- CA14
Carbonic anhydrase XIV, also known as CA14, is a human
gene .cite web | title = Entrez Gene: CA14 carbonic anhydrase XIV| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23632| accessdate = ]PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: CA14 carbonic anhydrase XIV| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23632| accessdate = ]References
Further reading
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citations =
*cite journal | author=Fujikawa-Adachi K, Nishimori I, Taguchi T, Onishi S |title=Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and mapping to chromosome 1. |journal=Genomics |volume=61 |issue= 1 |pages= 74–81 |year= 1999 |pmid= 10512682 |doi= 10.1006/geno.1999.5938
*cite journal | author=Parkkila S, Parkkila AK, Rajaniemi H, "et al." |title=Expression of membrane-associated carbonic anhydrase XIV on neurons and axons in mouse and human brain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 4 |pages= 1918–23 |year= 2001 |pmid= 11172051 |doi= 10.1073/pnas.98.4.1918
*cite journal | author=Kaunisto K, Parkkila S, Rajaniemi H, "et al." |title=Carbonic anhydrase XIV: luminal expression suggests key role in renal acidification. |journal=Kidney Int. |volume=61 |issue= 6 |pages= 2111–8 |year= 2002 |pmid= 12028451 |doi= 10.1046/j.1523-1755.2002.00371.x
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Juel C, Lundby C, Sander M, "et al." |title=Human skeletal muscle and erythrocyte proteins involved in acid-base homeostasis: adaptations to chronic hypoxia. |journal=J. Physiol. (Lond.) |volume=548 |issue= Pt 2 |pages= 639–48 |year= 2003 |pmid= 12611920 |doi= 10.1113/jphysiol.2002.035899
*cite journal | author=Clark HF, Gurney AL, Abaya E, "et al." |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003
*cite journal | author=Tarun AS, Bryant B, Zhai W, "et al." |title=Gene expression for carbonic anhydrase isoenzymes in human nasal mucosa. |journal=Chem. Senses |volume=28 |issue= 7 |pages= 621–9 |year= 2004 |pmid= 14578124 |doi=
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Gregory SG, Barlow KF, McLay KE, "et al." |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727PBB_Controls
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