Biology:Carbonic anhydrase 14
 Generic protein structure example |
Carbonic anhydrase 14 is an enzyme that in humans is encoded by the CA14 gene.[1][2]
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.[2]
In melanocytic cells CA14 gene expression may be regulated by MITF.[3]
References
- ↑ "Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and mapping to chromosome 1". Genomics 61 (1): 74–81. Nov 1999. doi:10.1006/geno.1999.5938. PMID 10512682.
- ↑ 2.0 2.1 "Entrez Gene: CA14 carbonic anhydrase XIV". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23632.
- ↑ "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. 2008. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
External links
- Human CA14 genome location and CA14 gene details page in the UCSC Genome Browser.
Further reading
- "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. 2001. doi:10.1073/pnas.98.4.1918. PMID 11172051. Bibcode: 2001PNAS...98.1918P.
- "Carbonic anhydrase XIV: luminal expression suggests key role in renal acidification.". Kidney Int. 61 (6): 2111–8. 2002. doi:10.1046/j.1523-1755.2002.00371.x. PMID 12028451.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932.
- "Human skeletal muscle and erythrocyte proteins involved in acid-base homeostasis: adaptations to chronic hypoxia.". J. Physiol. 548 (Pt 2): 639–48. 2003. doi:10.1113/jphysiol.2002.035899. PMID 12611920.
- "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. 2003. doi:10.1101/gr.1293003. PMID 12975309.
- "Gene expression for carbonic anhydrase isoenzymes in human nasal mucosa.". Chem. Senses 28 (7): 621–9. 2004. doi:10.1093/chemse/bjg054. PMID 14578124.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. 2006. doi:10.1038/nature04727. PMID 16710414. Bibcode: 2006Natur.441..315G.
 |
