Carbonic anhydrase III, muscle specific

Carbonic anhydrase 3 is an enzyme that in humans is encoded by the CA3 gene.[5]

CA3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1Z93, 1Z97, 2HFW, 3UYN, 3UYQ
Identifiers
Aliases	CA3, CAIII, Car3, carbonic anhydrase 3
External IDs	OMIM: 114750 MGI: 88270 HomoloGene: 31298 GeneCards: CA3
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8q21.2 Start 85,373,436 bp[1] End 85,449,040 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3 A1|3 3.22 cM Start 14,863,512 bp[2] End 14,872,523 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • carbonate dehydratase activity • phosphatase activity • zinc ion binding • nickel cation binding • metal ion binding • lyase activity • Carbonic anhydrase Cellular component • cytoplasm • cytosol Biological process • bicarbonate transport • response to ethanol • response to oxidative stress • dephosphorylation • response to bacterium Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	761	12350
Ensembl	ENSG00000164879	ENSMUSG00000027559
UniProt	P07451	P16015
RefSeq (mRNA)	NM_005181	NM_007606
RefSeq (protein)	NP_005172	NP_031632
Location (UCSC)	Chr 8: 85.37 – 85.45 Mb	Chr 3: 14.86 – 14.87 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Carbonic anhydrase III (CAIII) is a member of a multigene family (at least six separate genes are known) that encode carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyze the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue-specific and present at high levels in skeletal muscle and much lower levels in cardiac and smooth muscle. CA3 is insufficient in muscles of Myasthenia Gravis patients.[6] A proportion of carriers of Duchenne muscle dystrophy have a higher CA3 level than normal. Autoantibodies to CA3 have been found to be significantly higher in patients with rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes.[7] The gene spans 10.3 kb and contains seven exons and six introns.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000164879 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027559 - 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. Shima K, Tashiro K, Hibi N, Tsukada Y, Hirai H (Jun 1983). "Carbonic anhydrase-III immunohistochemical localization in human skeletal muscle". Acta Neuropathol. 59 (3): 237–9. doi:10.1007/BF00703210. PMID 6221502. S2CID 523577.
6. Du AL, Ren HM, Lu CZ, Tu JL, Xu CF, Sun YA (Mar 2009). "Carbonic anhydrase III is insufficient in muscles of myasthenia gravis patients". Autoimmunity. 42 (3): 209–15. doi:10.1080/08916930802668610. PMID 19301202. S2CID 3135174.
7. Liu C, Wei Y, Wang J, Pi L, Huang J, Wang P (Sep 2012). "Carbonic anhydrases III and IV autoantibodies in rheumatoid arthritis, systemic lupus erythematosus, diabetes, hypertensive renal disease, and heart failure". Clin Dev Immunol. 2012: 354594. doi:10.1155/2012/354594. PMC 3461255. PMID 23049597.
8. "Entrez Gene: CA3 carbonic anhydrase III, muscle specific".

Further reading

• Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies". Annu. Rev. Biochem. 64: 375–401. doi:10.1146/annurev.bi.64.070195.002111. PMID 7574487.
• Carter N, Jeffery S, Shiels A, et al. (1980). "Characterization of human carbonic anhydrase III from skeletal muscle". Biochem. Genet. 17 (9–10): 837–54. doi:10.1007/BF00504307. PMID 120192. S2CID 8616344.
• Oikarinen A, Vuori J, Autio P, et al. (1993). "Comparison of muscle-derived serum carbonic anhydrase III and myoglobin in dermatological patients: effects of isotretinoin treatment". Acta Derm. Venereol. 72 (5): 352–4. PMID 1361281.
• Oguni M, Setogawa T, Tanaka O, et al. (1992). "Immunohistochemical study of carbonic anhydrase III in the extraocular muscles of human embryos". Acta Anat (Basel). 144 (4): 316–9. doi:10.1159/000147322. PMID 1414196.
• Vuori J, Rasi S, Takala T, Väänänen K (1992). "Dual-label time-resolved fluoroimmunoassay for simultaneous detection of myoglobin and carbonic anhydrase III in serum". Clin. Chem. 37 (12): 2087–92. doi:10.1093/clinchem/37.12.2087. PMID 1764784.
• Shamsutdinov NSh, Islamov RI, Valuillin VV (1991). "[Carbonic anhydrase III--a marker of the myoepithelial cells of human salivary glands]". Biulleten' eksperimental'noĭ biologii i meditsiny. 111 (3): 320–1. PMID 1905166.
• Nork TM, Wallow IH, Sramek SJ, et al. (1990). "Immunocytochemical study of an eye with proliferative vitreoretinopathy and retinal tacks". Retina (Philadelphia, Pa.). 10 (1): 78–85. doi:10.1097/00006982-199001010-00015. PMID 1971453. S2CID 7418386.
• Lloyd J, Brownson C, Tweedie S, et al. (1987). "Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues". Genes Dev. 1 (6): 594–602. doi:10.1101/gad.1.6.594. PMID 2824285.
• Lloyd JC, Isenberg H, Hopkinson DA, Edwards YH (1986). "Isolation of a cDNA clone for the human muscle specific carbonic anhydrase, CAIII". Ann. Hum. Genet. 49 (Pt 3): 241–51. doi:10.1111/j.1469-1809.1985.tb01698.x. PMID 3000276. S2CID 30747496.
• Lloyd J, McMillan S, Hopkinson D, Edwards YH (1986). "Nucleotide sequence and derived amino acid sequence of a cDNA encoding human muscle carbonic anhydrase". Gene. 41 (2–3): 233–9. doi:10.1016/0378-1119(86)90103-4. PMID 3086182.
• Wade R, Gunning P, Eddy R, et al. (1987). "Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely linked CAI and CAII genes". Proc. Natl. Acad. Sci. U.S.A. 83 (24): 9571–5. doi:10.1073/pnas.83.24.9571. PMC 387182. PMID 3099285.
• Väänänen HK, Autio-Harmainen H (1987). "Carbonic anhydrase III: a new histochemical marker for myoepithelial cells". J. Histochem. Cytochem. 35 (6): 683–6. doi:10.1177/35.6.3106467. PMID 3106467.
• Nakagawa Y, Perentes E, Rubinstein LJ (1987). "Non-specificity of anti-carbonic anhydrase C antibody as a marker in human neurooncology". J. Neuropathol. Exp. Neurol. 46 (4): 451–60. doi:10.1097/00005072-198707000-00004. PMID 3110380. S2CID 101554.
• Edwards YH, Lloyd J, Parkar M, Povey S (1988). "The gene for human muscle specific carbonic anhydrase (CAIII) is assigned to chromosome 8". Ann. Hum. Genet. 50 (Pt 1): 41–7. doi:10.1111/j.1469-1809.1986.tb01937.x. PMID 3122635. S2CID 22462255.
• Väänänen HK, Paloniemi M, Vuori J (1985). "Purification and localization of human carbonic anhydrase. III. Typing of skeletal muscle fibers in paraffin embedded sections". Histochemistry. 83 (3): 231–5. doi:10.1007/bf00953989. PMID 3930440. S2CID 20902453.
• Carter ND, Heath R, Jeffery S, Rodeck C (1982). "Fetal plasma carbonic anhydrase III in Duchenne dystrophy". Lancet. 1 (8262): 39–40. doi:10.1016/S0140-6736(82)92574-0. PMID 6119426. S2CID 32433390.
• Heath R, Schwartz MS, Brown IR, Carter ND (1983). "Carbonic anhydrase III in neuromuscular disorders". J. Neurol. Sci. 59 (3): 383–8. doi:10.1016/0022-510X(83)90023-0. PMID 6410007. S2CID 8548497.
• Wåhlstrand T, Wistrand PJ (1980). "Carbonic anhydrase C in the human renal medulla". Ups. J. Med. Sci. 85 (1): 7–17. doi:10.3109/03009738009179167. PMID 6770531.
• Jeffery S, Edwards Y, Carter N (1981). "Distribution of CAIII in fetal and adult human tissue". Biochem. Genet. 18 (9–10): 843–9. doi:10.1007/BF00500117. PMID 6784712. S2CID 13229349.

External links

• Overview of all the structural information available in the PDB for UniProt: P07451 (Carbonic anhydrase 3) at the PDBe-KB.