Carbonic anhydrase III, muscle specific

Protein-coding gene in the species Homo sapiens

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| 14,928,572 bp[2]
End| 14,937,583 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| 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
BioGPS| |

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: 14.93 – 14.94 Mb
PubMed search| [3]| [4]
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[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000164879 \- Ensembl, May 2017
2. ^ a b c 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 Neuropathologica. 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". Clinical and Developmental Immunology. 2012: 354594. doi:10.1155/2012/354594. PMC 3461255. PMID 23049597.
8. ^ "Entrez Gene: CA3 carbonic anhydrase III, muscle specific".

## Further reading[edit]

* 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[edit]

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

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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

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Carbonic anhydrases

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

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