[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SNAP-25A AND SNAP-25B). Kataoka M.; Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SNAP-25A). TISSUE=Brain; Cho A.R., You K.H.; "Cloning of the SNAP-25 gene from a rat brain cDNA library."; Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-25B). TISSUE=Brain; 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).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 10-190 (ISOFORM SNAP-25B). TISSUE=Brain; DOI=10.1046/j.1471-4159.1999.0720988.x; PubMed=10037470 [NCBI, ExPASy, EBI, Israel, Japan] Madison D.L., Krueger W.H., Cheng D., Trapp B.D., Pfeiffer S.E.; "SNARE complex proteins, including the cognate pair VAMP-2 and syntaxin-4, are expressed in cultured oligodendrocytes."; J. Neurochem. 72:988-998(1999).
[5]	PROTEIN SEQUENCE OF 46-69; 84-94; 104-119; 125-136 AND 143-161, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord; Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.; Submitted (SEP-2007) to UniProtKB.
[6]	PALMITOYLATION, AND SUBCELLULAR LOCATION. PubMed=1281490 [NCBI, ExPASy, EBI, Israel, Japan] Hess D.T., Slater T.M., Wilson M.C., Skene J.H.P.; "The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS."; J. Neurosci. 12:4634-4641(1992).
[7]	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).
[8]	SUBCELLULAR LOCATION OF RNA TRANSCRIPTS. DOI=10.1016/0169-328X(95)00272-T; PubMed=8738135 [NCBI, ExPASy, EBI, Israel, Japan] Jacobsson G., Piehl F., Bark I.C., Zhang X., Meister B.; "Differential subcellular localization of SNAP-25a and SNAP-25b RNA transcripts in spinal motoneurons and plasticity in expression after nerve injury."; Brain Res. Mol. Brain Res. 37:49-62(1996).
[9]	INTERACTION WITH HGS. DOI=10.1038/385826a0; PubMed=9039916 [NCBI, ExPASy, EBI, Israel, Japan] Bean A.J., Seifert R., Chen Y.A., Sacks R., Scheller R.H.; "Hrs-2 is an ATPase implicated in calcium-regulated secretion."; Nature 385:826-829(1997).
[10]	IDENTIFICATION IN A TERNARY COMPLEX WITH STX1A AND VAMP8. DOI=10.1074/jbc.274.22.15440; PubMed=10336434 [NCBI, ExPASy, EBI, Israel, Japan] Fasshauer D., Antonin W., Margittai M., Pabst S., Jahn R.; "Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties."; J. Biol. Chem. 274:15440-15446(1999).
[11]	INTERACTION WITH RIMS1. DOI=10.1074/jbc.M100929200; PubMed=11438518 [NCBI, ExPASy, EBI, Israel, Japan] Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S., Schiavo G., Regazzi R.; "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin."; J. Biol. Chem. 276:32756-32762(2001).
[12]	INTERACTION WITH STXBP6. DOI=10.1074/jbc.M204929200; PubMed=12145319 [NCBI, ExPASy, EBI, Israel, Japan] Scales S.J., Hesser B.A., Masuda E.S., Scheller R.H.; "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly."; J. Biol. Chem. 277:28271-28279(2002).
[13]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-83 AND 120-206 IN COMPLEX WITH STX1A AND VAMP2. DOI=10.1038/26412; PubMed=9759724 [NCBI, ExPASy, EBI, Israel, Japan] Sutton R.B., Fasshauer D., Jahn R., Brunger A.T.; "Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution."; Nature 395:347-353(1998).
[14]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-83 IN COMPLEX WITH STX1A. DOI=10.1074/jbc.M106853200; PubMed=11533035 [NCBI, ExPASy, EBI, Israel, Japan] Misura K.M.S., Gonzalez L.C. Jr., May A.P., Scheller R.H., Weis W.I.; "Crystal structure and biophysical properties of a complex between the N-terminal SNARE region of SNAP25 and syntaxin 1a."; J. Biol. Chem. 276:41301-41309(2001).
[15]	X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 7-83 AND 141-204 IN COMPLEX WITH STX1A AND VAMP2. DOI=10.1074/jbc.M211889200; PubMed=12496247 [NCBI, ExPASy, EBI, Israel, Japan] Ernst J.A., Brunger A.T.; "High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex."; J. Biol. Chem. 278:8630-8636(2003).

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: Interacts with CENP and OTOF. Found in a complex containing SYT1, SV2B and syntaxin-1 (By similarity). 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.
INTERACTION:
Q9QXY2:P140; NbExp=1; IntAct=EBI-1027214, EBI-1394088;
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By similarity). Cell membrane; Lipid-anchor. Cell junction, synapse, synaptosome. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region (By similarity).

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.

Name	SNAP-25b
Isoform ID	P60881-1, P13795-1
This is the isoform sequence displayed in this entry.

Name	SNAP-25a
Isoform ID	P60881-2, P13795-2
Features which should be applied to build the isoform sequence: VSP_010020.

PTM: Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association (By similarity).
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

AB003991; BAA20151.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB003992; BAA20152.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF245227; AAF81202.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U56262; AAA99826.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC087699; AAH87699.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U56261; AAA99825.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00204644; -.
IPI00231420; -.

RefSeq

NP_112253.1; -.

UniGene

Rn.107689

3D structure databases

PDB

1JTH; X-ray; 2.00 A; A/C=1-82.	[ExPASy / RCSB / EBI]
1N7S; X-ray; 1.45 A; C=7-83, D=141-204.	[ExPASy / RCSB / EBI]
1SFC; X-ray; 2.40 A; C/G/K=1-83, D/H/L=120-206.	[ExPASy / RCSB / EBI]
1URQ; X-ray; 2.00 A; C=7-83, D=142-204.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1JTH; -.
1N7S; -.
1SFC; -.
1URQ; -.

DisProt

DP00068; -.

ModBase

P60881.

Protein-protein interaction databases

DIP

DIP:29205N; -.

IntAct

P60881; 5.

PTM databases

PhosphoSite

P60881; -.

Organism-specific databases

RGD

3728; Snap25.

Gene expression databases

ArrayExpress

P60881; -.

GermOnline

ENSRNOG00000006037; Rattus norvegicus.

Ontologies

GO:0030054;	Cellular component: cell junction (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005768;	Cellular component: endosome (inferred from direct assay from RGD).
GO:0030426;	Cellular component: growth cone (inferred from direct assay from HGNC).
GO:0045121;	Cellular component: membrane raft (inferred from direct assay from RGD).
GO:0043005;	Cellular component: neuron projection (inferred from direct assay from HGNC).
GO:0048471;	Cellular component: perinuclear region of cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0045202;	Cellular component: synapse (inferred from electronic annotation from UniProtKB-SubCell).
GO:0070044;	Cellular component: synaptobrevin 2-SNAP-25-syntaxin-1a complex (inferred from direct assay from MGI).
GO:0070032;	Cellular component: synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex (inferred from direct assay from MGI).
GO:0019717;	Cellular component: synaptosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008076;	Cellular component: voltage-gated potassium channel complex (inferred from physical interaction from RGD).
GO:0017022;	Molecular function: myosin binding (inferred from physical interaction from RGD).
GO:0047485;	Molecular function: protein N-terminus binding (inferred from physical interaction from RGD).
GO:0005484;	Molecular function: SNAP receptor activity (traceable author statement from RGD).
GO:0017075;	Molecular function: syntaxin-1 binding (inferred from direct assay from MGI).
GO:0005249;	Molecular function: voltage-gated potassium channel activity (inferred from direct assay from RGD).
GO:0007409;	Biological process: axonogenesis (inferred from expression pattern from RGD).
GO:0048791;	Biological process: calcium ion-dependent exocytosis of neurotransmitter (inferred from direct assay from RGD).
GO:0016197;	Biological process: endosome transport (inferred from direct assay from RGD).
GO:0006887;	Biological process: exocytosis (traceable author statement from RGD).
GO:0030252;	Biological process: growth hormone secretion (inferred from expression pattern from RGD).
GO:0007616;	Biological process: long-term memory (inferred from mutant phenotype from RGD).
GO:0032024;	Biological process: positive regulation of insulin secretion (inferred from expression pattern from RGD).
GO:0051963;	Biological process: regulation of synaptogenesis (inferred from expression pattern from RGD).
GO:0030431;	Biological process: sleep (inferred from direct assay from RGD).
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

P60881; -.

Genome annotation databases

Ensembl

ENSRNOG00000006037; Rattus norvegicus. [Contig view]

GeneID

25012; -.

KEGG

rno:25012; -.

Phylogenomic databases

HOVERGEN

P60881; -.

Other

605093; -.

P60881; -.

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

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 206`	`206`	`Synaptosomal-associated protein 25.`	`PRO_0000213592`
`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 (By similarity).`
`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 (By similarity).`
`LIPID`	`88 88`		`S-palmitoyl cysteine (By similarity).`
`LIPID`	`90 90`		`S-palmitoyl cysteine (By similarity).`
`LIPID`	`92 92`		`S-palmitoyl cysteine (By similarity).`
`VAR_SEQ`	`58 89`		`ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV -> DRVEEGMNHINQDMKEAEKNLKDLGKCCGLFI (in isoform SNAP-25a).`	`VSP_010020`
`HELIX`	`7 82`	`76`
`HELIX`	`142 201`	`60`

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

P60881 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools