CA4

From Wikipedia, the free encyclopedia

Carbonic anhydrase IV

PDB rendering based on 1znc.

Available structures: 1znc

Identifiers

Symbol(s)

CA4; CAIV; Car4; RP17

External IDs

OMIM: 114760 MGI: 1096574 HomoloGene: 20183

Gene ontology
Molecular Function:	• carbonate dehydratase activity • zinc ion binding • lyase activity • metal ion binding • GPI anchor binding
Cellular Component:	• membrane fraction • membrane
Biological Process:	• one-carbon compound metabolic process • visual perception • response to stimulus

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000717 (mRNA)
NP_000708 (protein)

NM_007607 (mRNA)
NP_031633 (protein)

Location

Chr 17: 55.58 - 55.59 Mb

Chr 11: 84.77 - 84.78 Mb

Pubmed search

[1]

[2]

Carbonic anhydrase IV, also known as CA4, is a human gene.^[1]

Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. CA IV is a glycosylphosphatidyl-inositol-anchored membrane isozyme expressed on the luminal surfaces of pulmonary (and certain other) capillaries and of proximal renal tubules. Its exact function is not known, however, it may have a role in inherited renal abnormalities of bicarbonate transport.^[1]

[edit] References

^ ^a ^b Entrez Gene: CA4 carbonic anhydrase IV.

[edit] Further reading

Okuyama T, Sato S, Zhu XL, et al. (1992). "Human carbonic anhydrase IV: cDNA cloning, sequence comparison, and expression in COS cell membranes.". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1315–9. PMID 1311094.
Hageman GS, Zhu XL, Waheed A, Sly WS (1991). "Localization of carbonic anhydrase IV in a specific capillary bed of the human eye.". Proc. Natl. Acad. Sci. U.S.A. 88 (7): 2716–20. PMID 1901414.
Zhu XL, Sly WS (1990). "Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney.". J. Biol. Chem. 265 (15): 8795–801. PMID 2111324.
Carter ND, Fryer A, Grant AG, et al. (1990). "Membrane specific carbonic anhydrase (CAIV) expression in human tissues.". Biochim. Biophys. Acta 1026 (1): 113–6. PMID 2116168.
Whitney PL, Briggle TV (1982). "Membrane-associated carbonic anhydrase purified from bovine lung.". J. Biol. Chem. 257 (20): 12056–9. PMID 6811592.
Bardien S, Ebenezer N, Greenberg J, et al. (1995). "An eighth locus for autosomal dominant retinitis pigmentosa is linked to chromosome 17q.". Hum. Mol. Genet. 4 (8): 1459–62. PMID 7581389.
Okuyama T, Waheed A, Kusumoto W, et al. (1995). "Carbonic anhydrase IV: role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activity.". Arch. Biochem. Biophys. 320 (2): 315–22. PMID 7625839.
Mahieu I, Benjamin A, Stephens R, et al. (1995). "Characterization of membrane bound carbonic anhydrase IV (CA IV) located on the external surface of lung pulmonary endothelial cells.". Biochem. Soc. Trans. 23 (2): 320S. PMID 7672351.
Sender S, Gros G, Waheed A, et al. (1994). "Immunohistochemical localization of carbonic anhydrase IV in capillaries of rat and human skeletal muscle.". J. Histochem. Cytochem. 42 (9): 1229–36. PMID 8064130.
Okuyama T, Batanian JR, Sly WS (1993). "Genomic organization and localization of gene for human carbonic anhydrase IV to chromosome 17q.". Genomics 16 (3): 678–84. doi:10.1006/geno.1993.1247. PMID 8325641.
Fleming RE, Parkkila S, Parkkila AK, et al. (1996). "Carbonic anhydrase IV expression in rat and human gastrointestinal tract regional, cellular, and subcellular localization.". J. Clin. Invest. 96 (6): 2907–13. PMID 8675662.
Waheed A, Okuyama T, Heyduk T, Sly WS (1996). "Carbonic anhydrase IV: purification of a secretory form of the recombinant human enzyme and identification of the positions and importance of its disulfide bonds.". Arch. Biochem. Biophys. 333 (2): 432–8. doi:10.1006/abbi.1996.0412. PMID 8809084.
Parkkila S, Parkkila AK, Juvonen T, et al. (1996). "Membrane-bound carbonic anhydrase IV is expressed in the luminal plasma membrane of the human gallbladder epithelium.". Hepatology 24 (5): 1104–8. doi:10.1002/hep.510240521. PMID 8903383.
Stams T, Nair SK, Okuyama T, et al. (1997). "Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution.". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13589–94. PMID 8942978.
Bardien S, Ramesar R, Bhattacharya S, Greenberg J (1997). "Retinitis pigmentosa locus on 17q (RP17): fine localization to 17q22 and exclusion of the PDEG and TIMP2 genes.". Hum. Genet. 101 (1): 13–7. PMID 9385361.
Sender S, Decker B, Fenske CD, et al. (1998). "Localization of carbonic anhydrase IV in rat and human heart muscle.". J. Histochem. Cytochem. 46 (7): 855–61. PMID 9632745.
Wistrand PJ, Carter ND, Conroy CW, Mahieu I (1999). "Carbonic anhydrase IV activity is localized on the exterior surface of human erythrocytes.". Acta Physiol. Scand. 165 (2): 211–8. PMID 10090333.
Fujikawa-Adachi K, Nishimori I, Sakamoto S, et al. (1999). "Identification of carbonic anhydrase IV and VI mRNA expression in human pancreas and salivary glands.". Pancreas 18 (4): 329–35. PMID 10231836.
Sterling D, Alvarez BV, Casey JR (2002). "The extracellular component of a transport metabolon. Extracellular loop 4 of the human AE1 Cl-/HCO3- exchanger binds carbonic anhydrase IV.". J. Biol. Chem. 277 (28): 25239–46. doi:10.1074/jbc.M202562200. PMID 11994299.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.