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P63040 (CPLX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complexin-1
Alternative name(s):
921-S
Complexin I
Short name=CPX I
Synaphin-2
Gene names
Name:Cplx1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length134 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Positively regulates a late step in synaptic vesicle exocytosis. Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. Also involved in glucose-induced secretion of insulin by pancreatic beta-cells. Essential for motor behavior. Ref.4 Ref.5

Subunit structure

Binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A By similarity.

Subcellular location

Cytoplasmcytosol. Note: Enriched at synaptic-releasing sites in mature neurons. Ref.1 Ref.4

Tissue specificity

Nervous system, and pancreatic islet cells. Present in many brain regions, including hippocampus and cerebellum. In the retina, present at conventional amacrine cell synapses (at protein level). Ref.1 Ref.4 Ref.6

Developmental stage

In the brain, expression starts at P6 and increases to reach a plateau at P20. Ref.6

Disruption phenotype

Mice have no obvious brain abnormality, but suffer from severe ataxia with dystonia starting from P7. Adult mice lacking Cplx1 are not capable of coordinated running or swimming and exhibit pronounced resting tremor. They also fail to habituate to confinement and have reduced exploration abilities in open field. Ref.5

Sequence similarities

Belongs to the complexin/synaphin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 134134Complexin-1
PRO_0000144871

Regions

Region48 – 7023Interaction with the SNARE complex By similarity
Coiled coil29 – 6436 Potential

Experimental info

Sequence conflict841A → V in AAH14803. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P63040 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: BA1B6F074923A3A4

FASTA13415,122
        10         20         30         40         50         60 
MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE 

        70         80         90        100        110        120 
VMRQGIRDKY GIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEPE EEDESILDTV 

       130 
IKYLPGPLQD MFKK 

« Hide

References

« Hide 'large scale' references
[1]"Identification of two highly homologous presynaptic proteins distinctly localized at the dendritic and somatic synapses."
Takahashi S., Yamamoto H., Matsuda Z., Ogawa M., Yagyu K., Taniguchi T., Miyata T., Kaba H., Higuchi T., Okutani F., Fujimoto S.
FEBS Lett. 368:455-460(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Strain: BALB/c.
Tissue: Brain.
[2]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Inner ear, Medulla oblongata and Visual cortex.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[4]"Complexin I regulates glucose-induced secretion in pancreatic beta-cells."
Abderrahmani A., Niederhauser G., Plaisance V., Roehrich M.-E., Lenain V., Coppola T., Regazzi R., Waeber G.
J. Cell Sci. 117:2239-2247(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
[5]"Profound ataxia in complexin I knockout mice masks a complex phenotype that includes exploratory and habituation deficits."
Glynn D., Drew C.J., Reim K., Brose N., Morton A.J.
Hum. Mol. Genet. 14:2369-2385(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"Structurally and functionally unique complexins at retinal ribbon synapses."
Reim K., Wegmeyer H., Brandstaetter J.H., Xue M., Rosenmund C., Dresbach T., Hofmann K., Brose N.
J. Cell Biol. 169:669-680(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38614 mRNA. Translation: BAA07605.1.
AK134820 mRNA. Translation: BAE22299.1.
AK158166 mRNA. Translation: BAE34390.1.
AK159026 mRNA. Translation: BAE34774.1.
BC014803 mRNA. Translation: AAH14803.1.
CCDSCCDS39206.1.
PIRS66294.
RefSeqNP_031782.3. NM_007756.3.
UniGeneMm.5195.

3D structure databases

ProteinModelPortalP63040.
SMRP63040. Positions 32-72.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP63040. 1 interaction.
MINTMINT-4091813.

PTM databases

PhosphoSiteP63040.

Proteomic databases

MaxQBP63040.
PaxDbP63040.
PRIDEP63040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046892; ENSMUSP00000038502; ENSMUSG00000033615.
GeneID12889.
KEGGmmu:12889.
UCSCuc008yof.2. mouse.

Organism-specific databases

CTD10815.
MGIMGI:104727. Cplx1.

Phylogenomic databases

eggNOGNOG85303.
GeneTreeENSGT00490000043416.
HOGENOMHOG000017716.
HOVERGENHBG062792.
InParanoidP63040.
KOK15294.
OMAKYARMEA.
OrthoDBEOG71G9XG.
PhylomeDBP63040.
TreeFamTF315172.

Gene expression databases

ArrayExpressP63040.
BgeeP63040.
CleanExMM_CPLX1.
GenevestigatorP63040.

Family and domain databases

InterProIPR008849. Synaphin.
[Graphical view]
PANTHERPTHR16705. PTHR16705. 1 hit.
PfamPF05835. Synaphin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282486.
PROP63040.
SOURCESearch...

Entry information

Entry nameCPLX1_MOUSE
AccessionPrimary (citable) accession number: P63040
Secondary accession number(s): O09057 expand/collapse secondary AC list , O09142, Q3UYB3, Q64276, Q91WJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot