CA14
| CA14 | |||||||||||||||||
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| Identifiers | |||||||||||||||||
| Aliases | CA14, CAXiV, carbonic anhydrase 14 | ||||||||||||||||
| External IDs | MGI: 1344341 HomoloGene: 69105 GeneCards: CA14 | ||||||||||||||||
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| Species | Human | Mouse | |||||||||||||||
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| Location (UCSC) | Chr 1: 150.26 – 150.27 Mb | Chr 3: 95.9 – 95.9 Mb | |||||||||||||||
| PubMed search | [1] | [2] | |||||||||||||||
| Wikidata | |||||||||||||||||
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Carbonic anhydrase 14 is an enzyme that in humans is encoded by the CA14 gene.[3][4]
Carbonic anhydrases (CAs) 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. CA XIV is predicted to be a type I membrane protein and shares highest sequence similarity with the other transmembrane CA isoform, CA XII; however, they have different patterns of tissue-specific expression and thus may play different physiologic roles.[4]
In melanocytic cells CA14 gene expression may be regulated by MITF.[5]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Fujikawa-Adachi K, Nishimori I, Taguchi T, Onishi S (Nov 1999). "Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and mapping to chromosome 1". Genomics. 61 (1): 74–81. PMID 10512682. doi:10.1006/geno.1999.5938.
- 1 2 "Entrez Gene: CA14 carbonic anhydrase XIV".
- ↑ Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. PMID 19067971. doi:10.1111/j.1755-148X.2008.00505.x.
External links
- Human CA14 genome location and CA14 gene details page in the UCSC Genome Browser.
Further reading
- Parkkila S, Parkkila AK, Rajaniemi H, et al. (2001). "Expression of membrane-associated carbonic anhydrase XIV on neurons and axons in mouse and human brain.". Proc. Natl. Acad. Sci. U.S.A. 98 (4): 1918–23. PMC 29357
. PMID 11172051. doi:10.1073/pnas.98.4.1918. - Kaunisto K, Parkkila S, Rajaniemi H, et al. (2002). "Carbonic anhydrase XIV: luminal expression suggests key role in renal acidification.". Kidney Int. 61 (6): 2111–8. PMID 12028451. doi:10.1046/j.1523-1755.2002.00371.x.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
- Juel C, Lundby C, Sander M, et al. (2003). "Human skeletal muscle and erythrocyte proteins involved in acid-base homeostasis: adaptations to chronic hypoxia.". J. Physiol. (Lond.). 548 (Pt 2): 639–48. PMC 2342856 . PMID 12611920. doi:10.1113/jphysiol.2002.035899.
- Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. PMC 403697 . PMID 12975309. doi:10.1101/gr.1293003.
- Tarun AS, Bryant B, Zhai W, et al. (2004). "Gene expression for carbonic anhydrase isoenzymes in human nasal mucosa.". Chem. Senses. 28 (7): 621–9. PMID 14578124. doi:10.1093/chemse/bjg054.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. PMID 14702039. doi:10.1038/ng1285.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
- Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature. 441 (7091): 315–21. PMID 16710414. doi:10.1038/nature04727.
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