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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.
22-NOV-2017, entry version 147.
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]
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).
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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. 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}.
-!- 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).
{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:23341457, ECO:0000269|PubMed:25253725}.
-!- 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: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}.
-!- 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. [P60879-1]
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; MINT-2411221; -.
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-181430; Norepinephrine Neurotransmitter Release Cycle.
Reactome; R-MMU-210500; Glutamate 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; -.
CleanEx; MM_SNAP25; -.
Genevisible; P60879; MM.
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:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:SynGO-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:MGI.
GO; GO:0098794; C:postsynapse; IDA:SynGO.
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:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; ISS:ParkinsonsUK-UCL.
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:0008306; P:associative learning; IMP: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: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:0031915; P:positive regulation of synaptic plasticity; IMP:MGI.
GO; GO:0070201; P:regulation of establishment of protein localization; IMP:MGI.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0010975; P:regulation of neuron projection development; IGI:ParkinsonsUK-UCL.
GO; GO:1990926; P:short-term synaptic potentiation; IMP: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; IPR000727; T_SNARE_dom.
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 Cleavage; by BONT/E. {ECO:0000250}.
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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