Carbonic anhydrase III, muscle specific

CA3

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1Z93, 1Z97, 2HFW, 3UYN, 3UYQ

Identifiers

Aliases

CA3, CAIII, Car3, carbonic anhydrase 3

External IDs

MGI: 88270 HomoloGene: 31298 GeneCards: CA3

Gene ontology
Molecular function	• carbonate dehydratase activity • phosphatase activity • zinc ion binding • nickel cation binding • metal ion binding • lyase activity
Cellular component	• cytoplasm • cytosol
Biological process	• bicarbonate transport • response to ethanol • one-carbon metabolic process • response to oxidative stress • dephosphorylation
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


761


12350

Ensembl


ENSG00000164879


ENSMUSG00000027559

UniProt


P07451


P16015

RefSeq (mRNA)


NM_005181


NM_007606

RefSeq (protein)


NP_005172.1


NP_031632.2

Location (UCSC)

Chr 8: 85.37 – 85.45 Mb

Chr 3: 14.86 – 14.87 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

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

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.^[4] 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.^[5] The gene spans 10.3 kb and contains seven exons and six introns.^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
↑ 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.
↑ 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.
↑ "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.". Biochem. Genet. 17 (9–10): 837–54. doi:10.1007/BF00504307. PMID 120192.
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. 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.
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.
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.
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.
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.
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.
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.
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.

PDB gallery

1flj: CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III

1z93: Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.

1z97: Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer.

2hfw: Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III

2hfx: Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III

2hfy: Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III

Carbonic anhydrases

CA1 CA2 CA3 CA4 CA5A CA5B CA6 CA7 CA8 CA9 CA10 CA11 CA12 CA13 CA14

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Carbonic anhydrase III, muscle specific

References

Further reading