Carbonic anhydrase III, muscle specific

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]
End	85,449,040 bp[1]
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)[2]
End	14,937,583 bp[2]
RNA expression pattern
	Top expressed in
	vastus lateralis muscle; ; biceps brachii; ; thoracic diaphragm; ; gastrocnemius muscle; ; triceps brachii muscle; ; body of tongue; ; deltoid muscle; ; tibialis anterior muscle; ; right lung; ; gastric mucosa;
	Top expressed in
	intercostal muscle; ; subcutaneous adipose tissue; ; white adipose tissue; ; ankle; ; body of femur; ; brown adipose tissue; ; sternocleidomastoid muscle; ; vastus lateralis muscle; ; triceps brachii muscle; ; left lobe of liver;
	More reference expression data
	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
	761
	12350
	ENSG00000164879
	ENSMUSG00000027559
	P07451
	P16015
	NM_005181
	NM_007606
	NP_005172
	NP_031632
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

GRCh38: Ensembl release 89: ENSG00000164879 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000027559 - 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.
Shima K, Tashiro K, Hibi N, Tsukada Y, Hirai H (Jun 1983). "Carbonic anhydrase-III immunohistochemical localization in human skeletal muscle". Acta Neuropathologica. 59 (3): 237–9. doi:10.1007/BF00703210. PMID 6221502. S2CID 523577.
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.
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". Clinical and Developmental Immunology. 2012: 354594. doi:10.1155/2012/354594. PMC 3461255. PMID 23049597.
"Entrez Gene: CA3 carbonic anhydrase III, muscle specific".

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". Biochemical Genetics. 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 Dermato-Venereologica. 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 Anatomica. 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". Clinical Chemistry. 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. 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 & Development. 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". Annals of Human Genetics. 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". Proceedings of the National Academy of Sciences. 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". Journal of Histochemistry & Cytochemistry. 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". Journal of Neuropathology and Experimental Neurology. 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". Annals of Human Genetics. 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". Journal of the Neurological Sciences. 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". Upsala Journal of Medical Sciences. 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". Biochemical Genetics. 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000164879 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid6221502-5] Shima K, Tashiro K, Hibi N, Tsukada Y, Hirai H (Jun 1983). "Carbonic anhydrase-III immunohistochemical localization in human skeletal muscle". Acta Neuropathologica. 59 (3): 237–9. doi:10.1007/BF00703210. PMID 6221502. S2CID 523577.

[pmid19301202-6] 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.

[pmid23049597-7] 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". Clinical and Developmental Immunology. 2012: 354594. doi:10.1155/2012/354594. PMC 3461255. PMID 23049597.

[entrez-8] "Entrez Gene: CA3 carbonic anhydrase III, muscle specific".

Carbonic anhydrase III, muscle specific

References

Further reading

External links