Skip Header

Contribute Send feedback
Read comments (?) or add your own

P36975 (SNP25_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptosomal-associated protein 25

Short name=SNAP-25
Alternative name(s):
Synaptosomal-associated 25 kDa protein
Gene names
Name:Snap25
ORF Names:CG40452
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion.

Subcellular location

Cell junctionsynapsesynaptosome By similarity. Note: Complexed with macromolecular elements of the nerve terminal.

Tissue specificity

Exclusively found in brain and ganglia.

Sequence similarities

Belongs to the SNAP-25 family.

Contains 2 t-SNARE coiled-coil homology domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P36975-1)

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 B (identifier: P36975-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-61: PADPSEEVAPQVPKTELEELQINAQGVADESLESTRRMLALCEESKEAGIRTLVALDDQG → R
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Synaptosomal-associated protein 25
PRO_0000213594

Regions

Domain26 – 8863t-SNARE coiled-coil homology 1
Domain148 – 21063t-SNARE coiled-coil homology 2
Compositional bias91 – 999Cys-rich

Natural variations

Alternative sequence2 – 6160PADPS…LDDQG → R in isoform B.
VSP_022126

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: BDC90649A1AF3AC8

FASTA21223,685
        10         20         30         40         50         60 
MPADPSEEVA PQVPKTELEE LQINAQGVAD ESLESTRRML ALCEESKEAG IRTLVALDDQ 

        70         80         90        100        110        120 
GEQLDRIEEG MDQINADMRE AEKNLSGMEK CCGICVLPCN KSQSFKEDDG TWKGNDDGKV 

       130        140        150        160        170        180 
VNNQPQRVMD DRNGMMAQAG YIGRITNDAR EDEMEENMGQ VNTMIGNLRN MALDMGSELE 

       190        200        210 
NQNRQIDRIN RKGESNEARI AVANQRAHQL LK 

« Hide

Isoform B [UniParc].

Checksum: 3C95F54CCD764161
Show »

FASTA15317,380

References

« Hide 'large scale' references
[1]"Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones."
Risinger C., Blomqvist A.G., Lundell I., Lambertsson A., Nassel D., Pieribone V.A., Brodin L., Larhammar D.
J. Biol. Chem. 268:24408-24414(1993) [PubMed: 8226991] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Head.
[2]"Complex gene organization of synaptic protein SNAP-25 in Drosophila melanogaster."
Risinger C., Deitcher D.L., Lundell I., Schwarz T.L., Larhammar D.
Gene 194:169-177(1997) [PubMed: 9272858] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., Karpen G.H.
Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002) [PubMed: 12537574] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[6]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L22021 mRNA. Translation: AAA16059.1.
U81153 expand/collapse EMBL AC list , U81147, U81148, U81149, U81150, U81151, U81152 Genomic DNA. Translation: AAB39757.1.
AE014296 Genomic DNA. Translation: EAA46071.2.
AE014296 Genomic DNA. Translation: EAL24571.1.
BT023789 mRNA. Translation: AAZ41798.1.
RefSeqNP_001036641.1. NM_001043176.1.
UniGeneDm.33412.

3D structure databases

ProteinModelPortalP36975.
SMRP36975. Positions 17-85, 149-207.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-23273N.
MINTMINT-1714865.
STRINGP36975.

Proteomic databases

PRIDEP36975.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0111143; FBpp0110435; FBgn0011288.
GeneID3355084.
KEGGdme:Dmel_CG40452.

Organism-specific databases

CTD6616.
FlyBaseFBgn0011288. Snap25.

Phylogenomic databases

eggNOGinNOG07049.
GeneTreeEMGT00050000012066.
InParanoidP36975.
OMAESADAYQ.
OrthoDBEOG45HQDD.
PhylomeDBP36975.

Gene expression databases

BgeeP36975.

Family and domain databases

InterProIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
KOK08508.
PfamPF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]
SMARTSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEPS50192. T_SNARE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio850492.

Entry information

Entry nameSNP25_DROME
AccessionPrimary (citable) accession number: P36975
Secondary accession number(s): Q5LJU6, Q7PLV2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families