Reviewed, UniProtKB/Swiss-Prot P60879 (SNP25_MOUSE)

Names and origin

Protein names

Recommended name:
    Synaptosomal-associated protein 25
      Short name=SNAP-25
Alternative name(s):
    Synaptosomal-associated 25 kDa protein
    Super protein
      Short name=SUP

Gene names

Name:	Snap25
Synonyms:	Snap

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Ref.13
Subunit structure	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.
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. Ref.13 Ref.1
Post-translational modification	Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association. Ref.8
Sequence similarities	Belongs to the SNAP-25 family. Contains 2 t-SNARE coiled-coil homology domains.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	neurotransmitter secretion Inferred from mutant phenotype. Source: MGI
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB synapse Inferred from electronic annotation. Source: UniProtKB-KW synaptosome Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network Inferred from direct assay. Source: UniProtKB
Molecular function	SNARE binding Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cenpf	Q155P7	5	EBI-445270,EBI-2211248

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: 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.

Isoform SNAP-25b (identifier: P60879-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform SNAP-25a (identifier: P60879-2)

The sequence of this isoform differs from the canonical sequence as follows:
     58-89: ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV → DRVEEGMNHINQDMKEAEKNLKDLGKCCGLFI

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 206

206

Synaptosomal-associated protein 25

PRO_0000213589

Regions

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

Compositional bias

85 – 92

8

Cys-rich

Sites

Site

180 – 181

2

Cleavage; by BONT/E By similarity

Amino acid modifications

Modified residue

138

1

Phosphothreonine; by PKC and PKA Ref.10

Modified residue

187

1

Phosphoserine; by PKC Ref.10

Lipidation

85

1

S-palmitoyl cysteine Ref.8

Lipidation

88

1

S-palmitoyl cysteine Ref.8

Lipidation

90

1

S-palmitoyl cysteine Ref.8

Lipidation

92

1

S-palmitoyl cysteine Ref.8

Natural variations

Alternative sequence

58 – 89

32

ERIEE…CGLCV → DRVEEGMNHINQDMKEAEKN LKDLGKCCGLFI in isoform SNAP-25a.

VSP_010019

Experimental info

Mutagenesis

85

1

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. Ref.8

Mutagenesis

88

1

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. Ref.8

Mutagenesis

90

1

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. Ref.8

Mutagenesis

92

1

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. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

206

Helix Strand Turn

Details...

Helix

21 – 73

53

Turn

74 – 76

3

Helix

77 – 81

5

Turn

140 – 143

4

Helix

144 – 202

59

Turn

203 – 205

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform SNAP-25b [UniParc]. Last modified April 13, 2004. Version 1. Checksum: FBED2B082A4CB6A6	FASTA	206	23,315
	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
	Isoform SNAP-25a [UniParc] [UniParc]. Checksum: E272652C701EA984	FASTA	206	23,336
	10 20 30 40 50 60 MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLDRV 70 80 90 100 110 120 EEGMNHINQD MKEAEKNLKD LGKCCGLFIC PCNKLKSSDA YKKAWGNNQD GVVASQPARV 130 140 150 160 170 180 VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR 190 200 IMEKADSNKT RIDEANQRAT KMLGSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations." Oyler G.A., Higgins G.A., Hart R.A., Battenberg E., Billingsley M., Bloom F.E., Wilson M.C. J. Cell Biol. 109:3039-3052(1989) [PubMed: 2592413] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SNAP-25A), SUBCELLULAR LOCATION. Strain: BALB/c.
[2]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." 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. Mamm. Genome 12:657-663(2001) [PubMed: 11471062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SNAP-25A). Strain: ILS and ISS.
[3]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-25B). Strain: C57BL/6J. Tissue: Medulla oblongata.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-25A). Strain: C57BL/6. Tissue: Eye.
[7]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 18-31; 60-72; 125-135 AND 143-176, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[8]	"Characterization of the palmitoylation domain of SNAP-25." Lane S.R., Liu Y. J. Neurochem. 69:1864-1869(1997) [PubMed: 9349529] [Abstract] Cited for: PALMITOYLATION AT CYS-85; CYS-88; CYS-90 AND CYS-92, MUTAGENESIS OF CYS-85; CYS-88; CYS-90 AND CYS-92.
[9]	"Snapin: a SNARE-associated protein implicated in synaptic transmission." Ilardi J.M., Mochida S., Sheng Z.-H. Nat. Neurosci. 2:119-124(1999) [PubMed: 10195194] [Abstract] Cited for: INTERACTION WITH SNAP25BP.
[10]	"Differential phosphorylation of SNAP-25 in vivo by protein kinase C and protein kinase A." Hepp R., Cabaniols J.-P., Roche P.A. FEBS Lett. 532:52-56(2002) [PubMed: 12459461] [Abstract] Cited for: PHOSPHORYLATION AT THR-138 AND SER-187.
[11]	"SV2B regulates synaptotagmin 1 by direct interaction." Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R. J. Biol. Chem. 279:52124-52131(2004) [PubMed: 15466855] [Abstract] Cited for: INTERACTION WITH SYT1; SV2B AND SYNTAXIN-1.
[12]	"Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse." 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. Cell 127:277-289(2006) [PubMed: 17055430] [Abstract] Cited for: INTERACTION WITH OTOF. Strain: BALB/c. Tissue: Cochlea.
[13]	"CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25." Pooley R.D., Reddy S., Soukoulis V., Roland J.T., Goldenring J.R., Bader D.M. Mol. Biol. Cell 17:3176-3186(2006) [PubMed: 16672379] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPF.
[14]	"The synaptic SNARE complex is a parallel four-stranded helical bundle." Poirier M.A., Xiao W., Macosko J.C., Chan C., Shin Y.K., Bennett M.K. Nat. Struct. Biol. 5:765-769(1998) [PubMed: 9731768] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 18-206 IN COMPLEX WITH VAMP2 AND STX1A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M22012 mRNA. Translation: AAA61741.1.
AF483516 mRNA. Translation: AAL90790.1.
AF483517 mRNA. Translation: AAL90791.1.
AK078038 mRNA. Translation: BAC37105.1.
AL732447 Genomic DNA. Translation: CAM15064.1.
AL732447 Genomic DNA. Translation: CAM15065.1.
CH466519 Genomic DNA. Translation: EDL28390.1.
BC018249 mRNA. Translation: AAH18249.1.

IPI

IPI00125635.
IPI00225389.

PIR

A33623.

RefSeq

NP_035558.1.

UniGene

Mm.45953

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BU0	model	-	C	18-82	[»]
			D	139-206	[»]

SMR

P60879. Positions 7-83, 131-204.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:29066N.

IntAct

P60879. 7 interactions.

STRING

P60879.

PTM databases

PhosphoSite

P60879.

Proteomic databases

PRIDE

P60879.

Genome annotation databases

Ensembl

ENSMUST00000028727; ENSMUSP00000028727; ENSMUSG00000027273; Mus musculus. [Genome view]
ENSMUST00000110098; ENSMUSP00000105725; ENSMUSG00000027273; Mus musculus. [Genome view]

GeneID

20614.

KEGG

mmu:20614.

UCSC

uc008mop.1. mouse.

Organism-specific databases

CTD

20614.

MGI

MGI:98331. Snap25.

Phylogenomic databases

HOVERGEN

P60879.

OMA

LADEXSK.

Gene expression databases

ArrayExpress

P60879.

Bgee

P60879.

CleanEx

MM_SNAP25.

Genevestigator

P60879.

GermOnline

ENSMUSG00000027273. Mus musculus.

Family and domain databases

InterPro

IPR000928. SNAP-25.
IPR000727. T_SNARE.
[Graphical view]

Pfam

PF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]

SMART

SM00397. t_SNARE. 2 hits.
[Graphical view]

PROSITE

PS50192. T_SNARE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

298983.

SOURCE

Search...

Entry information

Entry name

SNP25_MOUSE

Accession

Primary (citable) accession number: P60879
Secondary accession number(s): A2AIC2 , A2AIC3, P13795, P36974, P70557, P70558, Q8IXK3, Q96FM2, Q9BR45

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	November 3, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)