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; OMA:CA3 - orthologs
Gene location (Human)
Chr.	Chromosome 8 (human)
End	85,449,040 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	14,937,583 bp
RNA expression pattern
	Top expressed in
	Skeletal muscle tissue of rectus abdominis; ; muscle of thigh; ; vastus lateralis muscle; ; biceps brachii; ; Skeletal muscle tissue of biceps brachii; ; thoracic diaphragm; ; gastrocnemius muscle; ; glutes; ; triceps brachii muscle; ; body of tongue;
	Top expressed in
	intercostal muscle; ; subcutaneous adipose tissue; ; white adipose tissue; ; tunica adventitia of aorta; ; vestibular sensory epithelium; ; ankle; ; body of femur; ; brown adipose tissue; ; sternocleidomastoid muscle; ; vastus lateralis muscle;
	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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000164879 – Ensembl, May 2017
^ ^a ^b ^c 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".

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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.
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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.