Carbonic anhydrase 1 (CA1)
The protein contains 261 amino acids for an estimated molecular weight of 28870 Da.
Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea. (updated: April 1, 2015)
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.
- 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.
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 |
|---|---|
| variant Michigan-1 | |
| dbSNP:rs7821248 | |
| Guam |
No binding partner found
Biological Process
Bicarbonate transport
Interleukin-12-mediated signaling pathway
One-carbon metabolic process
Small molecule metabolic process
Molecular Function
Arylesterase activity
Carbonate dehydratase activity
Hydro-lyase activity
Zinc ion binding
The reference OMIM entry for this protein is 114800
Carbonic anhydrase i; ca1
Ca i
Carbonic anhydrase a
Carbonic anhydrase b, formerly
DESCRIPTION
Carbonic anhydrases (CAs; carbonate dehydratase; carbonate hydrolyase; EC 4.2.1.1) form a large family of genes encoding zinc metalloenzymes of great physiologic importance. As catalysts of the reversible hydration of carbon dioxide, these enzymes participate in a variety of biologic processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid (Dodgson et al., 1991). CAs are encoded by members of 3 independent CA gene families, i.e., alpha-CA, beta-CA, and gamma-CA (Hewett-Emmett and Tashian, 1996). Genes in the alpha-carbonic anhydrase family encode either active carbonic anhydrase isozymes or 'acatalytic' (i.e., devoid of CO2 hydration activity) carbonic anhydrase-related proteins. Alpha-carbonic anhydrases show extensive diversity in tissue distribution and in their putative or established biologic functions. Some of the alpha-CAs are expressed in almost all tissues (e.g., CA II, 611492), whereas some show a more restricted expression (e.g., CA VI (114780) in salivary glands). In cells, they may reside in cytoplasm, in mitochondria, or in secretory granules, or associate with membranes.CLONING
Erythrocyte carbonic anhydrase has 2 isoenzymes with different amino acid sequences and specific activities. B and C were the original designations for these 2 major forms which later were called CA I (or A) and CA II (or B; 611492), respectively. Tashian (1969) reviewed the biochemical genetics of the 2 forms of red cell carbonic anhydrase, which are under the control of separate autosomal loci. Andersson et al. (1972) stated that CA I is the major form of the enzyme in human red cells. They found that the protein consists of 260 amino acids. Barlow et al. (1987) cloned human carbonic anhydrase I cDNA.MAPPING
CA I and CA II are linked in the rodent genus Cavia (Carter, 1972), closely linked in an Old World monkey, Macaca nemestrina (DeSimone et al., 1973), and tightly linked in the mouse (Eicher et al., 1976). Using a cDNA clone of the CA1 gene in the study of human-rodent hybrids, Butterworth et al. (1985) and Edwards et al. (1986) assigned the CA1 gene to chromosome 8, which carries a cluster of CA genes. By somatic cell genetic techniques and in situ hybridization, Davis et al. (1986, 1987) mapped the CA1 and CA3 (114750) genes to 8q13-q22. By pulsed field gel electrophoresis, Lowe et al. (1991) determined that the order of the genes is CA2, CA3, CA1. CA2 and CA3 are separated by 20 kb and are transcribed in the same direction, away from CA1. CA1 is separated from CA3 by over 80 kb and is transcribed in the opposite direction to CA2 and CA3. Lowe et al. (1991) concluded that the arrangement of the genes is consistent with proposals that the duplication event that gave rise to CA1 predated the duplication that gave rise to CA2 and CA3. The order of the 3 genes differs from that suggested for the mouse based on recombination frequency.GENE STRUCTURE
Tashian (1992) reviewed the gene organization and evolutionary relationships of the carbonic anhydrases. See also Hewett-Emmett and Tashian (1996).GENE FUNCTION
Gao et al. (2007) performed proteomic analysis on vitreous fluid samples and found that the CA1 concentration from patients with diabetic retinopathy (see 603933) was 15.3 and 8.2 times higher than that from nondiabetic patients and diabetics with no diabetic retino ... More on the omim web site
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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 114800 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed