Version 5.4
Bos taurus Protein: CNN3
Summary
InnateDB Protein IDBP-688289.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CNN3
Protein Name Calponin-3
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000027115
InnateDB Gene IDBG-636372 (CNN3)
Protein Structure
UniProt Annotation
Function Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity). {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 7 interaction(s) predicted by orthology.
Predicted by orthology
Total 7 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003779 actin binding
GO:0005515 protein binding
GO:0005516 calmodulin binding
GO:0008017 microtubule binding
Biological Process
GO:0031032 actomyosin structure organization
Cellular Component
Protein Structure and Domains
PDB ID
InterPro IPR000557 Calponin repeat
IPR001715 Calponin homology domain
IPR001997 Calponin
IPR003096 Smooth muscle protein/calponin
PFAM PF00402
PF00307
PRINTS PR00889
PR00888
PIRSF
SMART SM00033
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q32L92
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 538975
UniGene Bt.5099
RefSeq NP_001033268
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC109697
GenPept AAI09698

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca