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 27-MAR-2024, entry version 184. 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, RC Pancreas, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000112138; -. DR ProteomicsDB; 261530; -. DR Pumba; O09044; -. DR Antibodypedia; 712; 478 antibodies from 36 providers. DR DNASU; 20619; -. DR Ensembl; ENSMUST00000028743.10; ENSMUSP00000028743.4; ENSMUSG00000027287.15. DR Ensembl; ENSMUST00000110711.9; ENSMUSP00000106339.3; ENSMUSG00000027287.15. DR GeneID; 20619; -. DR KEGG; mmu:20619; -. DR UCSC; uc008lwg.1; mouse. DR AGR; MGI:109356; -. 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; DLTKCCG; -. DR OrthoDB; 388796at2759; -. 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-9013149; RAC1 GTPase cycle. DR Reactome; R-MMU-9013406; RHOQ 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 79 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 261 other cell types or tissues. DR ExpressionAtlas; O09044; baseline and differential. 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:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IBA:GO_Central. DR GO; GO:0005484; F:SNAP receptor activity; ISO:MGI. DR GO; GO:0019905; F:syntaxin binding; ISO:MGI. DR GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central. 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: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:0016192; P:vesicle-mediated transport; ISO:MGI. DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:MGI. DR CDD; cd15884; SNARE_SNAP23C; 1. DR CDD; cd15895; SNARE_SNAP23N; 1. DR Gene3D; 1.20.5.110; -; 2. DR InterPro; IPR000928; SNAP-25_dom. DR InterPro; IPR000727; T_SNARE_dom. DR PANTHER; PTHR19305; SYNAPTOSOMAL ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR19305:SF4; SYNAPTOSOMAL-ASSOCIATED PROTEIN 23; 1. DR Pfam; PF00835; SNAP-25; 1. DR SMART; SM00397; t_SNARE; 2. DR SUPFAM; SSF58038; SNARE fusion complex; 2. DR PROSITE; PS50192; T_SNARE; 2. DR Genevisible; O09044; MM. 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 //