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UniProtKB/Swiss-Prot entry P60879


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SNP25_MOUSE
Primary accession number P60879
Secondary accession numbers A2AIC2 A2AIC3 P13795 P36974 P70557 P70558 Q8IXK3 Q96FM2 Q9BR45
Integrated into Swiss-Prot on April 13, 2004
Sequence was last modified on April 13, 2004 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 69)
Name and origin of the protein
Protein name Synaptosomal-associated protein 25
Synonyms SNAP-25
Synaptosomal-associated 25 kDa protein
Super protein
SUP
Gene name
Name: Snap25
Synonyms: Snap
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SNAP-25A), AND SUBCELLULAR LOCATION.
STRAIN=BALB/c;
DOI=10.1083/jcb.109.6.3039; PubMed=2592413 [NCBI, ExPASy, EBI, Israel, Japan]
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 SNAP-25A).
STRAIN=ILS, and ISS;
DOI=10.1007/s00335-001-1001-x; PubMed=11471062 [NCBI, ExPASy, EBI, Israel, Japan]
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 SNAP-25B).
STRAIN=C57BL/6J;
TISSUE=Medulla oblongata;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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;
The mouse genome sequencing consortium;
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
[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 SNAP-25A).
STRAIN=C57BL/6;
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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 MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[8]
PALMITOYLATION AT CYS-85; CYS-88; CYS-90 AND CYS-92, AND MUTAGENESIS OF CYS-85; CYS-88; CYS-90 AND CYS-92.
PubMed=9349529 [NCBI, ExPASy, EBI, Israel, Japan]
Lane S.R., Liu Y.;
"Characterization of the palmitoylation domain of SNAP-25.";
J. Neurochem. 69:1864-1869(1997).
[9]
INTERACTION WITH SNAP25BP.
DOI=10.1038/5673; PubMed=10195194 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/S0014-5793(02)03629-3; PubMed=12459461 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1074/jbc.M407502200; PubMed=15466855 [NCBI, ExPASy, EBI, Israel, Japan]
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/c;
TISSUE=Cochlea;
DOI=10.1016/j.cell.2006.08.040; PubMed=17055430 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1091/mbc.E05-12-1127; PubMed=16672379 [NCBI, ExPASy, EBI, Israel, Japan]
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]
3D-STRUCTURE MODELING OF 18-206 IN COMPLEX WITH VAMP2 AND STX1A.
DOI=10.1038/1799; PubMed=9731768 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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.
  • SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds CPLX1. Interacts with TRIM9, RIMS1, SNAP25BP and HGS. Binds STXBP6. Found in a ternary complex with STX1A and VAMP8 (By similarity). Found in a complex containing SYT1, SV2B and syntaxin-1. Interacts with CENPF and OTOF.
  • INTERACTION:
    Q155P7:Cenpf; NbExp=5; IntAct=EBI-445270, EBI-2211248;
  • SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cell membrane; Lipid-anchor. Cell junction, synapse, synaptosome. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing. Isoforms differ by the usage of two alternative homologous exons (5a and 5b) which encode for positions 56 to 94 and differ only in 9 positions out of 39.
    NameSNAP-25b
    Isoform IDP60879-1, P13795-1
    This is the isoform sequence displayed in this entry.
    NameSNAP-25a
    Isoform IDP60879-2, P13795-2
    Features which should be applied to build the isoform sequence: VSP_010019.
  • PTM: Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association.
  • SIMILARITY: Belongs to the SNAP-25 family.
  • SIMILARITY: Contains 2 t-SNARE coiled-coil homology domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M22012; AAA61741.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF483516; AAL90790.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF483517; AAL90791.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK078038; BAC37105.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL732447; CAM15064.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL732447; CAM15065.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH466519; EDL28390.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018249; AAH18249.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00125635; -.
IPI00225389; -.
PIR A33623; A33623.
RefSeq NP_035558.1; -.
UniGene Mm.45953
3D structure databases
PDB
2BU0; Model; -; C=18-82, D=139-206.[ExPASy / RCSB / EBI]
PDBsum 2BU0; -.
SMR P60879; 7-83, 131-204.
ModBase P60879.
Protein-protein interaction databases
DIP DIP:29066N; -.
IntAct P60879; 4.
PTM databases
PhosphoSite P60879; -.
Organism-specific databases
MGI MGI:98331; Snap25.
Gene expression databases
ArrayExpress P60879; -.
Bgee P60879; -.
CleanEx MM_SNAP25; -.
GermOnline ENSMUSG00000027273; Mus musculus.
Ontologies
GO
GO:0030054; Cellular component: cell junction (inferred from electronic annotation from UniProtKB-SubCell).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0045202; Cellular component: synapse (inferred from electronic annotation from UniProtKB-SubCell).
GO:0019717; Cellular component: synaptosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005802; Cellular component: trans-Golgi network (inferred from direct assay from UniProtKB).
GO:0000149; Molecular function: SNARE binding (inferred from direct assay from MGI).
GO:0007269; Biological process: neurotransmitter secretion (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000928; SNAP-25.
IPR000727; T_SNARE.
Graphical view of domain structure.
Pfam PF00835; SNAP-25; 1.
PF05739; SNARE; 1.
Pfam graphical view of domain structure.
SMART SM00397; t_SNARE; 2.
SMART graphical view of domain structure.
PROSITE PS50192; T_SNARE; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P60879; -.
Genome annotation databases
Ensembl ENSMUSG00000027273; Mus musculus. [Contig view]
GeneID 20614; -.
KEGG mmu:20614; -.
Phylogenomic databases
HOVERGEN P60879; -.
OMA P60879; LADEXSK.
Other
NextBio 298983; -.
SOURCE Snap25; Mus musculus.
ProtoNet P60879.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell junction; Cell membrane; Coiled coil; Cytoplasm; Direct protein sequencing; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Repeat; Synapse; Synaptosome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   206  206     Synaptosomal-associated protein 25. PRO_0000213589
DOMAIN   19    81  63     t-SNARE coiled-coil homology 1. 
DOMAIN   140   202  63     t-SNARE coiled-coil homology 2. 
REGION   1    75  75     Interaction with CENPF. 
COMPBIAS   85    92  8     Cys-rich. 
SITE   180   181  2     Cleavage; by BONT/E (By similarity). 
MOD_RES   138   138        Phosphothreonine; by PKC and PKA. 
MOD_RES   187   187        Phosphoserine; by PKC. 
LIPID   85    85        S-palmitoyl cysteine. 
LIPID   88    88        S-palmitoyl cysteine. 
LIPID   90    90        S-palmitoyl cysteine. 
LIPID   92    92        S-palmitoyl cysteine. 
VAR_SEQ   58    89        ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV -> DRVEEGMNHINQDMKEAEKNLKDLGKCCGLFI (in isoform SNAP-25a). 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. 
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. 
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. 
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. 
HELIX   21    73  53      
TURN   74    76  3      
HELIX   77    81  5      
TURN   140   143  4      
HELIX   144   202  59      
TURN   203   205  3      
Sequence information
Length: 206 AA [This is the length of the unprocessed precursor] Molecular weight: 23315 Da [This is the MW of the unprocessed precursor] CRC64: FBED2B082A4CB6A6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI 

        70         80         90        100        110        120 
EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV 

       130        140        150        160        170        180 
VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR 

       190        200 
IMEKADSNKT RIDEANQRAT KMLGSG 

P60879 in FASTA format

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