Carbonic anhydrase-related protein (CA8)
The protein contains 290 amino acids for an estimated molecular weight of 32973 Da.
Does not have a carbonic anhydrase catalytic activity. (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.
- 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.
- 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 |
|---|---|
| CMARQ3 |
The reference OMIM entry for this protein is 114815
Carbonic anhydrase viii; ca8
Ca viii
Carbonic anhydrase-related polypeptide; carp
Carbonic anhydrase-like sequence; cals
DESCRIPTION
The CA8 (CARP) gene encodes carbonic anhydrase VIII, which is part of a family of zinc metalloenzymes. Although CA8 has a central carbonic anhydrase motif, it lacks carbonic anhydrase activity (EC 4.2.1.1) due to absence of catalytic zinc coordinating residues (Kato, 1990). Nonetheless, the gene product was designated carbonic anhydrase VIII by several workers because it showed a clear sequence identity to other members of the carbonic anhydrase gene family from many sources. For background information on the CA family, see CA1 (114800).CLONING
Kato (1990) discovered a new member of the carbonic anhydrase gene family in a mouse brain cDNA library and demonstrated that it is expressed in the Purkinje cells of the cerebellum. The deduced 291-residue gene product was referred to as CA-related protein, or polypeptide (CARP). Skaggs et al. (1993) used PCR to amplify the human CARP gene from several cDNA libraries. They found a cDNA with a sequence that was 89.3% identical to mouse CARP at the nucleotide level and 97.9% at the amino acid level.MAPPING
Bergenhem et al. (1993) found that CARP cosegregated with human chromosome 8. Using human-mouse hybrid mapping and fluorescence in situ hybridization, Bergenhem et al. (1995) demonstrated that the CA8 gene is located on human chromosome 8q11-q12 between the centromere and the CA1/CA2/CA3 cluster at 8q22-q23. Kelly et al. (1994) mapped the mouse homolog (Car8) to chromosome 4 in a region syntenic to human chromosome 8.GENE FUNCTION
In mouse brain, Hirota et al. (2003) identified Carp as an ITPR1 (147265)-binding protein. Western blot and immunohistochemical studies showed that Carp colocalized and interacted with ITPR1 predominantly in the cytoplasm of cerebellar Purkinje cells. Lower levels of Carp expression were seen in other regions, including cerebrum, olfactory bulb, lung, liver, and adrenal gland. Deletion mutagenesis studies showed that residues 45 to 291 of Carp were essential for its association with the modulatory domain of ITPR1 (residues 1387 to 1647). Carp functioned as an inhibitor of IP3 binding to ITPR1 by reducing the affinity of the receptor for IP3.MOLECULAR GENETICS
By genomewide linkage analysis followed by candidate gene sequencing of a consanguineous Iraqi family with congenital cerebellar ataxia and mild mental retardation (CAMRQ3; 613227), Turkmen et al. (2009) identified a homozygous mutation in the CA8 gene (S100P; 186910.0001) on chromosome 8q12. By homozygosity mapping followed by exon enrichment and next-generation sequencing in 136 consanguineous families (over 90% Iranian and less than 10% Turkish or Arabic) segregating syndromic or nonsyndromic forms of autosomal recessive intellectual disability, Najmabadi et al. (2011) identified a missense mutation in the CA8 gene (114815.0002) as the cause of CAMRQ3 in a family (M107) in which first-cousin parents had 2 healthy and 4 affected children.ANIMAL MODEL
Kelly et al. (1994) reported absence of CA VIII mRNA in the cerebellum of the 'lurcher' mutant mouse with a neurologic defect. Sjoblom et al. (1996) constructed a mutant form of mouse Carp by introducing arg117-to-his and glu115-to-gln mutations and showed that this mutated protein binds zinc and catalyzes the hydration of carbon dioxide. The autosomal recessive 'waddles' (wdl) mouse shows ataxia and appendicular dystonia with frequent tail elevation and an abnormally elevated trunk d ... 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 114815 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed