Carbonic anhydrase 7

Carbonic anhydrase VII
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3MDZ​, 3ML5​
Identifiers
Symbols	CA7 ; CAVII
External IDs	OMIM: 114770 MGI: 103100 HomoloGene: 55875 ChEMBL: 2326 GeneCards: CA7 Gene
EC number	4.2.1.1
Gene ontology Molecular function • carbonate dehydratase activity • zinc ion binding Cellular component • cytosol Biological process • positive regulation of defense response to virus by host • one-carbon metabolic process • bicarbonate transport • positive regulation of synaptic transmission, GABAergic • positive regulation of cellular pH reduction • small molecule metabolic process • activation of mitophagy in response to mitochondrial depolarization • regulation of chloride transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	766	12354
Ensembl	ENSG00000168748	ENSMUSG00000031883
UniProt	P43166	Q9ERQ8
RefSeq (mRNA)	NM_001014435	NM_001301164
RefSeq (protein)	NP_001014435	NP_001288093
Location (UCSC)	Chr 16: 66.84 – 66.85 Mb	Chr 8: 104.53 – 104.55 Mb
PubMed search

Carbonic anhydrase 7 (CA7) is an enzyme that in humans is encoded by the CA7 gene.^[1][2]

Function

Carbonic anhydrases are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. The cytosolic protein encoded by this gene is predominantly expressed in the salivary glands. Alternative splicing in the coding region results in multiple transcript variants encoding different isoforms.^[2]

References

1. Montgomery JC, Venta PJ, Eddy RL, Fukushima YS, Shows TB, Tashian RE (Dec 1991). "Characterization of the human gene for a newly discovered carbonic anhydrase, CA VII, and its localization to chromosome 16". Genomics 11 (4): 835–48. doi:10.1016/0888-7543(91)90006-Z. PMID 1783392.
2. "Entrez Gene: CA7 carbonic anhydrase VII".

Further reading

• Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies". Annual Review of Biochemistry 64: 375–401. doi:10.1146/annurev.bi.64.070195.002111. PMID 7574487.
• Breton S (Jul 2001). "The cellular physiology of carbonic anhydrases". Jop 2 (4 Suppl): 159–64. PMID 11875253.
• Rivera C, Voipio J, Kaila K (Jan 2005). "Two developmental switches in GABAergic signalling: the K+-Cl- cotransporter KCC2 and carbonic anhydrase CAVII". The Journal of Physiology 562 (Pt 1): 27–36. doi:10.1113/jphysiol.2004.077495. PMC 1665491. PMID 15528236.
• Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD (Sep 1999). "Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q". Genomics 60 (3): 295–308. doi:10.1006/geno.1999.5927. PMID 10493829.
• Chagnon P, Michaud J, Mitchell G, Mercier J, Marion JF, Drouin E, Rasquin-Weber A, Hudson TJ, Richter A (Dec 2002). "A missense mutation (R565W) in cirhin (FLJ14728) in North American Indian childhood cirrhosis". American Journal of Human Genetics 71 (6): 1443–9. doi:10.1086/344580. PMC 378590. PMID 12417987.
• Vullo D, Voipio J, Innocenti A, Rivera C, Ranki H, Scozzafava A, Kaila K, Supuran CT (Feb 2005). "Carbonic anhydrase inhibitors. Inhibition of the human cytosolic isozyme VII with aromatic and heterocyclic sulfonamides". Bioorganic & Medicinal Chemistry Letters 15 (4): 971–6. doi:10.1016/j.bmcl.2004.12.052. PMID 15686895.