Full text data of SNAP23
SNAP23
[Confidence: high (present in two of the MS resources)]
Synaptosomal-associated protein 23; SNAP-23 (Vesicle-membrane fusion protein SNAP-23)
Synaptosomal-associated protein 23; SNAP-23 (Vesicle-membrane fusion protein SNAP-23)
hRBCD
IPI00010438
IPI00010438 Splice isoform SNAP-23a of O00161 Synaptosomal-associated protein 23 Splice isoform SNAP-23a of O00161 Synaptosomal-associated protein 23 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a membrane bound splice isoform a and b found at its expected molecular weight found at molecular weight
IPI00010438 Splice isoform SNAP-23a of O00161 Synaptosomal-associated protein 23 Splice isoform SNAP-23a of O00161 Synaptosomal-associated protein 23 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a membrane bound splice isoform a and b found at its expected molecular weight found at molecular weight
Comments
Isoform O00161-2 was detected.
Isoform O00161-2 was detected.
UniProt
O00161
ID SNP23_HUMAN Reviewed; 211 AA.
AC O00161; O00162; Q13602; Q6IAE3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Synaptosomal-associated protein 23;
DE Short=SNAP-23;
DE AltName: Full=Vesicle-membrane fusion protein SNAP-23;
GN Name=SNAP23;
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] (ISOFORM SNAP-23A).
RC TISSUE=B-cell;
RX PubMed=8663154; DOI=10.1074/jbc.271.23.13300;
RA Ravichandran V., Chawla A., Roche P.A.;
RT "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding
RT protein, SNAP-23, expressed in non-neuronal tissues.";
RL J. Biol. Chem. 271:13300-13303(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SNAP-23A AND SNAP-23B).
RC TISSUE=Neutrophil;
RX PubMed=9070898; DOI=10.1006/bbrc.1997.6196;
RA Mollinedo F., Lazo P.A.;
RT "Identification of two isoforms of the vesicle-membrane fusion protein
RT SNAP-23 in human neutrophils and HL-60 cells.";
RL Biochem. Biophys. Res. Commun. 231:808-812(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=11354632; DOI=10.1007/s004390100480;
RA Lazo P.A., Nadal M., Ferrer M., Area E., Hernandez-Torres J.,
RA Nabokina S.M., Mollinedo F., Estivill X.;
RT "Genomic organization, chromosomal localization, alternative splicing,
RT and isoforms of human Synaptosome associated protein-23 gene
RT implicated in vesicle-membrane fusion.";
RL Hum. Genet. 108:211-215(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
RC TISSUE=Cervix, Placenta, and Testis;
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 [7]
RP PROTEIN SEQUENCE OF 1-12, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 1-12 AND 55-64, ACETYLATION AT MET-1, AND MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX1A.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASS
RP SPECTROMETRY.
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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-110, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PALMITOYLATION AT CYS-79; CYS-80; CYS-83; CYS-85; CYS-87 AND CYS-112.
RX PubMed=21044946; DOI=10.1194/jlr.D011106;
RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
RA Stamler J.S., Casey P.J.;
RT "Site-specific analysis of protein S-acylation by resin-assisted
RT capture.";
RL J. Lipid Res. 52:393-398(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-34 AND SER-110, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-76, COILED-COIL DOMAIN,
RP AND SUBUNIT.
RX PubMed=12556468; DOI=10.1074/jbc.M210483200;
RA Freedman S.J., Song H.K., Xu Y., Sun Z.Y., Eck M.J.;
RT "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil
RT domain.";
RL J. Biol. Chem. 278:13462-13467(2003).
CC -!- FUNCTION: Essential component of the high affinity receptor for
CC the general membrane fusion machinery and an important regulator
CC of transport vesicle docking and fusion.
CC -!- SUBUNIT: Homotetramer (via coiled-coil domain), also forms
CC heterotetramers with STX4 and VAMP3. Binds simultaneously to
CC SNAPIN and SYN4. Found in a complex with VAMP8 and STX4 in
CC pancreas. Interacts with STX1A and STX12 (By similarity). Binds
CC tightly to multiple syntaxins and synaptobrevins/VAMPs. Found in a
CC complex with VAMP8 and STX1A.
CC -!- INTERACTION:
CC P54920:NAPA; NbExp=2; IntAct=EBI-745000, EBI-749652;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Cell membrane; Lipid-anchor. Cell junction, synapse, synaptosome.
CC Note=Mainly localized to the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=SNAP-23a;
CC IsoId=O00161-1; Sequence=Displayed;
CC Name=SNAP-23b;
CC IsoId=O00161-2; Sequence=VSP_006187, VSP_006188;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels where found in
CC placenta.
CC -!- SIMILARITY: Belongs to the SNAP-25 family.
CC -!- SIMILARITY: Contains 2 t-SNARE coiled-coil homology domains.
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DR EMBL; U55936; AAC50537.1; -; mRNA.
DR EMBL; Y09567; CAA70760.1; -; mRNA.
DR EMBL; Y09568; CAA70761.1; -; mRNA.
DR EMBL; AJ011915; CAA09864.1; -; mRNA.
DR EMBL; AJ278972; CAC07504.1; -; Genomic_DNA.
DR EMBL; AJ278973; CAC07504.1; JOINED; Genomic_DNA.
DR EMBL; AJ278974; CAC07504.1; JOINED; Genomic_DNA.
DR EMBL; BT006916; AAP35562.1; -; mRNA.
DR EMBL; CR457212; CAG33493.1; -; mRNA.
DR EMBL; BC000148; AAH00148.1; -; mRNA.
DR EMBL; BC003686; AAH03686.1; -; mRNA.
DR EMBL; BC022890; AAH22890.1; -; mRNA.
DR PIR; JC5296; JC5296.
DR PIR; JC5297; JC5297.
DR RefSeq; NP_003816.2; NM_003825.3.
DR RefSeq; NP_570710.1; NM_130798.2.
DR RefSeq; XP_005254797.1; XM_005254740.1.
DR UniGene; Hs.511149; -.
DR PDB; 1NHL; X-ray; 2.30 A; A=23-76.
DR PDB; 3ZUS; X-ray; 2.95 A; A/B/C/D=150-209.
DR PDBsum; 1NHL; -.
DR PDBsum; 3ZUS; -.
DR ProteinModelPortal; O00161; -.
DR SMR; O00161; 23-76, 147-205.
DR IntAct; O00161; 13.
DR MINT; MINT-4999382; -.
DR STRING; 9606.ENSP00000249647; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR PhosphoSite; O00161; -.
DR OGP; O00161; -.
DR PaxDb; O00161; -.
DR PRIDE; O00161; -.
DR DNASU; 8773; -.
DR Ensembl; ENST00000249647; ENSP00000249647; ENSG00000092531.
DR Ensembl; ENST00000349777; ENSP00000207062; ENSG00000092531.
DR Ensembl; ENST00000397138; ENSP00000380327; ENSG00000092531.
DR GeneID; 8773; -.
DR KEGG; hsa:8773; -.
DR UCSC; uc001zpz.2; human.
DR CTD; 8773; -.
DR GeneCards; GC15P042787; -.
DR HGNC; HGNC:11131; SNAP23.
DR HPA; HPA001214; -.
DR MIM; 602534; gene.
DR neXtProt; NX_O00161; -.
DR PharmGKB; PA35979; -.
DR eggNOG; NOG259235; -.
DR HOGENOM; HOG000231599; -.
DR HOVERGEN; HBG056971; -.
DR InParanoid; O00161; -.
DR KO; K08508; -.
DR OMA; ETRTKNF; -.
DR PhylomeDB; O00161; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; SNAP23; human.
DR EvolutionaryTrace; O00161; -.
DR GeneWiki; SNAP23; -.
DR GenomeRNAi; 8773; -.
DR NextBio; 32894; -.
DR PMAP-CutDB; O00161; -.
DR PRO; PR:O00161; -.
DR ArrayExpress; O00161; -.
DR Bgee; O00161; -.
DR CleanEx; HS_SNAP23; -.
DR Genevestigator; O00161; -.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
DR InterPro; IPR000928; SNAP-25.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF00835; SNAP-25; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell junction;
KW Cell membrane; Coiled coil; Complete proteome;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Synapse; Synaptosome; Transport.
FT CHAIN 1 211 Synaptosomal-associated protein 23.
FT /FTId=PRO_0000213598.
FT DOMAIN 14 76 t-SNARE coiled-coil homology 1.
FT DOMAIN 146 208 t-SNARE coiled-coil homology 2.
FT COILED 23 76
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 20 20 Phosphoserine (By similarity).
FT MOD_RES 23 23 Phosphoserine (By similarity).
FT MOD_RES 34 34 Phosphoserine.
FT MOD_RES 110 110 Phosphoserine.
FT LIPID 79 79 S-palmitoyl cysteine.
FT LIPID 80 80 S-palmitoyl cysteine.
FT LIPID 83 83 S-palmitoyl cysteine.
FT LIPID 85 85 S-palmitoyl cysteine.
FT LIPID 87 87 S-palmitoyl cysteine.
FT LIPID 112 112 S-palmitoyl cysteine.
FT VAR_SEQ 89 89 R -> S (in isoform SNAP-23b).
FT /FTId=VSP_006187.
FT VAR_SEQ 90 142 Missing (in isoform SNAP-23b).
FT /FTId=VSP_006188.
FT CONFLICT 135 135 A -> V (in Ref. 1; AAC50537).
FT HELIX 24 74
SQ SEQUENCE 211 AA; 23354 MW; AC378E9786C3A239 CRC64;
MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE QLNRIEEGLD
QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK TTWGDGGENS PCNVVSKQPG
PVTNGQLQQP TTGAASGGYI KRITNDARED EMEENLTQVG SILGNLKDMA LNIGNEIDAQ
NPQIKRITDK ADTNRDRIDI ANARAKKLID S
//
ID SNP23_HUMAN Reviewed; 211 AA.
AC O00161; O00162; Q13602; Q6IAE3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Synaptosomal-associated protein 23;
DE Short=SNAP-23;
DE AltName: Full=Vesicle-membrane fusion protein SNAP-23;
GN Name=SNAP23;
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] (ISOFORM SNAP-23A).
RC TISSUE=B-cell;
RX PubMed=8663154; DOI=10.1074/jbc.271.23.13300;
RA Ravichandran V., Chawla A., Roche P.A.;
RT "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding
RT protein, SNAP-23, expressed in non-neuronal tissues.";
RL J. Biol. Chem. 271:13300-13303(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SNAP-23A AND SNAP-23B).
RC TISSUE=Neutrophil;
RX PubMed=9070898; DOI=10.1006/bbrc.1997.6196;
RA Mollinedo F., Lazo P.A.;
RT "Identification of two isoforms of the vesicle-membrane fusion protein
RT SNAP-23 in human neutrophils and HL-60 cells.";
RL Biochem. Biophys. Res. Commun. 231:808-812(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=11354632; DOI=10.1007/s004390100480;
RA Lazo P.A., Nadal M., Ferrer M., Area E., Hernandez-Torres J.,
RA Nabokina S.M., Mollinedo F., Estivill X.;
RT "Genomic organization, chromosomal localization, alternative splicing,
RT and isoforms of human Synaptosome associated protein-23 gene
RT implicated in vesicle-membrane fusion.";
RL Hum. Genet. 108:211-215(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
RC TISSUE=Cervix, Placenta, and Testis;
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 [7]
RP PROTEIN SEQUENCE OF 1-12, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 1-12 AND 55-64, ACETYLATION AT MET-1, AND MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX1A.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASS
RP SPECTROMETRY.
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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-110, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PALMITOYLATION AT CYS-79; CYS-80; CYS-83; CYS-85; CYS-87 AND CYS-112.
RX PubMed=21044946; DOI=10.1194/jlr.D011106;
RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
RA Stamler J.S., Casey P.J.;
RT "Site-specific analysis of protein S-acylation by resin-assisted
RT capture.";
RL J. Lipid Res. 52:393-398(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-34 AND SER-110, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-76, COILED-COIL DOMAIN,
RP AND SUBUNIT.
RX PubMed=12556468; DOI=10.1074/jbc.M210483200;
RA Freedman S.J., Song H.K., Xu Y., Sun Z.Y., Eck M.J.;
RT "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil
RT domain.";
RL J. Biol. Chem. 278:13462-13467(2003).
CC -!- FUNCTION: Essential component of the high affinity receptor for
CC the general membrane fusion machinery and an important regulator
CC of transport vesicle docking and fusion.
CC -!- SUBUNIT: Homotetramer (via coiled-coil domain), also forms
CC heterotetramers with STX4 and VAMP3. Binds simultaneously to
CC SNAPIN and SYN4. Found in a complex with VAMP8 and STX4 in
CC pancreas. Interacts with STX1A and STX12 (By similarity). Binds
CC tightly to multiple syntaxins and synaptobrevins/VAMPs. Found in a
CC complex with VAMP8 and STX1A.
CC -!- INTERACTION:
CC P54920:NAPA; NbExp=2; IntAct=EBI-745000, EBI-749652;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Cell membrane; Lipid-anchor. Cell junction, synapse, synaptosome.
CC Note=Mainly localized to the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=SNAP-23a;
CC IsoId=O00161-1; Sequence=Displayed;
CC Name=SNAP-23b;
CC IsoId=O00161-2; Sequence=VSP_006187, VSP_006188;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels where found in
CC placenta.
CC -!- SIMILARITY: Belongs to the SNAP-25 family.
CC -!- SIMILARITY: Contains 2 t-SNARE coiled-coil homology domains.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U55936; AAC50537.1; -; mRNA.
DR EMBL; Y09567; CAA70760.1; -; mRNA.
DR EMBL; Y09568; CAA70761.1; -; mRNA.
DR EMBL; AJ011915; CAA09864.1; -; mRNA.
DR EMBL; AJ278972; CAC07504.1; -; Genomic_DNA.
DR EMBL; AJ278973; CAC07504.1; JOINED; Genomic_DNA.
DR EMBL; AJ278974; CAC07504.1; JOINED; Genomic_DNA.
DR EMBL; BT006916; AAP35562.1; -; mRNA.
DR EMBL; CR457212; CAG33493.1; -; mRNA.
DR EMBL; BC000148; AAH00148.1; -; mRNA.
DR EMBL; BC003686; AAH03686.1; -; mRNA.
DR EMBL; BC022890; AAH22890.1; -; mRNA.
DR PIR; JC5296; JC5296.
DR PIR; JC5297; JC5297.
DR RefSeq; NP_003816.2; NM_003825.3.
DR RefSeq; NP_570710.1; NM_130798.2.
DR RefSeq; XP_005254797.1; XM_005254740.1.
DR UniGene; Hs.511149; -.
DR PDB; 1NHL; X-ray; 2.30 A; A=23-76.
DR PDB; 3ZUS; X-ray; 2.95 A; A/B/C/D=150-209.
DR PDBsum; 1NHL; -.
DR PDBsum; 3ZUS; -.
DR ProteinModelPortal; O00161; -.
DR SMR; O00161; 23-76, 147-205.
DR IntAct; O00161; 13.
DR MINT; MINT-4999382; -.
DR STRING; 9606.ENSP00000249647; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR PhosphoSite; O00161; -.
DR OGP; O00161; -.
DR PaxDb; O00161; -.
DR PRIDE; O00161; -.
DR DNASU; 8773; -.
DR Ensembl; ENST00000249647; ENSP00000249647; ENSG00000092531.
DR Ensembl; ENST00000349777; ENSP00000207062; ENSG00000092531.
DR Ensembl; ENST00000397138; ENSP00000380327; ENSG00000092531.
DR GeneID; 8773; -.
DR KEGG; hsa:8773; -.
DR UCSC; uc001zpz.2; human.
DR CTD; 8773; -.
DR GeneCards; GC15P042787; -.
DR HGNC; HGNC:11131; SNAP23.
DR HPA; HPA001214; -.
DR MIM; 602534; gene.
DR neXtProt; NX_O00161; -.
DR PharmGKB; PA35979; -.
DR eggNOG; NOG259235; -.
DR HOGENOM; HOG000231599; -.
DR HOVERGEN; HBG056971; -.
DR InParanoid; O00161; -.
DR KO; K08508; -.
DR OMA; ETRTKNF; -.
DR PhylomeDB; O00161; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; SNAP23; human.
DR EvolutionaryTrace; O00161; -.
DR GeneWiki; SNAP23; -.
DR GenomeRNAi; 8773; -.
DR NextBio; 32894; -.
DR PMAP-CutDB; O00161; -.
DR PRO; PR:O00161; -.
DR ArrayExpress; O00161; -.
DR Bgee; O00161; -.
DR CleanEx; HS_SNAP23; -.
DR Genevestigator; O00161; -.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
DR InterPro; IPR000928; SNAP-25.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF00835; SNAP-25; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell junction;
KW Cell membrane; Coiled coil; Complete proteome;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Synapse; Synaptosome; Transport.
FT CHAIN 1 211 Synaptosomal-associated protein 23.
FT /FTId=PRO_0000213598.
FT DOMAIN 14 76 t-SNARE coiled-coil homology 1.
FT DOMAIN 146 208 t-SNARE coiled-coil homology 2.
FT COILED 23 76
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 20 20 Phosphoserine (By similarity).
FT MOD_RES 23 23 Phosphoserine (By similarity).
FT MOD_RES 34 34 Phosphoserine.
FT MOD_RES 110 110 Phosphoserine.
FT LIPID 79 79 S-palmitoyl cysteine.
FT LIPID 80 80 S-palmitoyl cysteine.
FT LIPID 83 83 S-palmitoyl cysteine.
FT LIPID 85 85 S-palmitoyl cysteine.
FT LIPID 87 87 S-palmitoyl cysteine.
FT LIPID 112 112 S-palmitoyl cysteine.
FT VAR_SEQ 89 89 R -> S (in isoform SNAP-23b).
FT /FTId=VSP_006187.
FT VAR_SEQ 90 142 Missing (in isoform SNAP-23b).
FT /FTId=VSP_006188.
FT CONFLICT 135 135 A -> V (in Ref. 1; AAC50537).
FT HELIX 24 74
SQ SEQUENCE 211 AA; 23354 MW; AC378E9786C3A239 CRC64;
MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE QLNRIEEGLD
QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK TTWGDGGENS PCNVVSKQPG
PVTNGQLQQP TTGAASGGYI KRITNDARED EMEENLTQVG SILGNLKDMA LNIGNEIDAQ
NPQIKRITDK ADTNRDRIDI ANARAKKLID S
//
MIM
602534
*RECORD*
*FIELD* NO
602534
*FIELD* TI
*602534 SYNAPTOSOMAL-ASSOCIATED PROTEIN, 23-KD; SNAP23
;;SNAP23A
SNAP23B;;
SNAP23C;;
read moreSNAP23D;;
SNAP23E
*FIELD* TX
DESCRIPTION
Synaptosomal-associated proteins (SNAPs), such as SNAP23, are involved
in the process of membrane fusion in intracellular vesicle traffic
(Ravichandran et al., 1996).
CLONING
Ravichandran et al. (1996) used syntaxin-4 (186591) as bait in
expression cloning to isolate novel proteins involved in membrane fusion
in other cell types. From a human B-cell lymphocyte library, they
identified SNAP23, which shows homology to SNAP25 (600322). SNAP25 is
part of a complex, termed 'SNARE,' that is responsible for membrane
fusion in neurons. The SNAP23 cDNA encodes a 211-amino acid polypeptide
with a predicted mass of 23 kD. Its amino acid sequence is 59% identical
to that of SNAP25. Northern blot analysis revealed that SNAP23 is
ubiquitously expressed.
Mollinedo and Lazo (1997) used RT-PCR to identify an alternatively
spliced variant of SNAP23 in human neutrophils. This isoform, termed
SNAP23B, encodes a protein sequence of 158 amino acids with a deduced
mass of 17.8 kD. Lazo et al. (2001) determined that SNAP23B lacks a
region that is required for nonspecific binding to plasma membranes.
Shukla et al. (2001) identified 3 additional splice variants that they
designated SNAP23C, SNAP23D, and SNAP23E, all of which showed deletions
in comparison with SNAP23A. With use of variant-specific primers in
RT-PCR, they found mRNA for all 5 SNAP23 variants in human eosinophils,
peripheral blood mononuclear cells, neutrophils, brain tissue, and
basophilic and eosinophilic cell lines. Transfection of a basophilic
cell line with reporter constructs for each of these variants revealed a
plasma membrane localization for SNAPA and SNAPB, and both membrane and
intracellular localization for SNAP23C, SNAPD, and SNAP23E.
GENE FUNCTION
Ravichandran et al. (1996) determined that SNAP23 is able to bind to
multiple syntaxins as well as to multiple vesicle-associated membrane
proteins (see 185880).
Guo et al. (1998) reported that SNAP23 relocates in response to
stimulation from plasma membrane lamellipodia-like projections to
granule membranes in permeabilized mast cells. While relocation is a
prerequisite for secretion, it can occur without membrane fusion and
will expedite a subsequent secretory response. After relocation, SNAP23
is required for exocytosis, implying a crucial role in promoting
membrane fusion. Thus, relocation of SNAP23 regulates compound
exocytosis and links granule-plasma membrane and granule-granule
fusions.
Using immunofluorescence and immunoelectron microscopy, Galli et al.
(1998) demonstrated that human TIVAMP (VAMP7; 300053), syntaxin-3
(STX3A; 600876), and SNAP23, were insensitive to proteolysis by numerous
clostridial neurotoxins (NTs). TIVAMP-containing vesicles were
concentrated in the apical domain of epithelial cells. STX3A and SNAP23
were codistributed at the apical plasma membrane, where they formed
N-ethyl maleimide-dependent SNARE complexes with TIVAMP and cellubrevin
(VAMP3; 603657). Galli et al. (1998) proposed that TIVAMP, STX3A, and
SNAP23 participate in exocytotic processes at the apical plasma membrane
of epithelial cells and in clostridial NT-resistant pathways.
Using RT-PCR, immunoblot analysis, and immunofluorescence microscopy,
Sander et al. (2008) demonstrated that human intestinal mast cells (MCs)
expressed SNAP23, STX1B (601485), STX2 (132350), STX3, STX4 (STX4A;
186591), and STX6 (603944), but not SNAP25. MCs also expressed VAMP3,
VAMP7, and VAMP8 (603177), but, in contrast with rodent MCs, they
expressed only low levels of VAMP2 (185881). 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.
GENE STRUCTURE
Lazo et al. (2001) found that the SNAP23 gene has 8 exons, with the
initiation codon located in exon 2. They determined that SNAP23B is the
result of alternative splicing where exon 5 is joined to exon 7,
skipping exon 6.
MAPPING
By fluorescence in situ hybridization, Lazo et al. (2001) mapped the
SNAP23 gene to chromosome 15q21-q22. Lazo et al. (2001) suggested that
alterations in the SNAP23 gene may be involved in neurologic and other
diseases with defects in vesicle-membrane fusion processes that map to
15q15-q21.
*FIELD* RF
1. Galli, T.; Zahraoui, A.; Vaidyanathan, V. V.; Raposo, G.; Tian,
J. M.; Karin, M.; Niemann, H.; Louvard, D.: A novel tetanus neurotoxin-insensitive
vesicle-associated membrane protein in SNARE complexes of the apical
plasma membrane of epithelial cells. Molec. Biol. Cell 9: 1437-1448,
1998.
2. Guo, Z.; Turner, C.; Castle, D.: Relocation of the t-SNARE SNAP-23
from lamellipodia-like cell surface projections regulates compound
exocytosis in mast cells. Cell 94: 537-548, 1998.
3. Lazo, P. A.; Nadal, M.; Ferrer, M.; Area, E.; Hernandez-Torres,
J.; Nabokina, S. M.; Mollinedo, F.; Estivill, X.: Genomic organization,
chromosomal localization, alternative splicing, and isoforms of the
human synaptosome-associated protein-23 gene implicated in vesicle-membrane
fusion processes. Hum. Genet. 108: 211-215, 2001.
4. Mollinedo, F.; Lazo, P. A.: Identification of two isoforms of
the vesicle-membrane fusion protein SNAP-23 in human neutrophils and
HL-60 cells. Biochem. Biophys. Res. Commun. 231: 808-812, 1997.
5. Ravichandran, V.; Chawla, A.; Roche, P. A.: Identification of
a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23,
expressed in non-neuronal tissues. J. Biol. Chem. 271: 13300-13303,
1996.
6. 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.
7. Shukla, A.; Corydon, T. J.; Nielsen, S.; Hoffmann, H. J.; Dahl,
R.: Identification of three new splice variants of the SNARE protein
SNAP-23. Biochem. Biophys. Res. Commun. 285: 320-327, 2001.
*FIELD* CN
Paul J. Converse - updated: 10/8/2009
Patricia A. Hartz - updated: 5/1/2002
Victor A. McKusick - updated: 4/6/2001
Stylianos E. Antonarakis - updated: 9/15/1998
*FIELD* CD
Jennifer P. Macke: 4/20/1998
*FIELD* ED
mgross: 10/09/2009
mgross: 10/9/2009
terry: 10/8/2009
carol: 5/1/2002
mcapotos: 4/16/2001
mcapotos: 4/9/2001
terry: 4/6/2001
carol: 12/22/1998
carol: 9/15/1998
dholmes: 5/12/1998
*RECORD*
*FIELD* NO
602534
*FIELD* TI
*602534 SYNAPTOSOMAL-ASSOCIATED PROTEIN, 23-KD; SNAP23
;;SNAP23A
SNAP23B;;
SNAP23C;;
read moreSNAP23D;;
SNAP23E
*FIELD* TX
DESCRIPTION
Synaptosomal-associated proteins (SNAPs), such as SNAP23, are involved
in the process of membrane fusion in intracellular vesicle traffic
(Ravichandran et al., 1996).
CLONING
Ravichandran et al. (1996) used syntaxin-4 (186591) as bait in
expression cloning to isolate novel proteins involved in membrane fusion
in other cell types. From a human B-cell lymphocyte library, they
identified SNAP23, which shows homology to SNAP25 (600322). SNAP25 is
part of a complex, termed 'SNARE,' that is responsible for membrane
fusion in neurons. The SNAP23 cDNA encodes a 211-amino acid polypeptide
with a predicted mass of 23 kD. Its amino acid sequence is 59% identical
to that of SNAP25. Northern blot analysis revealed that SNAP23 is
ubiquitously expressed.
Mollinedo and Lazo (1997) used RT-PCR to identify an alternatively
spliced variant of SNAP23 in human neutrophils. This isoform, termed
SNAP23B, encodes a protein sequence of 158 amino acids with a deduced
mass of 17.8 kD. Lazo et al. (2001) determined that SNAP23B lacks a
region that is required for nonspecific binding to plasma membranes.
Shukla et al. (2001) identified 3 additional splice variants that they
designated SNAP23C, SNAP23D, and SNAP23E, all of which showed deletions
in comparison with SNAP23A. With use of variant-specific primers in
RT-PCR, they found mRNA for all 5 SNAP23 variants in human eosinophils,
peripheral blood mononuclear cells, neutrophils, brain tissue, and
basophilic and eosinophilic cell lines. Transfection of a basophilic
cell line with reporter constructs for each of these variants revealed a
plasma membrane localization for SNAPA and SNAPB, and both membrane and
intracellular localization for SNAP23C, SNAPD, and SNAP23E.
GENE FUNCTION
Ravichandran et al. (1996) determined that SNAP23 is able to bind to
multiple syntaxins as well as to multiple vesicle-associated membrane
proteins (see 185880).
Guo et al. (1998) reported that SNAP23 relocates in response to
stimulation from plasma membrane lamellipodia-like projections to
granule membranes in permeabilized mast cells. While relocation is a
prerequisite for secretion, it can occur without membrane fusion and
will expedite a subsequent secretory response. After relocation, SNAP23
is required for exocytosis, implying a crucial role in promoting
membrane fusion. Thus, relocation of SNAP23 regulates compound
exocytosis and links granule-plasma membrane and granule-granule
fusions.
Using immunofluorescence and immunoelectron microscopy, Galli et al.
(1998) demonstrated that human TIVAMP (VAMP7; 300053), syntaxin-3
(STX3A; 600876), and SNAP23, were insensitive to proteolysis by numerous
clostridial neurotoxins (NTs). TIVAMP-containing vesicles were
concentrated in the apical domain of epithelial cells. STX3A and SNAP23
were codistributed at the apical plasma membrane, where they formed
N-ethyl maleimide-dependent SNARE complexes with TIVAMP and cellubrevin
(VAMP3; 603657). Galli et al. (1998) proposed that TIVAMP, STX3A, and
SNAP23 participate in exocytotic processes at the apical plasma membrane
of epithelial cells and in clostridial NT-resistant pathways.
Using RT-PCR, immunoblot analysis, and immunofluorescence microscopy,
Sander et al. (2008) demonstrated that human intestinal mast cells (MCs)
expressed SNAP23, STX1B (601485), STX2 (132350), STX3, STX4 (STX4A;
186591), and STX6 (603944), but not SNAP25. MCs also expressed VAMP3,
VAMP7, and VAMP8 (603177), but, in contrast with rodent MCs, they
expressed only low levels of VAMP2 (185881). 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.
GENE STRUCTURE
Lazo et al. (2001) found that the SNAP23 gene has 8 exons, with the
initiation codon located in exon 2. They determined that SNAP23B is the
result of alternative splicing where exon 5 is joined to exon 7,
skipping exon 6.
MAPPING
By fluorescence in situ hybridization, Lazo et al. (2001) mapped the
SNAP23 gene to chromosome 15q21-q22. Lazo et al. (2001) suggested that
alterations in the SNAP23 gene may be involved in neurologic and other
diseases with defects in vesicle-membrane fusion processes that map to
15q15-q21.
*FIELD* RF
1. Galli, T.; Zahraoui, A.; Vaidyanathan, V. V.; Raposo, G.; Tian,
J. M.; Karin, M.; Niemann, H.; Louvard, D.: A novel tetanus neurotoxin-insensitive
vesicle-associated membrane protein in SNARE complexes of the apical
plasma membrane of epithelial cells. Molec. Biol. Cell 9: 1437-1448,
1998.
2. Guo, Z.; Turner, C.; Castle, D.: Relocation of the t-SNARE SNAP-23
from lamellipodia-like cell surface projections regulates compound
exocytosis in mast cells. Cell 94: 537-548, 1998.
3. Lazo, P. A.; Nadal, M.; Ferrer, M.; Area, E.; Hernandez-Torres,
J.; Nabokina, S. M.; Mollinedo, F.; Estivill, X.: Genomic organization,
chromosomal localization, alternative splicing, and isoforms of the
human synaptosome-associated protein-23 gene implicated in vesicle-membrane
fusion processes. Hum. Genet. 108: 211-215, 2001.
4. Mollinedo, F.; Lazo, P. A.: Identification of two isoforms of
the vesicle-membrane fusion protein SNAP-23 in human neutrophils and
HL-60 cells. Biochem. Biophys. Res. Commun. 231: 808-812, 1997.
5. Ravichandran, V.; Chawla, A.; Roche, P. A.: Identification of
a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23,
expressed in non-neuronal tissues. J. Biol. Chem. 271: 13300-13303,
1996.
6. 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.
7. Shukla, A.; Corydon, T. J.; Nielsen, S.; Hoffmann, H. J.; Dahl,
R.: Identification of three new splice variants of the SNARE protein
SNAP-23. Biochem. Biophys. Res. Commun. 285: 320-327, 2001.
*FIELD* CN
Paul J. Converse - updated: 10/8/2009
Patricia A. Hartz - updated: 5/1/2002
Victor A. McKusick - updated: 4/6/2001
Stylianos E. Antonarakis - updated: 9/15/1998
*FIELD* CD
Jennifer P. Macke: 4/20/1998
*FIELD* ED
mgross: 10/09/2009
mgross: 10/9/2009
terry: 10/8/2009
carol: 5/1/2002
mcapotos: 4/16/2001
mcapotos: 4/9/2001
terry: 4/6/2001
carol: 12/22/1998
carol: 9/15/1998
dholmes: 5/12/1998