Version 5.4
Bos taurus Protein: CAPZA2
Summary
InnateDB Protein IDBP-684471.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CAPZA2
Protein Name F-actin-capping protein subunit alpha-2
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000005324
InnateDB Gene IDBG-632806 (CAPZA2)
Protein Structure
UniProt Annotation
Function F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (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 14 interaction(s) predicted by orthology.
Predicted by orthology
Total 14 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003779 actin binding
GO:0005515 protein binding
Biological Process
GO:0030036 actin cytoskeleton organization
GO:0051016 barbed-end actin filament capping
GO:0051693 actin filament capping
Cellular Component
GO:0008290 F-actin capping protein complex
GO:0016020 membrane
GO:0030863 cortical cytoskeleton
GO:0070062 extracellular vesicular exosome
GO:0071203 WASH complex
Protein Structure and Domains
PDB ID
InterPro IPR002189 F-actin-capping protein subunit alpha
PFAM PF01267
PRINTS PR00191
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q5E997
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 493728
UniGene Bt.13391
RefSeq NP_001013016
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC102732 BT021023 DP000008
GenPept AAI02733 AAR16258 AAX09040

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