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Synaptosomal-associated protein 23 (SNAP-23) (Syndet) (Vesicle-membrane fusion protein SNAP-23)

 SNP23_MOUSE             Reviewed;         210 AA.
O09044; O35620;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
22-NOV-2017, entry version 144.
RecName: Full=Synaptosomal-associated protein 23;
Short=SNAP-23;
AltName: Full=Syndet;
AltName: Full=Vesicle-membrane fusion protein SNAP-23;
Name=Snap23; Synonyms=Sndt;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adipose tissue;
PubMed=9168999; DOI=10.1006/bbrc.1997.6560;
Araki S., Tamori Y., Kawanishi M., Shinoda H., Masugi J., Mori H.,
Niki T., Okazawa H., Kubota T., Kasuga M.;
"Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c.";
Biochem. Biophys. Res. Commun. 234:257-262(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9067602;
Wang G., Witkin J.W., Hao G., Bankaitis V.A., Scherer P.E.,
Baldini G.;
"Syndet is a novel SNAP-25 related protein expressed in many
tissues.";
J. Cell Sci. 110:505-513(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Olken S.K., Doerre S., Corley R.B.;
"SNARE expression in mouse plasma cells.";
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=10773458; DOI=10.1016/S0378-1119(00)00100-1;
Vaidyanathan V.V., Roche P.A.;
"Structure and chromosomal localization of the mouse SNAP-23 gene.";
Gene 247:181-189(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH STX1A AND STX12.
PubMed=9507000; DOI=10.1074/jbc.273.12.6944;
Tang B.L., Tan A.E., Lim L.K., Lee S.S., Low D.Y., Hong W.;
"Syntaxin 12, a member of the syntaxin family localized to the
endosome.";
J. Biol. Chem. 273:6944-6950(1998).
[8]
IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX4.
PubMed=15363411; DOI=10.1016/j.devcel.2004.08.002;
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-34 AND
SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-160, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
INTERACTION WITH ZDHHC17 AND ZDHHC13, AND MUTAGENESIS OF PRO-119.
PubMed=26198635; DOI=10.1074/jbc.M115.657668;
Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
"Identification of a novel sequence motif recognized by the ankyrin
repeat domain of zDHHC17/13 S-acyltransferases.";
J. Biol. Chem. 290:21939-21950(2015).
-!- FUNCTION: Essential component of the high affinity receptor for
the general membrane fusion machinery and an important regulator
of transport vesicle docking and fusion. {ECO:0000250}.
-!- SUBUNIT: Homotetramer (via coiled-coil domain), also forms
heterotetramers with STX4 and VAMP3 (By similarity). Found in a
complex with VAMP8 and STX1A (By similarity). Found in a complex
with VAMP8 and STX4 in pancreas (PubMed:15363411). Interacts
simultaneously with SNAPIN and SYN4 (By similarity). Interacts
with STX1A (PubMed:9507000). Interacts with STX12
(PubMed:9507000). Interacts tightly to multiple syntaxins and
synaptobrevins/VAMPs (By similarity). Interacts with ZDHHC13 (via
ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK
repeats) (PubMed:26198635). {ECO:0000250|UniProtKB:O00161,
ECO:0000250|UniProtKB:O70377, ECO:0000269|PubMed:15363411,
ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:9507000}.
-!- INTERACTION:
P70452:Stx4; NbExp=2; IntAct=EBI-1812522, EBI-645716;
Q08850:Stx4 (xeno); NbExp=4; IntAct=EBI-1812522, EBI-918243;
P63044:Vamp2; NbExp=3; IntAct=EBI-1812522, EBI-521920;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell
junction, synapse, synaptosome. Note=Mainly localized to the
plasma membrane.
-!- TISSUE SPECIFICITY: Expressed in non-neuronal tissues.
-!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB000822; BAA20345.1; -; mRNA.
EMBL; U73143; AAB53597.1; -; mRNA.
EMBL; AF007169; AAB62932.1; -; mRNA.
EMBL; AF213257; AAF23503.1; -; Genomic_DNA.
EMBL; AF213251; AAF23503.1; JOINED; Genomic_DNA.
EMBL; AF213252; AAF23503.1; JOINED; Genomic_DNA.
EMBL; AF213253; AAF23503.1; JOINED; Genomic_DNA.
EMBL; AF213254; AAF23503.1; JOINED; Genomic_DNA.
EMBL; AF213255; AAF23503.1; JOINED; Genomic_DNA.
EMBL; AF213256; AAF23503.1; JOINED; Genomic_DNA.
EMBL; AK019162; BAB31577.1; -; mRNA.
EMBL; BC070456; AAH70456.1; -; mRNA.
CCDS; CCDS16622.1; -.
PIR; JC5512; JC5512.
RefSeq; NP_001171263.1; NM_001177792.1.
RefSeq; NP_001171264.1; NM_001177793.1.
RefSeq; NP_033248.1; NM_009222.3.
RefSeq; XP_006499120.1; XM_006499057.3.
UniGene; Mm.245715; -.
ProteinModelPortal; O09044; -.
SMR; O09044; -.
BioGrid; 203367; 10.
CORUM; O09044; -.
DIP; DIP-41401N; -.
IntAct; O09044; 10.
MINT; MINT-269238; -.
STRING; 10090.ENSMUSP00000112138; -.
iPTMnet; O09044; -.
PhosphoSitePlus; O09044; -.
SwissPalm; O09044; -.
EPD; O09044; -.
MaxQB; O09044; -.
PaxDb; O09044; -.
PRIDE; O09044; -.
Ensembl; ENSMUST00000028743; ENSMUSP00000028743; ENSMUSG00000027287.
Ensembl; ENSMUST00000110711; ENSMUSP00000106339; ENSMUSG00000027287.
GeneID; 20619; -.
KEGG; mmu:20619; -.
UCSC; uc008lwg.1; mouse.
CTD; 8773; -.
MGI; MGI:109356; Snap23.
eggNOG; KOG3065; Eukaryota.
eggNOG; ENOG410Y3Y0; LUCA.
GeneTree; ENSGT00390000012186; -.
HOGENOM; HOG000231599; -.
HOVERGEN; HBG056971; -.
InParanoid; O09044; -.
KO; K08508; -.
PhylomeDB; O09044; -.
Reactome; R-MMU-1236974; ER-Phagosome pathway.
Reactome; R-MMU-421837; Clathrin derived vesicle budding.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:O09044; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027287; -.
CleanEx; MM_SNAP23; -.
ExpressionAtlas; O09044; baseline and differential.
Genevisible; O09044; MM.
GO; GO:0042582; C:azurophil granule; ISO:MGI.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0031201; C:SNARE complex; IDA:MGI.
GO; GO:0042581; C:specific granule; ISO:MGI.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0019905; F:syntaxin binding; ISO:MGI.
GO; GO:0006887; P:exocytosis; IMP:MGI.
GO; GO:0002553; P:histamine secretion by mast cell; ISO:MGI.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
InterPro; IPR000928; SNAP-25.
InterPro; IPR000727; T_SNARE_dom.
Pfam; PF00835; SNAP-25; 1.
SMART; SM00397; t_SNARE; 2.
PROSITE; PS50192; T_SNARE; 2.
1: Evidence at protein level;
Acetylation; Cell junction; Cell membrane; Coiled coil;
Complete proteome; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Protein transport; Reference proteome; Repeat; Synapse; Synaptosome;
Transport.
CHAIN 1 210 Synaptosomal-associated protein 23.
/FTId=PRO_0000213599.
DOMAIN 14 76 t-SNARE coiled-coil homology 1.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
DOMAIN 145 207 t-SNARE coiled-coil homology 2.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
COILED 23 76 {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O00161}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:O00161}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
LIPID 79 79 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 80 80 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 83 83 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 85 85 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 87 87 S-palmitoyl cysteine. {ECO:0000250}.
MUTAGEN 119 119 P->A: Inhibits interaction with ZDHHC13
and ZDHHC17.
CONFLICT 6 6 P -> S (in Ref. 3; AAB62932).
{ECO:0000305}.
CONFLICT 204 204 A -> P (in Ref. 3; AAB62932).
{ECO:0000305}.
SEQUENCE 210 AA; 23261 MW; 6919E127E16BA2C9 CRC64;
MDNLSPEEVQ LRAHQVTDES LESTRRILGL AIESQDAGIK TITMLDEQGE QLNRIEEGMD
QINKDMREAE KTLTELNKCC GLCICPCNRT KNFESGKNYK ATWGDGGDNS PSNVVSKQPS
RITNGQPQQT TGAASGGYIK RITNDAREDE MEENLTQVGS ILGNLKNMAL DMGNEIDAQN
QQIQKITEKA DTNKNRIDIA NTRAKKLIDS


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