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Synaptosomal-associated protein 25 (SNAP-25) (Super protein) (SUP) (Synaptosomal-associated 25 kDa protein)

 SNP25_MOUSE             Reviewed;         206 AA.
P60879; A2AIC2; A2AIC3; P13795; P36974; P70557; P70558; Q8IXK3;
Q96FM2; Q9BR45;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 1.
12-SEP-2018, entry version 154.
RecName: Full=Synaptosomal-associated protein 25;
Short=SNAP-25;
AltName: Full=Super protein;
Short=SUP;
AltName: Full=Synaptosomal-associated 25 kDa protein;
Name=Snap25; Synonyms=Snap;
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] (ISOFORM 2), AND SUBCELLULAR LOCATION.
STRAIN=BALB/cJ;
PubMed=2592413; DOI=10.1083/jcb.109.6.3039;
Oyler G.A., Higgins G.A., Hart R.A., Battenberg E., Billingsley M.,
Bloom F.E., Wilson M.C.;
"The identification of a novel synaptosomal-associated protein, SNAP-
25, differentially expressed by neuronal subpopulations.";
J. Cell Biol. 109:3039-3052(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=ILS, and ISS;
PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
"High-throughput sequence identification of gene coding variants
within alcohol-related QTLs.";
Mamm. Genome 12:657-663(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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]
PROTEIN SEQUENCE OF 18-31; 60-72; 125-135 AND 143-176, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[8]
FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY
C.BOTULINUM NEUROTOXIN TYPES A AND E.
PubMed=8243676; DOI=10.1016/0014-5793(93)80448-4;
Schiavo G., Santtuci A., Dasgupta B.R., Mehta P.P., Jontes J.,
Benfenati F., Wilson M.C., Montecucco C.;
"Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct
COOH-terminal peptide bonds.";
FEBS Lett. 335:99-103(1993).
[9]
PALMITOYLATION AT CYS-85; CYS-88; CYS-90 AND CYS-92, MUTAGENESIS OF
CYS-85; CYS-88; CYS-90 AND CYS-92, AND SUBCELLULAR LOCATION.
PubMed=9349529;
Lane S.R., Liu Y.;
"Characterization of the palmitoylation domain of SNAP-25.";
J. Neurochem. 69:1864-1869(1997).
[10]
FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY
C.BOTULINUM NEUROTOXIN TYPES A AND E.
PubMed=8103915; DOI=10.1038/365160a0;
Blasi J., Chapman E.R., Link E., Binz T., Yamasaki S., De Camilli P.,
Suedhof T.C., Niemann H., Jahn R.;
"Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-
25.";
Nature 365:160-163(1993).
[11]
SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION)
BY C.BOTULINUM NEUROTOXIN TYPES A AND E.
PubMed=10413679;
Lalli G., Herreros J., Osborne S.L., Montecucco C., Rossetto O.,
Schiavo G.;
"Functional characterisation of tetanus and botulinum neurotoxins
binding domains.";
J. Cell Sci. 112:2715-2724(1999).
[12]
INTERACTION WITH SNAPIN.
PubMed=10195194; DOI=10.1038/5673;
Ilardi J.M., Mochida S., Sheng Z.-H.;
"Snapin: a SNARE-associated protein implicated in synaptic
transmission.";
Nat. Neurosci. 2:119-124(1999).
[13]
PHOSPHORYLATION AT THR-138 AND SER-187.
PubMed=12459461; DOI=10.1016/S0014-5793(02)03629-3;
Hepp R., Cabaniols J.-P., Roche P.A.;
"Differential phosphorylation of SNAP-25 in vivo by protein kinase C
and protein kinase A.";
FEBS Lett. 532:52-56(2002).
[14]
INTERACTION WITH SYT1; SV2B AND SYNTAXIN-1.
PubMed=15466855; DOI=10.1074/jbc.M407502200;
Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.;
"SV2B regulates synaptotagmin 1 by direct interaction.";
J. Biol. Chem. 279:52124-52131(2004).
[15]
INTERACTION WITH OTOF.
STRAIN=BALB/cJ; TISSUE=Cochlea;
PubMed=17055430; DOI=10.1016/j.cell.2006.08.040;
Roux I., Safieddine S., Nouvian R., Grati M., Simmler M.-C.,
Bahloul A., Perfettini I., Le Gall M., Rostaing P., Hamard G.,
Triller A., Avan P., Moser T., Petit C.;
"Otoferlin, defective in a human deafness form, is essential for
exocytosis at the auditory ribbon synapse.";
Cell 127:277-289(2006).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CENPF.
PubMed=16672379; DOI=10.1091/mbc.E05-12-1127;
Pooley R.D., Reddy S., Soukoulis V., Roland J.T., Goldenring J.R.,
Bader D.M.;
"CytLEK1 is a regulator of plasma membrane recycling through its
interaction with SNAP-25.";
Mol. Biol. Cell 17:3176-3186(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-154, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Brown adipose tissue;
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).
[18]
INTERACTION WITH EQTN.
PubMed=19285662; DOI=10.1016/j.fertnstert.2009.01.067;
Hu X.Q., Ji S.Y., Li Y.C., Fan C.H., Cai H., Yang J.L., Zhang C.P.,
Chen M., Pan Z.F., Hu Z.Y., Gao F., Liu Y.X.;
"Acrosome formation-associated factor is involved in fertilization.";
Fertil. Steril. 93:1482-1492(2010).
[19]
ASSOCIATION WITH THE BLOC-1 COMPLEX, SUBCELLULAR LOCATION, AND
INTERACTION WITH BLOC1S6.
PubMed=19546860; DOI=10.1038/mp.2009.58;
Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
Dell'Angelica E.C.;
"The dysbindin-containing complex (BLOC-1) in brain: developmental
regulation, interaction with SNARE proteins and role in neurite
outgrowth.";
Mol. Psychiatry 15:204-215(2010).
[20]
INTERACTION WITH SYT9 AND HSC70.
PubMed=20847230; DOI=10.1096/fj.09-152033;
Boal F., Laguerre M., Milochau A., Lang J., Scotti P.A.;
"A charged prominence in the linker domain of the cysteine-string
protein Cspalpha mediates its regulated interaction with the calcium
sensor synaptotagmin 9 during exocytosis.";
FASEB J. 25:132-143(2011).
[21]
INTERACTION WITH PRRT2.
PubMed=22832103; DOI=10.1016/j.celrep.2011.11.001;
Lee H.Y., Huang Y., Bruneau N., Roll P., Roberson E.D., Hermann M.,
Quinn E., Maas J., Edwards R., Ashizawa T., Baykan B., Bhatia K.,
Bressman S., Bruno M.K., Brunt E.R., Caraballo R., Echenne B.,
Fejerman N., Frucht S., Gurnett C.A., Hirsch E., Houlden H.,
Jankovic J., Lee W.L., Lynch D.R., Mohammed S., Mueller U.,
Nespeca M.P., Renner D., Rochette J., Rudolf G., Saiki S., Soong B.W.,
Swoboda K.J., Tucker S., Wood N., Hanna M., Bowcock A.M.,
Szepetowski P., Fu Y.H., Ptacek L.J.;
"Mutations in the gene PRRT2 cause paroxysmal kinesigenic dyskinesia
with infantile convulsions.";
Cell Rep. 1:2-12(2012).
[22]
INTERACTION WITH PLCL1.
PubMed=23341457; DOI=10.1074/jbc.M112.419317;
Zhang Z., Takeuchi H., Gao J., Wang D., James D.J., Martin T.F.,
Hirata M.;
"PRIP (phospholipase C-related but catalytically inactive protein)
inhibits exocytosis by direct interactions with syntaxin 1 and SNAP-25
through its C2 domain.";
J. Biol. Chem. 288:7769-7780(2013).
[23]
INTERACTION WITH ZDHHC17 AND ZDHHC13.
PubMed=25253725; DOI=10.1091/mbc.E14-06-1169;
Lemonidis K., Gorleku O.A., Sanchez-Perez M.C., Grefen C.,
Chamberlain L.H.;
"The Golgi S-acylation machinery comprises zDHHC enzymes with major
differences in substrate affinity and S-acylation activity.";
Mol. Biol. Cell 25:3870-3883(2014).
[24]
INTERACTION WITH ZDHHC17 AND ZDHHC13.
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).
[25]
INTERACTION WITH PRRT2.
PubMed=27052163; DOI=10.1016/j.celrep.2016.03.005;
Valente P., Castroflorio E., Rossi P., Fadda M., Sterlini B.,
Cervigni R.I., Prestigio C., Giovedi S., Onofri F., Mura E.,
Guarnieri F.C., Marte A., Orlando M., Zara F., Fassio A., Valtorta F.,
Baldelli P., Corradi A., Benfenati F.;
"PRRT2 Is a Key Component of the Ca(2+)-Dependent Neurotransmitter
Release Machinery.";
Cell Rep. 15:117-131(2016).
[26]
INTERACTION WITH PRRT2.
PubMed=29056747; DOI=10.1038/cr.2017.128;
Tan G.H., Liu Y.Y., Wang L., Li K., Zhang Z.Q., Li H.F., Yang Z.F.,
Li Y., Li D., Wu M.Y., Yu C.L., Long J.J., Chen R.C., Li L.X.,
Yin L.P., Liu J.W., Cheng X.W., Shen Q., Shu Y.S., Sakimura K.,
Liao L.J., Wu Z.Y., Xiong Z.Q.;
"PRRT2 deficiency induces paroxysmal kinesigenic dyskinesia by
regulating synaptic transmission in cerebellum.";
Cell Res. 28:90-110(2018).
[27]
3D-STRUCTURE MODELING OF 18-206 IN COMPLEX WITH VAMP2 AND STX1A.
PubMed=9731768; DOI=10.1038/1799;
Poirier M.A., Xiao W., Macosko J.C., Chan C., Shin Y.K., Bennett M.K.;
"The synaptic SNARE complex is a parallel four-stranded helical
bundle.";
Nat. Struct. Biol. 5:765-769(1998).
-!- FUNCTION: t-SNARE involved in the molecular regulation of
neurotransmitter release (PubMed:8243676, PubMed:8103915). May
play an important role in the synaptic function of specific
neuronal systems. Associates with proteins involved in vesicle
docking and membrane fusion. Regulates plasma membrane recycling
through its interaction with CENPF (PubMed:16672379). Modulates
the gating characteristics of the delayed rectifier voltage-
dependent potassium channel KCNB1 in pancreatic beta cells (By
similarity). {ECO:0000250|UniProtKB:P60881,
ECO:0000269|PubMed:16672379, ECO:0000305|PubMed:8103915,
ECO:0000305|PubMed:8243676}.
-!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2
and STX1A, this complex binds CPLX1 (By similarity). Found in a
complex containing SYT1, SV2B and syntaxin-1 (PubMed:15466855).
Found in a ternary complex with STX1A and VAMP8 (By similarity).
Isoform 1 and isoform 2 interact with BLOC1S6 (PubMed:19546860).
Interacts with CENPF (PubMed:16672379). Interacts with EQTN
(PubMed:19285662). Interacts with HGS (By similarity). Interacts
with KCNB1 (via N-terminus); reduces the voltage-dependent
potassium channel KCNB1 activity in pancreatic beta cells (By
similarity). Interacts with OTOF (PubMed:17055430). Interacts with
RIMS1 (By similarity). Interacts with SNAPIN (PubMed:10195194).
Interacts with STXBP6 (By similarity). Interacts with TRIM9 (By
similarity). Interacts with ZDHHC13 (via ANK repeats)
(PubMed:25253725). Interacts with ZDHHC17 (via ANK repeats)
(PubMed:25253725). Associates with the BLOC-1 complex
(PubMed:19546860). Interacts with HSC70 and with SYT9, forming a
complex with DNAJC5 (PubMed:20847230). The interaction with SYT9
is inhibited in presence of calcium (PubMed:20847230). Interacts
with PLCL1 (via C2 domain) (PubMed:23341457). Interacts with
PRRT2; this interaction may impair the formation of the SNARE
complex (PubMed:22832103, PubMed:27052163, PubMed:29056747).
{ECO:0000250|UniProtKB:P60881, ECO:0000269|PubMed:10195194,
ECO:0000269|PubMed:15466855, ECO:0000269|PubMed:16672379,
ECO:0000269|PubMed:17055430, ECO:0000269|PubMed:19285662,
ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:20847230,
ECO:0000269|PubMed:22832103, ECO:0000269|PubMed:23341457,
ECO:0000269|PubMed:25253725, ECO:0000269|PubMed:27052163,
ECO:0000269|PubMed:29056747}.
-!- INTERACTION:
Q155P7:Cenpf; NbExp=13; IntAct=EBI-445270, EBI-2211248;
O35526:Stx1a; NbExp=4; IntAct=EBI-445270, EBI-400878;
P32851:Stx1a (xeno); NbExp=7; IntAct=EBI-445270, EBI-539720;
P63044:Vamp2; NbExp=10; IntAct=EBI-445270, EBI-521920;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:16672379}. Cell membrane
{ECO:0000269|PubMed:10413679, ECO:0000269|PubMed:9349529}; Lipid-
anchor {ECO:0000269|PubMed:9349529}. Cell junction, synapse,
synaptosome {ECO:0000269|PubMed:2592413}. Note=Colocalizes with
KCNB1 at the cell membrane (By similarity). Membrane association
requires palmitoylation (PubMed:9349529). Expressed throughout
cytoplasm, concentrating at the perinuclear region
(PubMed:16672379). {ECO:0000250|UniProtKB:P60881,
ECO:0000269|PubMed:16672379, ECO:0000269|PubMed:9349529}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Isoforms differ by the usage of two alternative
homologous exons (5a and 5b) which code for positions 56 to 94
and differ only in 9 positions out of 39.;
Name=1; Synonyms=SNAP-25b;
IsoId=P60879-1, P13795-1;
Sequence=Displayed;
Name=2; Synonyms=SNAP-25a;
IsoId=P60879-2, P13795-2;
Sequence=VSP_010019;
-!- PTM: Palmitoylated. Cys-85 appears to be the main site, and
palmitoylation is required for membrane association.
{ECO:0000269|PubMed:9349529}.
-!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
neurotoxin type A (BoNT/A, botA) which hydrolyzes the 197-Gln-|-
Arg-198 bond and inhibits neurotransmitter release
(PubMed:8243676, PubMed:8103915). {ECO:0000269|PubMed:8243676,
ECO:0000305|PubMed:10413679, ECO:0000305|PubMed:8103915}.
-!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
neurotoxin type E (BoNT/E) which hydrolyzes the 180-Arg-|-Ile-181
bond and inhibits neurotransmitter release (PubMed:8243676,
PubMed:8103915). {ECO:0000269|PubMed:8243676,
ECO:0000305|PubMed:10413679, ECO:0000305|PubMed:8103915}.
-!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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EMBL; M22012; AAA61741.1; -; mRNA.
EMBL; AF483516; AAL90790.1; -; mRNA.
EMBL; AF483517; AAL90791.1; -; mRNA.
EMBL; AK078038; BAC37105.1; -; mRNA.
EMBL; AL732447; CAM15064.1; -; Genomic_DNA.
EMBL; AL732447; CAM15065.1; -; Genomic_DNA.
EMBL; CH466519; EDL28390.1; -; Genomic_DNA.
EMBL; BC018249; AAH18249.1; -; mRNA.
CCDS; CCDS16793.1; -.
CCDS; CCDS71153.1; -. [P60879-2]
PIR; A33623; A33623.
RefSeq; NP_001277985.1; NM_001291056.1. [P60879-2]
RefSeq; NP_035558.1; NM_011428.3. [P60879-1]
RefSeq; XP_017172247.1; XM_017316758.1.
RefSeq; XP_017172249.1; XM_017316760.1. [P60879-2]
UniGene; Mm.45953; -.
PDB; 2BU0; Model; -; C=18-82, D=139-206.
PDBsum; 2BU0; -.
ProteinModelPortal; P60879; -.
SMR; P60879; -.
BioGrid; 203362; 32.
CORUM; P60879; -.
DIP; DIP-29066N; -.
IntAct; P60879; 42.
MINT; P60879; -.
STRING; 10090.ENSMUSP00000028727; -.
TCDB; 1.F.1.1.4; the synaptosomal vesicle fusion pore (svf-pore) family.
iPTMnet; P60879; -.
PhosphoSitePlus; P60879; -.
SwissPalm; P60879; -.
MaxQB; P60879; -.
PaxDb; P60879; -.
PeptideAtlas; P60879; -.
PRIDE; P60879; -.
Ensembl; ENSMUST00000028727; ENSMUSP00000028727; ENSMUSG00000027273. [P60879-1]
Ensembl; ENSMUST00000110098; ENSMUSP00000105725; ENSMUSG00000027273. [P60879-2]
GeneID; 20614; -.
KEGG; mmu:20614; -.
UCSC; uc008mop.1; mouse.
UCSC; uc056zpt.1; mouse. [P60879-2]
CTD; 6616; -.
MGI; MGI:98331; Snap25.
eggNOG; KOG3065; Eukaryota.
eggNOG; ENOG410Y3Y0; LUCA.
GeneTree; ENSGT00390000012186; -.
HOVERGEN; HBG056971; -.
InParanoid; P60879; -.
KO; K18211; -.
OMA; GEMDENL; -.
OrthoDB; EOG091G0N7J; -.
PhylomeDB; P60879; -.
TreeFam; TF315125; -.
Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
Reactome; R-MMU-449836; Other interleukin signaling.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
ChiTaRS; Snap25; mouse.
PRO; PR:P60879; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027273; Expressed in 183 organ(s), highest expression level in cerebral cortex.
CleanEx; MM_SNAP25; -.
Genevisible; P60879; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0030424; C:axon; IDA:ParkinsonsUK-UCL.
GO; GO:0044295; C:axonal growth cone; ISO:MGI.
GO; GO:0031083; C:BLOC-1 complex; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:SynGO-UCL.
GO; GO:0030175; C:filopodium; ISO:MGI.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0043229; C:intracellular organelle; ISO:MGI.
GO; GO:0030027; C:lamellipodium; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0098794; C:postsynapse; IDA:SynGO.
GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
GO; GO:0036477; C:somatodendritic compartment; IDA:ParkinsonsUK-UCL.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; ISO:MGI.
GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IDA:MGI.
GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; ISO:MGI.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
GO; GO:0048306; F:calcium-dependent protein binding; ISS:ParkinsonsUK-UCL.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0017022; F:myosin binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0000149; F:SNARE binding; IDA:MGI.
GO; GO:0017075; F:syntaxin-1 binding; IDA:ParkinsonsUK-UCL.
GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
GO; GO:0008306; P:associative learning; IMP:MGI.
GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; ISO:MGI.
GO; GO:0016197; P:endosomal transport; ISO:MGI.
GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IMP:SynGO.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0007616; P:long-term memory; ISO:MGI.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
GO; GO:0099590; P:neurotransmitter receptor internalization; IMP:SynGO.
GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
GO; GO:0046887; P:positive regulation of hormone secretion; ISO:MGI.
GO; GO:0031915; P:positive regulation of synaptic plasticity; IMP:MGI.
GO; GO:0070201; P:regulation of establishment of protein localization; IMP:MGI.
GO; GO:0010975; P:regulation of neuron projection development; IGI:ParkinsonsUK-UCL.
GO; GO:1990926; P:short-term synaptic potentiation; IMP:MGI.
GO; GO:0030431; P:sleep; ISO:MGI.
GO; GO:0035493; P:SNARE complex assembly; ISO:MGI.
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; IPR039077; SNAP25.
InterPro; IPR000727; T_SNARE_dom.
PANTHER; PTHR19305:SF5; PTHR19305:SF5; 1.
Pfam; PF00835; SNAP-25; 1.
SMART; SM00397; t_SNARE; 2.
PROSITE; PS50192; T_SNARE; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
Repeat; Synapse; Synaptosome.
CHAIN 1 206 Synaptosomal-associated protein 25.
/FTId=PRO_0000213589.
DOMAIN 19 81 t-SNARE coiled-coil homology 1.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
DOMAIN 140 202 t-SNARE coiled-coil homology 2.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
REGION 1 75 Interaction with CENPF.
{ECO:0000269|PubMed:16672379}.
REGION 111 120 Interaction with ZDHHC17.
{ECO:0000250|UniProtKB:P60880}.
COMPBIAS 85 92 Cys-rich.
SITE 180 181 (Microbial infection) Cleavage; by
C.botulinum neurotoxin type E (BoNT/E).
{ECO:0000269|PubMed:8243676,
ECO:0000305|PubMed:8103915}.
SITE 197 198 (Microbial infection) Cleavage; by
C.botulinum neurotoxin type A (BoNT/A,
botA). {ECO:0000269|PubMed:8243676,
ECO:0000305|PubMed:8103915}.
MOD_RES 138 138 Phosphothreonine; by PKC and PKA.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:12459461}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 187 187 Phosphoserine; by PKC.
{ECO:0000269|PubMed:12459461}.
LIPID 85 85 S-palmitoyl cysteine.
{ECO:0000269|PubMed:9349529}.
LIPID 88 88 S-palmitoyl cysteine.
{ECO:0000269|PubMed:9349529}.
LIPID 90 90 S-palmitoyl cysteine.
{ECO:0000269|PubMed:9349529}.
LIPID 92 92 S-palmitoyl cysteine.
{ECO:0000269|PubMed:9349529}.
VAR_SEQ 58 89 ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV -> DRVEE
GMNHINQDMKEAEKNLKDLGKCCGLFI (in isoform
2). {ECO:0000303|PubMed:11471062,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2592413}.
/FTId=VSP_010019.
MUTAGEN 85 85 C->S: 91% reduction in palmitoylation
level. 14% membrane association. No
palmitoylation and less than 8% membrane
association; when associated with S-88 or
A-88. {ECO:0000269|PubMed:9349529}.
MUTAGEN 88 88 C->S: 79% reduction in palmitoylation
level. 18% membrane association. No
palmitoylation and less than 8% membrane
association; when associated with S-85 or
A-85. {ECO:0000269|PubMed:9349529}.
MUTAGEN 90 90 C->S: 58% reduction in palmitoylation
level. 28% membrane association. Very
little palmitoylation and less than 8%
membrane association; when associated
with S-92 or A-92.
{ECO:0000269|PubMed:9349529}.
MUTAGEN 92 92 C->S: 65% reduction in palmitoylation
level. 29% membrane association. No
palmitoylation and less than 8% membrane
association; when associated with S-90 or
A-90. {ECO:0000269|PubMed:9349529}.
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


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