SNP23_MOUSE
ID SNP23_MOUSE Reviewed; 210 AA.
AC O09044; O35620;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Synaptosomal-associated protein 23;
DE Short=SNAP-23;
DE AltName: Full=Syndet;
DE AltName: Full=Vesicle-membrane fusion protein SNAP-23;
GN Name=Snap23; Synonyms=Sndt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adipose tissue;
RX PubMed=9168999; DOI=10.1006/bbrc.1997.6560;
RA Araki S., Tamori Y., Kawanishi M., Shinoda H., Masugi J., Mori H., Niki T.,
RA Okazawa H., Kubota T., Kasuga M.;
RT "Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c.";
RL Biochem. Biophys. Res. Commun. 234:257-262(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9067602; DOI=10.1242/jcs.110.4.505;
RA Wang G., Witkin J.W., Hao G., Bankaitis V.A., Scherer P.E., Baldini G.;
RT "Syndet is a novel SNAP-25 related protein expressed in many tissues.";
RL J. Cell Sci. 110:505-513(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Olken S.K., Doerre S., Corley R.B.;
RT "SNARE expression in mouse plasma cells.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10773458; DOI=10.1016/s0378-1119(00)00100-1;
RA Vaidyanathan V.V., Roche P.A.;
RT "Structure and chromosomal localization of the mouse SNAP-23 gene.";
RL Gene 247:181-189(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [7]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPES
RP A AND E.
RX PubMed=9886085; DOI=10.1046/j.1471-4159.1999.0720327.x;
RA Vaidyanathan V.V., Yoshino K., Jahnz M., Doerries C., Bade S.,
RA Nauenburg S., Niemann H., Binz T.;
RT "Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E:
RT domains and amino acid residues controlling the formation of enzyme-
RT substrate complexes and cleavage.";
RL J. Neurochem. 72:327-337(1999).
RN [8]
RP INTERACTION WITH STX1A AND STX12.
RX PubMed=9507000; DOI=10.1074/jbc.273.12.6944;
RA Tang B.L., Tan A.E., Lim L.K., Lee S.S., Low D.Y., Hong W.;
RT "Syntaxin 12, a member of the syntaxin family localized to the endosome.";
RL J. Biol. Chem. 273:6944-6950(1998).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX4.
RX PubMed=15363411; DOI=10.1016/j.devcel.2004.08.002;
RA Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F., Hong W.;
RT "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar
RT cells.";
RL Dev. Cell 7:359-371(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-34 AND
RP SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP INTERACTION WITH ZDHHC17 AND ZDHHC13, AND MUTAGENESIS OF PRO-119.
RX PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT "Identification of a novel sequence motif recognized by the ankyrin repeat
RT domain of zDHHC17/13 S-acyltransferases.";
RL J. Biol. Chem. 290:21939-21950(2015).
CC -!- FUNCTION: Essential component of the high affinity receptor for the
CC general membrane fusion machinery and an important regulator of
CC transport vesicle docking and fusion. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer (via coiled-coil domain), also forms
CC heterotetramers with STX4 and VAMP3 (By similarity). Found in a complex
CC with VAMP8 and STX1A (By similarity). Found in a complex with VAMP8 and
CC STX4 in pancreas (PubMed:15363411). Interacts simultaneously with
CC SNAPIN and SYN4 (By similarity). Interacts with STX1A (PubMed:9507000).
CC Interacts with STX12 (PubMed:9507000). Interacts tightly to multiple
CC syntaxins and synaptobrevins/VAMPs (By similarity). Interacts with
CC ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with ZDHHC17
CC (via ANK repeats) (PubMed:26198635). {ECO:0000250|UniProtKB:O00161,
CC ECO:0000250|UniProtKB:O70377, ECO:0000269|PubMed:15363411,
CC ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:9507000}.
CC -!- INTERACTION:
CC O09044; Q08850: Stx4; Xeno; NbExp=4; IntAct=EBI-1812522, EBI-918243;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell
CC membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Synapse,
CC synaptosome. Note=Mainly localized to the plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed in non-neuronal tissues.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type A (BoNT/A, botA) which hydrolyzes the 202-Thr-|-Arg-203
CC bond; the in vitro reaction is not highly efficient (PubMed:9886085).
CC {ECO:0000269|PubMed:9886085}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type E (BoNT/E) which hydrolyzes the 185-Arg-|-Ile-186 bond;
CC the in vitro reaction is more efficient than that of BoNT/A
CC (PubMed:9886085). {ECO:0000269|PubMed:9886085}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; AB000822; BAA20345.1; -; mRNA.
DR EMBL; U73143; AAB53597.1; -; mRNA.
DR EMBL; AF007169; AAB62932.1; -; mRNA.
DR EMBL; AF213257; AAF23503.1; -; Genomic_DNA.
DR EMBL; AF213251; AAF23503.1; JOINED; Genomic_DNA.
DR EMBL; AF213252; AAF23503.1; JOINED; Genomic_DNA.
DR EMBL; AF213253; AAF23503.1; JOINED; Genomic_DNA.
DR EMBL; AF213254; AAF23503.1; JOINED; Genomic_DNA.
DR EMBL; AF213255; AAF23503.1; JOINED; Genomic_DNA.
DR EMBL; AF213256; AAF23503.1; JOINED; Genomic_DNA.
DR EMBL; AK019162; BAB31577.1; -; mRNA.
DR EMBL; BC070456; AAH70456.1; -; mRNA.
DR CCDS; CCDS16622.1; -.
DR PIR; JC5512; JC5512.
DR RefSeq; NP_001171263.1; NM_001177792.1.
DR RefSeq; NP_001171264.1; NM_001177793.1.
DR RefSeq; NP_033248.1; NM_009222.3.
DR RefSeq; XP_006499120.1; XM_006499057.3.
DR AlphaFoldDB; O09044; -.
DR SMR; O09044; -.
DR BioGRID; 203367; 15.
DR CORUM; O09044; -.
DR DIP; DIP-41401N; -.
DR IntAct; O09044; 10.
DR MINT; O09044; -.
DR STRING; 10090.ENSMUSP00000112138; -.
DR iPTMnet; O09044; -.
DR PhosphoSitePlus; O09044; -.
DR SwissPalm; O09044; -.
DR EPD; O09044; -.
DR jPOST; O09044; -.
DR MaxQB; O09044; -.
DR PaxDb; O09044; -.
DR PRIDE; O09044; -.
DR ProteomicsDB; 261530; -.
DR Antibodypedia; 712; 431 antibodies from 36 providers.
DR DNASU; 20619; -.
DR Ensembl; ENSMUST00000028743; ENSMUSP00000028743; ENSMUSG00000027287.
DR Ensembl; ENSMUST00000110711; ENSMUSP00000106339; ENSMUSG00000027287.
DR GeneID; 20619; -.
DR KEGG; mmu:20619; -.
DR UCSC; uc008lwg.1; mouse.
DR CTD; 8773; -.
DR MGI; MGI:109356; Snap23.
DR VEuPathDB; HostDB:ENSMUSG00000027287; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_096939_0_0_1; -.
DR InParanoid; O09044; -.
DR OMA; NYAVHKA; -.
DR OrthoDB; 1358184at2759; -.
DR PhylomeDB; O09044; -.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 20619; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Snap23; mouse.
DR PRO; PR:O09044; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O09044; protein.
DR Bgee; ENSMUSG00000027287; Expressed in ascending aorta and 258 other tissues.
DR ExpressionAtlas; O09044; baseline and differential.
DR Genevisible; O09044; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0042582; C:azurophil granule; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR GO; GO:0042581; C:specific granule; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; ISO:MGI.
DR GO; GO:0006887; P:exocytosis; IMP:MGI.
DR GO; GO:0002553; P:histamine secretion by mast cell; ISO:MGI.
DR GO; GO:0061025; P:membrane fusion; ISO:MGI.
DR GO; GO:0015031; P:protein transport; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:MGI.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:MGI.
DR InterPro; IPR000928; SNAP-25_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF00835; SNAP-25; 1.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coiled coil; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Synapse;
KW Synaptosome; Transport.
FT CHAIN 1..210
FT /note="Synaptosomal-associated protein 23"
FT /id="PRO_0000213599"
FT DOMAIN 14..76
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 145..207
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 104..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..76
FT /evidence="ECO:0000250"
FT COMPBIAS 105..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 185..186
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type E (BoNT/E)"
FT /evidence="ECO:0000269|PubMed:9886085"
FT SITE 202..203
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type A (BoNT/A, botA)"
FT /evidence="ECO:0000269|PubMed:9886085"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O00161"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00161"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 79
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 80
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 83
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 85
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 87
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 119
FT /note="P->A: Inhibits interaction with ZDHHC13 and
FT ZDHHC17."
FT CONFLICT 6
FT /note="P -> S (in Ref. 3; AAB62932)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="A -> P (in Ref. 3; AAB62932)"
FT /evidence="ECO:0000305"
SQ 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
