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Q8R1B5 (CPLX3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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-3
Alternative name(s):
Complexin III
Short name=CPX III
Gene names
Name:Cplx3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Positively regulates a late step in synaptic vesicle exocytosis. Ref.1

Subunit structure

Binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A. Ref.1

Subcellular location

Membrane; Lipid-anchor. Cell junctionsynapse. Cell membrane; Lipid-anchor. Note: Enriched at the synaptic terminal. Ref.1

Tissue specificity

Present in many brain regions, including hippocampus and cerebellum. In the retina, present both at conventional amacrine cell synapses and at photoreceptor ribbon synapses (at protein level). Ref.1

Developmental stage

In the brain, expression starts at P6 and increases to reach a plateau at P20. Ref.1

Post-translational modification

Farnesylation mediates presynaptic targeting.

Sequence similarities

Belongs to the complexin/synaphin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 155155Complexin-3
PRO_0000239273
Propeptide156 – 1583Removed in mature form
PRO_0000240234

Regions

Coiled coil39 – 7436 Potential

Amino acid modifications

Modified residue1551Cysteine methyl ester
Lipidation1551S-farnesyl cysteine Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8R1B5 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E452E829DC019A70

FASTA15817,586
        10         20         30         40         50         60 
MAFMVKSMVG GQLKNLTGSL GGGEDKGDGD KSAAEAQGMS REEYEEYQKQ LVEEKMERDA 

        70         80         90        100        110        120 
QFTQRKAERA TLRSHFRDKY RLPKNETDES QIQLAGGDVE LPRELAKMIE EDTEEEEDKA 

       130        140        150 
SVLGQLASLP GLDLSSLKDK AQTTLGDLKQ SAEKCHIM 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, ISOPRENYLATION AT CYS-155, DEVELOPMENTAL STAGE, 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: Retina.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY264290 mRNA. Translation: AAP22133.1.
AK044211 mRNA. Translation: BAC31818.1.
BC016632 mRNA. Translation: AAH16632.1.
BC024854 mRNA. Translation: AAH24854.1.
BC033343 mRNA. Translation: AAH33343.1.
RefSeqNP_666335.1. NM_146223.3.
UniGeneMm.35242.

3D structure databases

ProteinModelPortalQ8R1B5.
SMRQ8R1B5. Positions 44-82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000046748.

Proteomic databases

PaxDbQ8R1B5.
PRIDEQ8R1B5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045068; ENSMUSP00000046748; ENSMUSG00000039714.
GeneID235415.
KEGGmmu:235415.
UCSCuc009pvg.2. mouse.

Organism-specific databases

CTD594855.
MGIMGI:2384571. Cplx3.

Phylogenomic databases

eggNOGNOG38928.
GeneTreeENSGT00490000043378.
HOGENOMHOG000111927.
HOVERGENHBG060856.
InParanoidQ8R1B5.
KOK15295.
OMATENCSLM.
OrthoDBEOG70CR8H.
PhylomeDBQ8R1B5.
TreeFamTF331867.

Gene expression databases

BgeeQ8R1B5.
CleanExMM_CPLX3.
GenevestigatorQ8R1B5.

Family and domain databases

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

Other

NextBio382652.
PROQ8R1B5.
SOURCESearch...

Entry information

Entry nameCPLX3_MOUSE
AccessionPrimary (citable) accession number: Q8R1B5
Secondary accession number(s): Q96AW7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 82 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