
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_003752.2; NM_003761.4.
DR UniGene; Hs.714302; -.
DR ProteinModelPortal; Q9BV40; -.
DR SMR; Q9BV40; 12-64.
DR DIP; DIP-40358N; -.
DR IntAct; Q9BV40; 10.
DR MINT; MINT-4649115; -.
DR STRING; 9606.ENSP00000263864; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR PhosphoSite; Q9BV40; -.
DR DMDM; 55976764; -.
DR PaxDb; Q9BV40; -.
DR PeptideAtlas; Q9BV40; -.
DR PRIDE; Q9BV40; -.
DR DNASU; 8673; -.
DR Ensembl; ENST00000263864; ENSP00000263864; ENSG00000118640.
DR GeneID; 8673; -.
DR KEGG; hsa:8673; -.
DR UCSC; uc002spt.4; human.
DR CTD; 8673; -.
DR GeneCards; GC02P085788; -.
DR HGNC; HGNC:12647; VAMP8.
DR HPA; HPA006882; -.
DR MIM; 603177; gene.
DR neXtProt; NX_Q9BV40; -.
DR PharmGKB; PA37271; -.
DR eggNOG; NOG247118; -.
DR HOGENOM; HOG000042711; -.
DR HOVERGEN; HBG006675; -.
DR InParanoid; Q9BV40; -.
DR KO; K08512; -.
DR OMA; KMIVIIC; -.
DR PhylomeDB; Q9BV40; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR GeneWiki; Vesicle-associated_membrane_protein_8; -.
DR GenomeRNAi; 8673; -.
DR NextBio; 32533; -.
DR PRO; PR:Q9BV40; -.
DR ArrayExpress; Q9BV40; -.
DR Bgee; Q9BV40; -.
DR CleanEx; HS_VAMP8; -.
DR Genevestigator; Q9BV40; -.
DR GO; GO:0005769; C:early endosome; TAS:ProtInc.
DR GO; GO:0016021; C:integral to 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:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0000046; P:autophagic vacuole fusion; IMP:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0006461; P:protein complex assembly; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030100; P:regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0006906; P:vesicle fusion; IEA:Ensembl.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR016444; Synaptobrevin_met/fun.
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 Acetylation; Autophagy; Coiled coil; Complete proteome;
KW Direct protein sequencing; Endosome; Lysosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 100 Vesicle-associated membrane protein 8.
FT /FTId=PRO_0000206736.
FT TOPO_DOM 1 75 Cytoplasmic (Potential).
FT TRANSMEM 76 96 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 97 100 Vesicular (Potential).
FT DOMAIN 12 72 v-SNARE coiled-coil homology.
FT SITE 33 33 Interaction with STX8 (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 54 54 Phosphothreonine (By similarity).
FT MOD_RES 55 55 Phosphoserine (By similarity).
FT CONFLICT 12 12 R -> L (in Ref. 1; AAC08434).
FT CONFLICT 81 81 C -> R (in Ref. 3; CAG33276).
SQ SEQUENCE 100 AA; 11438 MW; 018B986442BBD9B6 CRC64;
MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT
TSQKVARKFW WKNVKMIVLI CVIVFIIILF IVLFATGAFS
//
ID VAMP8_HUMAN Reviewed; 100 AA.
AC Q9BV40; O60625; Q53SP9; Q6IB09;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Vesicle-associated membrane protein 8;
DE Short=VAMP-8;
DE AltName: Full=Endobrevin;
DE Short=EDB;
GN Name=VAMP8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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
RT project: 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, AND
RP IDENTIFICATION IN A COMPLEX WITH STX1A AND SNAP23.
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
RT in 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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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, INTERACTION WITH SNAP29 AND STX17, AND
RP SUBCELLULAR LOCATION.
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
RT autophagosomes for fusion with endosomes/lysosomes.";
RL Cell 151:1256-1269(2012).
CC -!- FUNCTION: SNAREs, Soluble N-ethylmaleimide-sensitive factor-
CC attachment protein receptors, are essential proteins for fusion of
CC cellular membranes. SNAREs localized on opposing membranes
CC assemble to form a trans-SNARE complex, an extended, parallel four
CC alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE
CC involved in autophagy through the direct control of autophagosome
CC membrane fusion with the lysososome membrane. Also required for
CC dense-granule secretion in platelets. Plays also a role in
CC regulated enzyme secretion in pancreatic acinar cells. Involved in
CC the abscission of the midbody during cell division, which leads to
CC completely separate daughter cells. Involved in the homotypic
CC fusion of early and late endosomes.
CC -!- SUBUNIT: Forms a SNARE complex composed of VAMP8, SNAP29 and STX17
CC involved in fusion of autophagosome with lysosome. Binds tightly
CC to multiple syntaxins. Found in a number of SNARE complexes with
CC NAPA, SNAP23, SNAP25, STX1A, STX4, STX7, STX8 and VTI1B.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type IV
CC membrane protein (Probable). Late endosome membrane; Single-pass
CC type IV membrane protein (Probable). Note=Perinuclear vesicular
CC structures of the early and late endosomes, coated pits, and
CC trans-Golgi. Sub-tight junctional domain in retinal pigment
CC epithelium cells. Midbody region during cytokinesis. Lumenal
CC oriented, apical membranes of nephric tubular cell. Cycles through
CC the apical but not through the basolateral plasma membrane. Apical
CC region of acinar cells; in zymogen granule membranes (By
CC similarity).
CC -!- TISSUE SPECIFICITY: Platelets.
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_003752.2; NM_003761.4.
DR UniGene; Hs.714302; -.
DR ProteinModelPortal; Q9BV40; -.
DR SMR; Q9BV40; 12-64.
DR DIP; DIP-40358N; -.
DR IntAct; Q9BV40; 10.
DR MINT; MINT-4649115; -.
DR STRING; 9606.ENSP00000263864; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR PhosphoSite; Q9BV40; -.
DR DMDM; 55976764; -.
DR PaxDb; Q9BV40; -.
DR PeptideAtlas; Q9BV40; -.
DR PRIDE; Q9BV40; -.
DR DNASU; 8673; -.
DR Ensembl; ENST00000263864; ENSP00000263864; ENSG00000118640.
DR GeneID; 8673; -.
DR KEGG; hsa:8673; -.
DR UCSC; uc002spt.4; human.
DR CTD; 8673; -.
DR GeneCards; GC02P085788; -.
DR HGNC; HGNC:12647; VAMP8.
DR HPA; HPA006882; -.
DR MIM; 603177; gene.
DR neXtProt; NX_Q9BV40; -.
DR PharmGKB; PA37271; -.
DR eggNOG; NOG247118; -.
DR HOGENOM; HOG000042711; -.
DR HOVERGEN; HBG006675; -.
DR InParanoid; Q9BV40; -.
DR KO; K08512; -.
DR OMA; KMIVIIC; -.
DR PhylomeDB; Q9BV40; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR GeneWiki; Vesicle-associated_membrane_protein_8; -.
DR GenomeRNAi; 8673; -.
DR NextBio; 32533; -.
DR PRO; PR:Q9BV40; -.
DR ArrayExpress; Q9BV40; -.
DR Bgee; Q9BV40; -.
DR CleanEx; HS_VAMP8; -.
DR Genevestigator; Q9BV40; -.
DR GO; GO:0005769; C:early endosome; TAS:ProtInc.
DR GO; GO:0016021; C:integral to 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:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0000046; P:autophagic vacuole fusion; IMP:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0006461; P:protein complex assembly; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030100; P:regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0006906; P:vesicle fusion; IEA:Ensembl.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR016444; Synaptobrevin_met/fun.
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 Acetylation; Autophagy; Coiled coil; Complete proteome;
KW Direct protein sequencing; Endosome; Lysosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 100 Vesicle-associated membrane protein 8.
FT /FTId=PRO_0000206736.
FT TOPO_DOM 1 75 Cytoplasmic (Potential).
FT TRANSMEM 76 96 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 97 100 Vesicular (Potential).
FT DOMAIN 12 72 v-SNARE coiled-coil homology.
FT SITE 33 33 Interaction with STX8 (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 54 54 Phosphothreonine (By similarity).
FT MOD_RES 55 55 Phosphoserine (By similarity).
FT CONFLICT 12 12 R -> L (in Ref. 1; AAC08434).
FT CONFLICT 81 81 C -> R (in Ref. 3; CAG33276).
SQ SEQUENCE 100 AA; 11438 MW; 018B986442BBD9B6 CRC64;
MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT
TSQKVARKFW WKNVKMIVLI CVIVFIIILF IVLFATGAFS
//
MIM
603177
*RECORD*
*FIELD* NO
603177
*FIELD* TI
*603177 VESICLE-ASSOCIATED MEMBRANE PROTEIN 8; VAMP8
;;ENDOBREVIN;;
SYNAPTOBREVIN-LIKE, ENDOSOME-ASSOCIATED
read more*FIELD* TX
DESCRIPTION
Synaptobrevins/VAMPs, syntaxins (e.g., 186590), and the 25-kD
synaptosomal-associated protein SNAP25 (600322) are the main components
of a protein complex involved in the docking and/or fusion of synaptic
vesicles with the presynaptic membrane. Bock and Scheller (1997)
reviewed the 'SNARE (SNAP receptor) hypothesis' of vesicular
trafficking.
CLONING
By searching sequence databases with the sequences of VAMP family
members, Wong et al. (1998) and Bock and Scheller (1997) identified
mammalian ESTs encoding VAMP8, or endobrevin, a protein with sequence
similarity to synaptobrevins. Wong et al. (1998) reported that the
predicted 100-amino acid human protein shares approximately 32%, 33%,
and 31% sequence identity with VAMP1 (185880), VAMP2 (185881), and
cellubrevin (VAMP3; 603657), respectively. Endobrevin migrates as a
15-kD protein on Western blots of mammalian cell extracts. Membrane
fractionation, immunofluorescence, and electron microscopy studies
demonstrated that endobrevin is associated with the perinuclear
vesicular structures of the early endocytic compartment.
Advani et al. (1998) cloned Vamp8 from an embryonic mouse cDNA library.
The deduced 101-amino acid protein contains an amphipathic helix that
may participate in coiled-coil interactions and a C-terminal hydrophobic
domain predicted to serve as a membrane anchor. Northern blot analysis
of mouse tissues revealed abundant expression in kidney, intermediate
expression in heart and spleen, and lower expression in brain, thymus,
and liver. Transfection of Vamp8 into normal rat kidney cells resulted
in broadly distributed puncta throughout the cell with a juxtanuclear
enrichment.
GENE FUNCTION
Using in vitro binding assays, Wong et al. (1998) found that endobrevin
interacts specifically with the soluble NSF (601633)-attachment protein
(NAPA; 603215), most likely through an endobrevin-containing SNARE
complex.
Low et al. (2003) found that 2 members of the SNARE membrane fusion
machinery, syntaxin-2 (EPIM; 132350) and Vamp8, localized to the midbody
during cytokinesis in rat and canine kidney cell lines. Inhibition of
syntaxin-2 and Vamp8 function by overexpression of nonmembrane-anchored
mutants caused failure of cytokinesis leading to the formation of
binucleated cells. Time-lapse microscopy showed that only midbody
abscission and not further upstream events, such as furrowing, were
affected.
Using RT-PCR, immunoblot analysis, and immunofluorescence microscopy,
Sander et al. (2008) demonstrated that human intestinal mast cells (MCs)
expressed SNAP23 (602534), STX1B (601485), STX2, STX3 (STX3A; 600876),
STX4 (STX4A; 186591), and STX6 (603944), but not SNAP25. MCs also
expressed VAMP3, VAMP7 (300053), and VAMP8, but, in contrast with rodent
MCs, they expressed only low levels of VAMP2. VAMP7 and VAMP8
translocated to the plasma membrane and interacted with SNAP23 and STX4
upon activation. Inhibition of STX4, SNAP23, VAMP7, or VAMP8, but not
VAMP2 or VAMP3, resulted in markedly reduced high-affinity IgE
receptor-mediated histamine release. Sander et al. (2008) concluded that
human MCs express a specific pattern of SNAREs and that VAMP7 and VAMP8,
but not VAMP2, are required for rapid degranulation.
MAPPING
By radiation hybrid analysis, Bui et al. (1998) mapped the VAMP8 gene to
human chromosome 2p12-p11.2 and to a region of conserved synteny on
mouse chromosome 6.
ANIMAL MODEL
Wang et al. (2004) found that Vamp8-null mice developed normally but
showed severe defects in the pancreas. Mutant acinar cells contained 3
times more zymogen granules than control acinar cells. Furthermore,
secretagogue-stimulated secretion was abolished in pancreatic fragments
derived from Vamp8-null mice. Mutant mice were partially resistant to
supramaximal cerulein-induced pancreatitis. Characterization of Vamp8
expression indicated that the protein was enriched on the membrane of
zymogen granules and existed in a complex with syntaxin-4 and Snap23.
Wang et al. (2004) concluded that VAMP8 plays a major role in regulating
exocytosis in pancreatic acinar cells by serving as a v-SNARE of zymogen
granules.
HISTORY
Pushparaj et al. (2009) reported studies in Vamp8 -/- mice suggesting
that VAMP8 is required for correct trafficking of secretory lysosomal
granules for exocytosis in macrophages and for the release of TNF.
Pushparaj and Tay (2013) retracted this paper because of the finding of
plagiarism and 'serious scientific misconduct' by one of the authors,
Dr. Melendez.
*FIELD* RF
1. Advani, R. J.; Bae, H.-R.; Bock, J. B.; Chao, D. S.; Doung, Y.-C.;
Prekeris, R.; Yoo, J.-S.; Scheller, R. H.: Seven novel mammalian
SNARE proteins localize to distinct membrane compartments. J. Biol.
Chem. 273: 10317-10324, 1998.
2. Bock, J. B.; Scheller, R. H.: A fusion of new ideas. Nature 387:
133-135, 1997.
3. Bui, T. D.; Wong, S. H.; Lu, L.; Hong, W.: Endobrevin maps to
chromosome 2 in human and chromosome 6 in mouse. Genomics 54: 579-580,
1998.
4. Low, S. H.; Li, X.; Miura, M.; Kudo, N.; Quinones, B.; Weimbs,
T.: Syntaxin 2 and endobrevin are required for the terminal step
of cytokinesis in mammalian cells. Dev. Cell 4: 753-759, 2003.
5. Pushparaj, P. N.; Tay, H. K.: Retraction: VAMP8 is essential in
anaphylatoxin-induced deregulation, TNF-alpha secretion, peritonitis,
and systemic inflammation. J. Immun. 190: 3007 only, 2013.
6. Pushparaj, P. N.; Tay, H. K.; Wang, C.-C.; Hong, W.; Melendez,
A. J.: VAMP8 is essential in anaphylatoxin-induced degranulation,
TNF-alpha secretion, peritonitis, and systemic inflammation. J. Immun. 183:
1413-1418, 2009. Note: Retraction: J. Immun. 190: 3007 only, 2013.
7. Sander, L. E.; Frank, S. P. C.; Bolat, S.; Blank, U.; Galli, T.;
Bigalke, H.; Bischoff, S. C.; Lorentz, A.: Vesicle associated membrane
protein (VAMP)-7 and VAMP-8, but not VAMP-2 or VAMP-3, are required
for activation-induced degranulation of mature human mast cells. Europ.
J. Immun. 38: 855-863, 2008.
8. Wang, C.-C.; Ng, C. P.; Lu, L.; Atlashkin, V.; Zhang, W.; Seet,
L.-F.; Hong, W.: A role of VAMP8/endobrevin in regulated exocytosis
of pancreatic acinar cells. Dev. Cell 7: 359-371, 2004.
9. Wong, S. H.; Zhang, T.; Xu, Y.; Subramaniam, V. N.; Griffiths,
G.; Hong, W.: Endobrevin, a novel synaptobrevin/VAMP-like protein
preferentially associated with the early endosome. Molec. Biol. Cell 9:
1549-1563, 1998.
*FIELD* CN
Paul J. Converse - updated: 11/3/2010
Paul J. Converse - updated: 10/9/2009
Patricia A. Hartz - updated: 9/2/2005
Patricia A. Hartz - updated: 10/7/2004
Patricia A. Hartz - updated: 5/7/2002
*FIELD* CD
Rebekah S. Rasooly: 10/21/1998
*FIELD* ED
carol: 10/01/2013
mgross: 11/4/2010
terry: 11/3/2010
mgross: 10/9/2009
mgross: 9/7/2005
terry: 9/2/2005
terry: 4/5/2005
mgross: 10/7/2004
carol: 5/7/2002
carol: 2/22/2002
carol: 3/18/1999
psherman: 11/30/1998
psherman: 10/22/1998
*RECORD*
*FIELD* NO
603177
*FIELD* TI
*603177 VESICLE-ASSOCIATED MEMBRANE PROTEIN 8; VAMP8
;;ENDOBREVIN;;
SYNAPTOBREVIN-LIKE, ENDOSOME-ASSOCIATED
read more*FIELD* TX
DESCRIPTION
Synaptobrevins/VAMPs, syntaxins (e.g., 186590), and the 25-kD
synaptosomal-associated protein SNAP25 (600322) are the main components
of a protein complex involved in the docking and/or fusion of synaptic
vesicles with the presynaptic membrane. Bock and Scheller (1997)
reviewed the 'SNARE (SNAP receptor) hypothesis' of vesicular
trafficking.
CLONING
By searching sequence databases with the sequences of VAMP family
members, Wong et al. (1998) and Bock and Scheller (1997) identified
mammalian ESTs encoding VAMP8, or endobrevin, a protein with sequence
similarity to synaptobrevins. Wong et al. (1998) reported that the
predicted 100-amino acid human protein shares approximately 32%, 33%,
and 31% sequence identity with VAMP1 (185880), VAMP2 (185881), and
cellubrevin (VAMP3; 603657), respectively. Endobrevin migrates as a
15-kD protein on Western blots of mammalian cell extracts. Membrane
fractionation, immunofluorescence, and electron microscopy studies
demonstrated that endobrevin is associated with the perinuclear
vesicular structures of the early endocytic compartment.
Advani et al. (1998) cloned Vamp8 from an embryonic mouse cDNA library.
The deduced 101-amino acid protein contains an amphipathic helix that
may participate in coiled-coil interactions and a C-terminal hydrophobic
domain predicted to serve as a membrane anchor. Northern blot analysis
of mouse tissues revealed abundant expression in kidney, intermediate
expression in heart and spleen, and lower expression in brain, thymus,
and liver. Transfection of Vamp8 into normal rat kidney cells resulted
in broadly distributed puncta throughout the cell with a juxtanuclear
enrichment.
GENE FUNCTION
Using in vitro binding assays, Wong et al. (1998) found that endobrevin
interacts specifically with the soluble NSF (601633)-attachment protein
(NAPA; 603215), most likely through an endobrevin-containing SNARE
complex.
Low et al. (2003) found that 2 members of the SNARE membrane fusion
machinery, syntaxin-2 (EPIM; 132350) and Vamp8, localized to the midbody
during cytokinesis in rat and canine kidney cell lines. Inhibition of
syntaxin-2 and Vamp8 function by overexpression of nonmembrane-anchored
mutants caused failure of cytokinesis leading to the formation of
binucleated cells. Time-lapse microscopy showed that only midbody
abscission and not further upstream events, such as furrowing, were
affected.
Using RT-PCR, immunoblot analysis, and immunofluorescence microscopy,
Sander et al. (2008) demonstrated that human intestinal mast cells (MCs)
expressed SNAP23 (602534), STX1B (601485), STX2, STX3 (STX3A; 600876),
STX4 (STX4A; 186591), and STX6 (603944), but not SNAP25. MCs also
expressed VAMP3, VAMP7 (300053), and VAMP8, but, in contrast with rodent
MCs, they expressed only low levels of VAMP2. VAMP7 and VAMP8
translocated to the plasma membrane and interacted with SNAP23 and STX4
upon activation. Inhibition of STX4, SNAP23, VAMP7, or VAMP8, but not
VAMP2 or VAMP3, resulted in markedly reduced high-affinity IgE
receptor-mediated histamine release. Sander et al. (2008) concluded that
human MCs express a specific pattern of SNAREs and that VAMP7 and VAMP8,
but not VAMP2, are required for rapid degranulation.
MAPPING
By radiation hybrid analysis, Bui et al. (1998) mapped the VAMP8 gene to
human chromosome 2p12-p11.2 and to a region of conserved synteny on
mouse chromosome 6.
ANIMAL MODEL
Wang et al. (2004) found that Vamp8-null mice developed normally but
showed severe defects in the pancreas. Mutant acinar cells contained 3
times more zymogen granules than control acinar cells. Furthermore,
secretagogue-stimulated secretion was abolished in pancreatic fragments
derived from Vamp8-null mice. Mutant mice were partially resistant to
supramaximal cerulein-induced pancreatitis. Characterization of Vamp8
expression indicated that the protein was enriched on the membrane of
zymogen granules and existed in a complex with syntaxin-4 and Snap23.
Wang et al. (2004) concluded that VAMP8 plays a major role in regulating
exocytosis in pancreatic acinar cells by serving as a v-SNARE of zymogen
granules.
HISTORY
Pushparaj et al. (2009) reported studies in Vamp8 -/- mice suggesting
that VAMP8 is required for correct trafficking of secretory lysosomal
granules for exocytosis in macrophages and for the release of TNF.
Pushparaj and Tay (2013) retracted this paper because of the finding of
plagiarism and 'serious scientific misconduct' by one of the authors,
Dr. Melendez.
*FIELD* RF
1. Advani, R. J.; Bae, H.-R.; Bock, J. B.; Chao, D. S.; Doung, Y.-C.;
Prekeris, R.; Yoo, J.-S.; Scheller, R. H.: Seven novel mammalian
SNARE proteins localize to distinct membrane compartments. J. Biol.
Chem. 273: 10317-10324, 1998.
2. Bock, J. B.; Scheller, R. H.: A fusion of new ideas. Nature 387:
133-135, 1997.
3. Bui, T. D.; Wong, S. H.; Lu, L.; Hong, W.: Endobrevin maps to
chromosome 2 in human and chromosome 6 in mouse. Genomics 54: 579-580,
1998.
4. Low, S. H.; Li, X.; Miura, M.; Kudo, N.; Quinones, B.; Weimbs,
T.: Syntaxin 2 and endobrevin are required for the terminal step
of cytokinesis in mammalian cells. Dev. Cell 4: 753-759, 2003.
5. Pushparaj, P. N.; Tay, H. K.: Retraction: VAMP8 is essential in
anaphylatoxin-induced deregulation, TNF-alpha secretion, peritonitis,
and systemic inflammation. J. Immun. 190: 3007 only, 2013.
6. Pushparaj, P. N.; Tay, H. K.; Wang, C.-C.; Hong, W.; Melendez,
A. J.: VAMP8 is essential in anaphylatoxin-induced degranulation,
TNF-alpha secretion, peritonitis, and systemic inflammation. J. Immun. 183:
1413-1418, 2009. Note: Retraction: J. Immun. 190: 3007 only, 2013.
7. Sander, L. E.; Frank, S. P. C.; Bolat, S.; Blank, U.; Galli, T.;
Bigalke, H.; Bischoff, S. C.; Lorentz, A.: Vesicle associated membrane
protein (VAMP)-7 and VAMP-8, but not VAMP-2 or VAMP-3, are required
for activation-induced degranulation of mature human mast cells. Europ.
J. Immun. 38: 855-863, 2008.
8. Wang, C.-C.; Ng, C. P.; Lu, L.; Atlashkin, V.; Zhang, W.; Seet,
L.-F.; Hong, W.: A role of VAMP8/endobrevin in regulated exocytosis
of pancreatic acinar cells. Dev. Cell 7: 359-371, 2004.
9. Wong, S. H.; Zhang, T.; Xu, Y.; Subramaniam, V. N.; Griffiths,
G.; Hong, W.: Endobrevin, a novel synaptobrevin/VAMP-like protein
preferentially associated with the early endosome. Molec. Biol. Cell 9:
1549-1563, 1998.
*FIELD* CN
Paul J. Converse - updated: 11/3/2010
Paul J. Converse - updated: 10/9/2009
Patricia A. Hartz - updated: 9/2/2005
Patricia A. Hartz - updated: 10/7/2004
Patricia A. Hartz - updated: 5/7/2002
*FIELD* CD
Rebekah S. Rasooly: 10/21/1998
*FIELD* ED
carol: 10/01/2013
mgross: 11/4/2010
terry: 11/3/2010
mgross: 10/9/2009
mgross: 9/7/2005
terry: 9/2/2005
terry: 4/5/2005
mgross: 10/7/2004
carol: 5/7/2002
carol: 2/22/2002
carol: 3/18/1999
psherman: 11/30/1998
psherman: 10/22/1998