F-actin-capping protein subunit alpha-1 (CAPZA1)
The protein contains 286 amino acids for an estimated molecular weight of 32923 Da.
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. May play a role in the formation of epithelial cell junctions. (updated: Jan. 31, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs555597264 |
Biological Process
Actin cytoskeleton organization
Antigen processing and presentation of exogenous peptide antigen via MHC class II
Barbed-end actin filament capping
Blood coagulation
Cell junction assembly
Endoplasmic reticulum to Golgi vesicle-mediated transport
Innate immune response
Interleukin-12-mediated signaling pathway
Movement of cell or subcellular component
Protein complex assembly
Protein-containing complex assembly
The reference OMIM entry for this protein is 601580
Capping protein, alpha-1; capza1
Cap protein, actin, alpha-1 subunit; cappa1
CLONING
Barron-Casella et al. (1995) stated that CapZ was identified in chicken as a nonsevering, barbed-end actin-binding protein composed of alpha and beta subunits. In the chicken, 2 cDNAs were isolated for the alpha subunit. The alpha-1 and alpha-2 (CAPZA2; 601571) isoforms, which share 85% identity, are the products of 2 separate genes; 1 gene appears to be responsible for beta-subunit expression (see CAPZB; 601572). By capping the barbed end of actin filaments, CapZ regulates the growth of the actin filament at the barbed end.MAPPING
Cooper (1999) noted that the STS stSG3463 (GenBank GENBANK G43425), which has been mapped to chromosome 1, shares sequence identity with the corresponding region of a CAPZA1 cDNA. Hart et al. (1997) cloned 3 mouse homologs of CAPZA1, 2 of which are pseudogenes. They mapped the functional mouse Capza1 gene to chromosome 3 by interspecific backcross analysis. ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 601580 was added.
Sept. 16, 2015: Protein entry updated
Automatic update: model status changed