Carbonic anhydrase 14

CA14
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4LU3, 5CJF
Identifiers
Aliases	CA14 , CAXiV, carbonic anhydrase 14
External IDs	OMIM: 604832; MGI: 1344341; HomoloGene: 69105; GeneCards: CA14; OMA:CA14 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1q21.2 Start 150,257,251 bp [1] End 150,265,078 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3|3 F2.1 Start 95,805,080 bp [2] End 95,812,003 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in retinal pigment epithelium substantia nigra vastus lateralis muscle corpus callosum embryo ganglionic eminence putamen prefrontal cortex amygdala left ventricle Top expressed in retinal pigment epithelium interventricular septum stria vascularis right ventricle iris utricle primitive streak ciliary body kidney left lobe of liver More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding lyase activity carbonate dehydratase activity zinc ion binding carbonic anhydrase Cellular component plasma membrane membrane integral component of membrane Biological process bicarbonate transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23632 23831 Ensembl ENSG00000118298 ENSMUSG00000038526 UniProt Q9ULX7 Q9WVT6 RefSeq (mRNA) NM_012113 NM_011797 NM_001355750 NM_001355751 NM_001355752 RefSeq (protein) NP_036245 NP_035927 NP_001342679 NP_001342680 NP_001342681 Location (UCSC) Chr 1: 150.26 – 150.27 Mb Chr 3: 95.81 – 95.81 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Carbonic anhydrase 14 is an enzyme that in humans is encoded by the CA14 gene. ^{[5] [6]}

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. ^[6]

In melanocytic cells CA14 gene expression may be regulated by MITF. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000118298 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000038526 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. doi:10.1006/geno.1999.5938. PMID   10512682.
6. "Entrez Gene: CA14 carbonic anhydrase XIV".
7. 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. 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

• 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. Bibcode:2001PNAS...98.1918P. doi: 10.1073/pnas.98.4.1918 . PMC   29357 . 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . 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. 548 (Pt 2): 639–48. doi:10.1113/jphysiol.2002.035899. PMC   2342856 . 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. PMC   403697 . 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. doi: 10.1093/chemse/bjg054 . 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. PMC   528928 . 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. Bibcode:2006Natur.441..315G. doi: 10.1038/nature04727 . PMID   16710414.