Version 5.4
Homo sapiens Protein: C2CD3
Summary
InnateDB Protein IDBP-64138.7
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol C2CD3
Protein Name C2 calcium-dependent domain containing 3
Synonyms OFD14;
Species Homo sapiens
Ensembl Protein ENSP00000323339
InnateDB Gene IDBG-64136 (C2CD3)
Protein Structure
UniProt Annotation
Function Component of the centrioles that acts as a positive regulator of centriole elongation (PubMed:24997988). Promotes assembly of centriolar distal appendage, a structure at the distal end of the mother centriole that acts as an anchor of the cilium, and is required for recruitment of centriolar distal appendages proteins CEP83, SCLT1, CEP89, FBF1 and CEP164. Not required for centriolar satellite integrity or RAB8 activation. Required for primary cilium formation (PubMed:23769972). Required for sonic hedgehog/SHH signaling and for proteolytic processing of GLI3. {ECO:0000269PubMed:23769972, ECO:0000269PubMed:24997988}.
Subcellular Localization Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269PubMed:23769972, ECO:0000269PubMed:24997988}. Note=Localizes to centrioles and procentrioles both in interphase and mitosis. Localizes to centriolar satellites, localization is dependent on PCM1 and dynein-mediated retrograde transport. Also localizes to the distal ends of the mother and daughter centrioles.
Disease Associations Note=Orofaciodigital syndrome (OFDS), a heterogeneous disease characterized by abnormalities in the oral cavity, face and digits, and associated phenotypic abnormalities that lead to the delineation of various subtypes. Patients with C2CD3-related OFDS present with severe microcephaly, cerebralmalformations including the molar tooth sign, and intellectual disability in addition to canonical OFDS features. The disease is caused by mutations affecting the gene represented in this entry (PubMed:24997988). {ECO:0000269PubMed:24997988}.
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
Biological Process
GO:0035058 nonmotile primary cilium assembly
Cellular Component
GO:0005813 centrosome
GO:0005814 centriole
GO:0042995 cell projection
Protein Structure and Domains
PDB ID
InterPro IPR000008 C2 domain
PFAM PF00168
PRINTS PR00360
PIRSF
SMART SM00239
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q4AC94
PhosphoSite PhosphoSite-Q4AC94
TrEMBL
UniProt Splice Variant
Entrez Gene 26005
UniGene Hs.694798
RefSeq NP_056346
HUGO HGNC:24564
OMIM 615944
CCDS CCDS31636
HPRD 16811
IMGT
EMBL AB231763 AB231764 AK091397 AK125894 AL080220 AL833903 AP000577 AP002392 AP003717 BC035599 BC110508
GenPept AAH35599 AAI10509 BAC03654 BAC86334 BAE17137 BAE46898 CAB45779 CAD38759

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