Carbonic anhydrase 14

CA14

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
4LU3, 5CJF

Identifiers

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]
Band	1q21.2	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]
Band	3\|3 F2.1	End	95,812,003 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

retinal pigment epithelium

C1 segment

substantia nigra

Epithelium of choroid plexus

vastus lateralis muscle

ventricular zone

corpus callosum

embryo

apex of heart

Skeletal muscle tissue of rectus abdominis

Top expressed in

retinal pigment epithelium

choroid plexus of fourth ventricle

Epithelium of choroid plexus

right kidney

epithelium of lens

epiblast

interventricular septum

stria vascularis

cardiac muscle tissue of left ventricle

muscle of thigh

More reference expression data


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

Species

Human

Mouse


23632


23831


ENSG00000118298


ENSMUSG00000038526


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]

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000118298 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000038526 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "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. 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.

v t e Carbonic anhydrases
CA1 CA2 CA3 CA4 CA5A CA5B CA6 CA7 CA8 CA9 CA10 CA11 CA12 CA13 CA14

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