CA14

From Wikipedia, the free encyclopedia

Carbonic anhydrase XIV

Identifiers

External IDs

OMIM: 604832 MGI: 1344341 HomoloGene: 69105

Gene ontology
Molecular Function:	• carbonate dehydratase activity • zinc ion binding • lyase activity • metal ion binding
Cellular Component:	• membrane • integral to membrane
Biological Process:	• one-carbon compound metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012113 (mRNA)
NP_036245 (protein)

NM_011797 (mRNA)
NP_035927 (protein)

Location

Chr 1: 148.5 - 148.5 Mb

Chr 3: 95.98 - 95.99 Mb

Pubmed search

[1]

[2]

Carbonic anhydrase XIV, also known as CA14, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: CA14 carbonic anhydrase XIV.

[edit] Further reading

Fujikawa-Adachi K, Nishimori I, Taguchi T, Onishi S (1999). "Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and mapping to chromosome 1.". Genomics 61 (1): 74–81. doi:10.1006/geno.1999.5938. PMID 10512682.
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. doi:10.1073/pnas.98.4.1918. PMID 11172051.
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. doi:10.1046/j.1523-1755.2002.00371.x. PMID 12028451.
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. doi:10.1073/pnas.242603899. PMID 12477932.
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. doi:10.1113/jphysiol.2002.035899. PMID 12611920.
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. doi:10.1101/gr.1293003. PMID 12975309.
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.
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. doi:10.1038/ng1285. PMID 14702039.
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. doi:10.1101/gr.2596504. PMID 15489334.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.