SNP25_MOUSE
ID SNP25_MOUSE Reviewed; 206 AA.
AC P60879; A2AIC2; A2AIC3; P13795; P36974; P70557; P70558; Q8IXK3; Q96FM2;
AC Q9BR45;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Synaptosomal-associated protein 25;
DE Short=SNAP-25;
DE AltName: Full=Super protein;
DE Short=SUP;
DE AltName: Full=Synaptosomal-associated 25 kDa protein;
GN Name=Snap25; Synonyms=Snap;
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] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=2592413; DOI=10.1083/jcb.109.6.3039;
RA Oyler G.A., Higgins G.A., Hart R.A., Battenberg E., Billingsley M.,
RA Bloom F.E., Wilson M.C.;
RT "The identification of a novel synaptosomal-associated protein, SNAP-25,
RT differentially expressed by neuronal subpopulations.";
RL J. Cell Biol. 109:3039-3052(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 PROTEIN SEQUENCE OF 18-31; 60-72; 125-135 AND 143-176, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [8]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM
RP NEUROTOXIN TYPES A AND E.
RX PubMed=8243676; DOI=10.1016/0014-5793(93)80448-4;
RA Schiavo G., Santtuci A., Dasgupta B.R., Mehta P.P., Jontes J.,
RA Benfenati F., Wilson M.C., Montecucco C.;
RT "Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-
RT terminal peptide bonds.";
RL FEBS Lett. 335:99-103(1993).
RN [9]
RP PALMITOYLATION AT CYS-85; CYS-88; CYS-90 AND CYS-92, MUTAGENESIS OF CYS-85;
RP CYS-88; CYS-90 AND CYS-92, AND SUBCELLULAR LOCATION.
RX PubMed=9349529; DOI=10.1046/j.1471-4159.1997.69051864.x;
RA Lane S.R., Liu Y.;
RT "Characterization of the palmitoylation domain of SNAP-25.";
RL J. Neurochem. 69:1864-1869(1997).
RN [10]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM
RP NEUROTOXIN TYPES A AND E.
RX PubMed=8103915; DOI=10.1038/365160a0;
RA Blasi J., Chapman E.R., Link E., Binz T., Yamasaki S., De Camilli P.,
RA Suedhof T.C., Niemann H., Jahn R.;
RT "Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25.";
RL Nature 365:160-163(1993).
RN [11]
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY
RP C.BOTULINUM NEUROTOXIN TYPES A AND E.
RX PubMed=10413679; DOI=10.1242/jcs.112.16.2715;
RA Lalli G., Herreros J., Osborne S.L., Montecucco C., Rossetto O.,
RA Schiavo G.;
RT "Functional characterisation of tetanus and botulinum neurotoxins binding
RT domains.";
RL J. Cell Sci. 112:2715-2724(1999).
RN [12]
RP INTERACTION WITH SNAPIN.
RX PubMed=10195194; DOI=10.1038/5673;
RA Ilardi J.M., Mochida S., Sheng Z.-H.;
RT "Snapin: a SNARE-associated protein implicated in synaptic transmission.";
RL Nat. Neurosci. 2:119-124(1999).
RN [13]
RP PHOSPHORYLATION AT THR-138 AND SER-187.
RX PubMed=12459461; DOI=10.1016/s0014-5793(02)03629-3;
RA Hepp R., Cabaniols J.-P., Roche P.A.;
RT "Differential phosphorylation of SNAP-25 in vivo by protein kinase C and
RT protein kinase A.";
RL FEBS Lett. 532:52-56(2002).
RN [14]
RP INTERACTION WITH SYT1; SV2B AND SYNTAXIN-1.
RX PubMed=15466855; DOI=10.1074/jbc.m407502200;
RA Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.;
RT "SV2B regulates synaptotagmin 1 by direct interaction.";
RL J. Biol. Chem. 279:52124-52131(2004).
RN [15]
RP INTERACTION WITH OTOF.
RC STRAIN=BALB/cJ; TISSUE=Cochlea;
RX PubMed=17055430; DOI=10.1016/j.cell.2006.08.040;
RA Roux I., Safieddine S., Nouvian R., Grati M., Simmler M.-C., Bahloul A.,
RA Perfettini I., Le Gall M., Rostaing P., Hamard G., Triller A., Avan P.,
RA Moser T., Petit C.;
RT "Otoferlin, defective in a human deafness form, is essential for exocytosis
RT at the auditory ribbon synapse.";
RL Cell 127:277-289(2006).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CENPF.
RX PubMed=16672379; DOI=10.1091/mbc.e05-12-1127;
RA Pooley R.D., Reddy S., Soukoulis V., Roland J.T., Goldenring J.R.,
RA Bader D.M.;
RT "CytLEK1 is a regulator of plasma membrane recycling through its
RT interaction with SNAP-25.";
RL Mol. Biol. Cell 17:3176-3186(2006).
RN [17]
RP INTERACTION WITH VAMP2.
RX PubMed=19196426; DOI=10.1111/j.1471-4159.2008.05849.x;
RA Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I.,
RA Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., Nagata K.;
RT "Sept8 controls the binding of vesicle-associated membrane protein 2 to
RT synaptophysin.";
RL J. Neurochem. 108:867-880(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-154, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Brown adipose tissue;
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 [19]
RP INTERACTION WITH EQTN.
RX PubMed=19285662; DOI=10.1016/j.fertnstert.2009.01.067;
RA Hu X.Q., Ji S.Y., Li Y.C., Fan C.H., Cai H., Yang J.L., Zhang C.P.,
RA Chen M., Pan Z.F., Hu Z.Y., Gao F., Liu Y.X.;
RT "Acrosome formation-associated factor is involved in fertilization.";
RL Fertil. Steril. 93:1482-1492(2010).
RN [20]
RP ASSOCIATION WITH THE BLOC-1 COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH BLOC1S6.
RX PubMed=19546860; DOI=10.1038/mp.2009.58;
RA Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
RA Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
RA Dell'Angelica E.C.;
RT "The dysbindin-containing complex (BLOC-1) in brain: developmental
RT regulation, interaction with SNARE proteins and role in neurite
RT outgrowth.";
RL Mol. Psychiatry 15:204-215(2010).
RN [21]
RP INTERACTION WITH ALPHA-SYNUCLEIN/SNCA.
RX PubMed=20798282; DOI=10.1126/science.1195227;
RA Burre J., Sharma M., Tsetsenis T., Buchman V., Etherton M.R., Suedhof T.C.;
RT "Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro.";
RL Science 329:1663-1667(2010).
RN [22]
RP INTERACTION WITH SYT9 AND HSC70.
RX PubMed=20847230; DOI=10.1096/fj.09-152033;
RA Boal F., Laguerre M., Milochau A., Lang J., Scotti P.A.;
RT "A charged prominence in the linker domain of the cysteine-string protein
RT Cspalpha mediates its regulated interaction with the calcium sensor
RT synaptotagmin 9 during exocytosis.";
RL FASEB J. 25:132-143(2011).
RN [23]
RP INTERACTION WITH PRRT2.
RX PubMed=22832103; DOI=10.1016/j.celrep.2011.11.001;
RA Lee H.Y., Huang Y., Bruneau N., Roll P., Roberson E.D., Hermann M.,
RA Quinn E., Maas J., Edwards R., Ashizawa T., Baykan B., Bhatia K.,
RA Bressman S., Bruno M.K., Brunt E.R., Caraballo R., Echenne B., Fejerman N.,
RA Frucht S., Gurnett C.A., Hirsch E., Houlden H., Jankovic J., Lee W.L.,
RA Lynch D.R., Mohammed S., Mueller U., Nespeca M.P., Renner D., Rochette J.,
RA Rudolf G., Saiki S., Soong B.W., Swoboda K.J., Tucker S., Wood N.,
RA Hanna M., Bowcock A.M., Szepetowski P., Fu Y.H., Ptacek L.J.;
RT "Mutations in the gene PRRT2 cause paroxysmal kinesigenic dyskinesia with
RT infantile convulsions.";
RL Cell Rep. 1:2-12(2012).
RN [24]
RP INTERACTION WITH PLCL1.
RX PubMed=23341457; DOI=10.1074/jbc.m112.419317;
RA Zhang Z., Takeuchi H., Gao J., Wang D., James D.J., Martin T.F., Hirata M.;
RT "PRIP (phospholipase C-related but catalytically inactive protein) inhibits
RT exocytosis by direct interactions with syntaxin 1 and SNAP-25 through its
RT C2 domain.";
RL J. Biol. Chem. 288:7769-7780(2013).
RN [25]
RP INTERACTION WITH ZDHHC17 AND ZDHHC13.
RX PubMed=25253725; DOI=10.1091/mbc.e14-06-1169;
RA Lemonidis K., Gorleku O.A., Sanchez-Perez M.C., Grefen C.,
RA Chamberlain L.H.;
RT "The Golgi S-acylation machinery comprises zDHHC enzymes with major
RT differences in substrate affinity and S-acylation activity.";
RL Mol. Biol. Cell 25:3870-3883(2014).
RN [26]
RP INTERACTION WITH ZDHHC17 AND ZDHHC13.
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).
RN [27]
RP INTERACTION WITH PRPH2; ROM1 AND STX3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=26406599; DOI=10.1371/journal.pone.0138508;
RA Zulliger R., Conley S.M., Mwoyosvi M.L., Stuck M.W., Azadi S., Naash M.I.;
RT "SNAREs Interact with Retinal Degeneration Slow and Rod Outer Segment
RT Membrane Protein-1 during Conventional and Unconventional Outer Segment
RT Targeting.";
RL PLoS ONE 10:E0138508-E0138508(2015).
RN [28]
RP INTERACTION WITH PRRT2.
RX PubMed=27052163; DOI=10.1016/j.celrep.2016.03.005;
RA Valente P., Castroflorio E., Rossi P., Fadda M., Sterlini B.,
RA Cervigni R.I., Prestigio C., Giovedi S., Onofri F., Mura E.,
RA Guarnieri F.C., Marte A., Orlando M., Zara F., Fassio A., Valtorta F.,
RA Baldelli P., Corradi A., Benfenati F.;
RT "PRRT2 Is a Key Component of the Ca(2+)-Dependent Neurotransmitter Release
RT Machinery.";
RL Cell Rep. 15:117-131(2016).
RN [29]
RP INTERACTION WITH PRRT2.
RX PubMed=29056747; DOI=10.1038/cr.2017.128;
RA Tan G.H., Liu Y.Y., Wang L., Li K., Zhang Z.Q., Li H.F., Yang Z.F., Li Y.,
RA Li D., Wu M.Y., Yu C.L., Long J.J., Chen R.C., Li L.X., Yin L.P., Liu J.W.,
RA Cheng X.W., Shen Q., Shu Y.S., Sakimura K., Liao L.J., Wu Z.Y., Xiong Z.Q.;
RT "PRRT2 deficiency induces paroxysmal kinesigenic dyskinesia by regulating
RT synaptic transmission in cerebellum.";
RL Cell Res. 28:90-110(2018).
RN [30]
RP 3D-STRUCTURE MODELING OF 18-206 IN COMPLEX WITH VAMP2 AND STX1A.
RX PubMed=9731768; DOI=10.1038/1799;
RA Poirier M.A., Xiao W., Macosko J.C., Chan C., Shin Y.K., Bennett M.K.;
RT "The synaptic SNARE complex is a parallel four-stranded helical bundle.";
RL Nat. Struct. Biol. 5:765-769(1998).
CC -!- FUNCTION: t-SNARE involved in the molecular regulation of
CC neurotransmitter release (PubMed:8243676, PubMed:8103915). May play an
CC important role in the synaptic function of specific neuronal systems.
CC Associates with proteins involved in vesicle docking and membrane
CC fusion. Regulates plasma membrane recycling through its interaction
CC with CENPF (PubMed:16672379). Modulates the gating characteristics of
CC the delayed rectifier voltage-dependent potassium channel KCNB1 in
CC pancreatic beta cells (By similarity). {ECO:0000250|UniProtKB:P60881,
CC ECO:0000269|PubMed:16672379, ECO:0000305|PubMed:8103915,
CC ECO:0000305|PubMed:8243676}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A, this complex binds CPLX1 (PubMed:19196426). Found in a complex
CC containing SYT1, SV2B and syntaxin-1 (PubMed:15466855). Found in a
CC ternary complex with STX1A and VAMP8 (PubMed:9731768). Interacts with
CC HSC70 and with SYT9, forming a complex with DNAJC5 (PubMed:20847230).
CC The interaction with SYT9 is inhibited in presence of calcium
CC (PubMed:20847230). Isoform 1 and isoform 2 interact with BLOC1S6
CC (PubMed:19546860). Interacts with CENPF (PubMed:16672379). Interacts
CC with EQTN (PubMed:19285662). Interacts with HGS (By similarity).
CC Interacts with KCNB1 (via N-terminus); reduces the voltage-dependent
CC potassium channel KCNB1 activity in pancreatic beta cells (By
CC similarity). Interacts with OTOF (PubMed:17055430). Interacts with
CC RIMS1 (By similarity). Interacts with SNAPIN (PubMed:10195194).
CC Interacts with STXBP6 (By similarity). Interacts with TRIM9 (By
CC similarity). Interacts with ZDHHC13 (via ANK repeats)
CC (PubMed:25253725). Interacts with ZDHHC17 (via ANK repeats)
CC (PubMed:25253725). Associates with the BLOC-1 complex
CC (PubMed:19546860). Interacts with PLCL1 (via C2 domain)
CC (PubMed:23341457). Interacts with PRRT2; this interaction may impair
CC the formation of the SNARE complex (PubMed:22832103, PubMed:27052163,
CC PubMed:29056747). Interacts with alpha-synuclein/SNCA
CC (PubMed:20798282). Interacts with PRPH2 (PubMed:26406599). Interacts
CC with ROM1 (PubMed:26406599). Interacts with STX3 isoform 3B
CC (PubMed:26406599). {ECO:0000250|UniProtKB:P60881,
CC ECO:0000269|PubMed:10195194, ECO:0000269|PubMed:15466855,
CC ECO:0000269|PubMed:16672379, ECO:0000269|PubMed:17055430,
CC ECO:0000269|PubMed:19196426, ECO:0000269|PubMed:19285662,
CC ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:20798282,
CC ECO:0000269|PubMed:20847230, ECO:0000269|PubMed:22832103,
CC ECO:0000269|PubMed:23341457, ECO:0000269|PubMed:25253725,
CC ECO:0000269|PubMed:26406599, ECO:0000269|PubMed:27052163,
CC ECO:0000269|PubMed:29056747, ECO:0000269|PubMed:9731768}.
CC -!- INTERACTION:
CC P60879; Q155P7: Cenpf; NbExp=13; IntAct=EBI-445270, EBI-2211248;
CC P60879; O35526: Stx1a; NbExp=4; IntAct=EBI-445270, EBI-400878;
CC P60879; P63044: Vamp2; NbExp=18; IntAct=EBI-445270, EBI-521920;
CC P60879; P32851: Stx1a; Xeno; NbExp=7; IntAct=EBI-445270, EBI-539720;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16672379}. Cell membrane
CC {ECO:0000269|PubMed:10413679, ECO:0000269|PubMed:9349529}; Lipid-anchor
CC {ECO:0000269|PubMed:9349529}. Synapse, synaptosome
CC {ECO:0000269|PubMed:2592413}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:26406599}. Note=Membrane association requires
CC palmitoylation (PubMed:9349529). Expressed throughout cytoplasm,
CC concentrating at the perinuclear region (PubMed:16672379). Colocalizes
CC with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1
CC at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60881,
CC ECO:0000269|PubMed:16672379, ECO:0000269|PubMed:9349529}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoforms differ by the usage of two alternative homologous
CC exons (5a and 5b) which code for positions 56 to 94 and differ only
CC in 9 positions out of 39.;
CC Name=1; Synonyms=SNAP-25b;
CC IsoId=P60879-1, P13795-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=SNAP-25a;
CC IsoId=P60879-2, P13795-2;
CC Sequence=VSP_010019;
CC -!- TISSUE SPECIFICITY: Expressed in the outer nuclear layer of the retina
CC (at protein level). {ECO:0000269|PubMed:26406599}.
CC -!- PTM: Palmitoylated. Cys-85 appears to be the main site, and
CC palmitoylation is required for membrane association.
CC {ECO:0000269|PubMed:9349529}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type A (BoNT/A, botA) which hydrolyzes the 197-Gln-|-Arg-198
CC bond and inhibits neurotransmitter release (PubMed:8243676,
CC PubMed:8103915). {ECO:0000269|PubMed:8243676,
CC ECO:0000305|PubMed:10413679, ECO:0000305|PubMed:8103915}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type E (BoNT/E) which hydrolyzes the 180-Arg-|-Ile-181 bond
CC and inhibits neurotransmitter release (PubMed:8243676, PubMed:8103915).
CC {ECO:0000269|PubMed:8243676, ECO:0000305|PubMed:10413679,
CC ECO:0000305|PubMed:8103915}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; M22012; AAA61741.1; -; mRNA.
DR EMBL; AF483516; AAL90790.1; -; mRNA.
DR EMBL; AF483517; AAL90791.1; -; mRNA.
DR EMBL; AK078038; BAC37105.1; -; mRNA.
DR EMBL; AL732447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28390.1; -; Genomic_DNA.
DR EMBL; BC018249; AAH18249.1; -; mRNA.
DR CCDS; CCDS16793.1; -.
DR CCDS; CCDS71153.1; -. [P60879-2]
DR PIR; A33623; A33623.
DR RefSeq; NP_001277985.1; NM_001291056.1. [P60879-2]
DR RefSeq; NP_035558.1; NM_011428.3. [P60879-1]
DR RefSeq; XP_017172247.1; XM_017316758.1.
DR RefSeq; XP_017172249.1; XM_017316760.1. [P60879-2]
DR AlphaFoldDB; P60879; -.
DR BMRB; P60879; -.
DR SMR; P60879; -.
DR BioGRID; 203362; 76.
DR CORUM; P60879; -.
DR DIP; DIP-29066N; -.
DR IntAct; P60879; 42.
DR MINT; P60879; -.
DR STRING; 10090.ENSMUSP00000028727; -.
DR TCDB; 1.F.1.1.4; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; P60879; -.
DR PhosphoSitePlus; P60879; -.
DR SwissPalm; P60879; -.
DR jPOST; P60879; -.
DR MaxQB; P60879; -.
DR PaxDb; P60879; -.
DR PeptideAtlas; P60879; -.
DR PRIDE; P60879; -.
DR ProteomicsDB; 257537; -.
DR ProteomicsDB; 257538; -. [P60879-2]
DR Antibodypedia; 713; 1205 antibodies from 48 providers.
DR DNASU; 20614; -.
DR Ensembl; ENSMUST00000028727; ENSMUSP00000028727; ENSMUSG00000027273. [P60879-1]
DR Ensembl; ENSMUST00000110098; ENSMUSP00000105725; ENSMUSG00000027273. [P60879-2]
DR GeneID; 20614; -.
DR KEGG; mmu:20614; -.
DR UCSC; uc008mop.1; mouse.
DR UCSC; uc056zpt.1; mouse. [P60879-2]
DR CTD; 6616; -.
DR MGI; MGI:98331; Snap25.
DR VEuPathDB; HostDB:ENSMUSG00000027273; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_096939_0_0_1; -.
DR InParanoid; P60879; -.
DR OMA; WKASEDG; -.
DR OrthoDB; 1197028at2759; -.
DR PhylomeDB; P60879; -.
DR TreeFam; TF315125; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
DR BioGRID-ORCS; 20614; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Snap25; mouse.
DR PRO; PR:P60879; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P60879; protein.
DR Bgee; ENSMUSG00000027273; Expressed in retrosplenial region and 159 other tissues.
DR Genevisible; P60879; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:ParkinsonsUK-UCL.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0031083; C:BLOC-1 complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:SynGO-UCL.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR GO; GO:0097470; C:ribbon synapse; IDA:MGI.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; ISO:MGI.
DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IDA:MGI.
DR GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0017022; F:myosin binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IDA:MGI.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IMP:SynGO.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0099590; P:neurotransmitter receptor internalization; IMP:SynGO.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR GO; GO:0046887; P:positive regulation of hormone secretion; ISO:MGI.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IMP:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IGI:ParkinsonsUK-UCL.
DR GO; GO:0030431; P:sleep; ISO:MGI.
DR GO; GO:0035493; P:SNARE complex assembly; ISO:MGI.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:SynGO.
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 InterPro; IPR039077; SNAP-25.
DR InterPro; IPR000928; SNAP-25_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19305:SF5; PTHR19305:SF5; 1.
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 Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..206
FT /note="Synaptosomal-associated protein 25"
FT /id="PRO_0000213589"
FT DOMAIN 19..81
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 140..202
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..75
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000269|PubMed:16672379"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..120
FT /note="Interaction with ZDHHC17"
FT /evidence="ECO:0000250|UniProtKB:P60880"
FT SITE 180..181
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type E (BoNT/E)"
FT /evidence="ECO:0000269|PubMed:8243676,
FT ECO:0000305|PubMed:8103915"
FT SITE 197..198
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type A (BoNT/A, botA)"
FT /evidence="ECO:0000269|PubMed:8243676,
FT ECO:0000305|PubMed:8103915"
FT MOD_RES 138
FT /note="Phosphothreonine; by PKC and PKA"
FT /evidence="ECO:0000269|PubMed:12459461,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 187
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:12459461"
FT LIPID 85
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:9349529"
FT LIPID 88
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:9349529"
FT LIPID 90
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:9349529"
FT LIPID 92
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:9349529"
FT VAR_SEQ 58..89
FT /note="ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV -> DRVEEGMNHINQDMKE
FT AEKNLKDLGKCCGLFI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11471062,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2592413"
FT /id="VSP_010019"
FT MUTAGEN 85
FT /note="C->S: 91% reduction in palmitoylation level. 14%
FT membrane association. No palmitoylation and less than 8%
FT membrane association; when associated with S-88 or A-88."
FT /evidence="ECO:0000269|PubMed:9349529"
FT MUTAGEN 88
FT /note="C->S: 79% reduction in palmitoylation level. 18%
FT membrane association. No palmitoylation and less than 8%
FT membrane association; when associated with S-85 or A-85."
FT /evidence="ECO:0000269|PubMed:9349529"
FT MUTAGEN 90
FT /note="C->S: 58% reduction in palmitoylation level. 28%
FT membrane association. Very little palmitoylation and less
FT than 8% membrane association; when associated with S-92 or
FT A-92."
FT /evidence="ECO:0000269|PubMed:9349529"
FT MUTAGEN 92
FT /note="C->S: 65% reduction in palmitoylation level. 29%
FT membrane association. No palmitoylation and less than 8%
FT membrane association; when associated with S-90 or A-90."
FT /evidence="ECO:0000269|PubMed:9349529"
SQ SEQUENCE 206 AA; 23315 MW; FBED2B082A4CB6A6 CRC64;
MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI
EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV
VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR
IMEKADSNKT RIDEANQRAT KMLGSG
