|Protein Name||Carbonic anhydrase 4|
|Ref Sequence ID||NP_776322.1|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Presence in other biological fluids/tissue/cells||found in a number of animal tissues, including kidney and brain|
|Protein Function||catalyses the hydration of carbon dioxide and the dehydration of bicarbonate ions; participates in physiological systems such as respiration, acid-base balance, ion transport, bone resorption, signal transduction, ureagenesis, gluconeogenesis, and lipogenesis; Bovine carbonic anhydrase acts as a powerful competitive inhibitor of the reduction of cytochrome c by xanthine oxidase. CA4-like was positioned to catalyze the conversion of HCO3- to CO2 in the ambient seawater which would facilitate CO2 uptake.|
|Biochemical Properties||Mammalian carbonic anhydrases can be divided into two groups according to their catalytic efficiencies in respect of the reactions between carbon dioxide, bicarbonate and water; presence of high proportion of proline residues, acidic and basic residues, and few sulphur-containing residues; bromide, iodide and nitrate inhibited the enzyme more strongly than did either acetate or chloride; Ki for carbonic anhydrase decreased with increasing pH, whereas K, for cytochrome c varied in the opposite fashion; ∆Hº for the reaction of carbonic anhydrase with xanthine oxidase is very close to 0.0 kcal per mole.|
|Significance in milk||CA VI is an essential factor in normal growth and development of the infant alimentary tract|
|PTMs||Glycosylated: Rabbit kidney CA IV had two N-glycosylation sites and was sialated|
| Site(s) of PTM(s) |
|Predicted Disorder Regions||NA|
|TM Helix Prediction||1TMH; (289-311)|
|Bibliography||1. Karhumaa, P. et al. (2001) ‘The identification of secreted carbonic anhydrase VI as a constitutive glycoprotein of human and rat milk.’, Proceedings of the National Academy of Sciences of the United States of America, 98(20), pp. 11604–8. doi: 10.1073/pnas.121172598. |
2. Fridovich, I. (1967) ‘A reversible association of bovine carbonic anhydrase with milk xanthine oxidase.’, The Journal of biological chemistry, 242(7), pp. 1445–9. Available at: http://www.ncbi.nlm.nih.gov/pubmed/4960670 (Accessed: 5 October 2019).
3. Schwartz, G. J. et al. (2000) ‘Carbonic anhydrase IV is expressed in H + -secreting cells of rabbit kidney’, American Journal of Physiology-Renal Physiology, 278(6), pp. F894–F904. doi: 10.1152/ajprenal.2000.278.6.F894. 4.Chew SF, Koh CZY, Hiong KC, Choo CYL, Wong WP, Neo ML, Ip YK. Light-enhanced expression of Carbonic Anhydrase 4-like supports shell formation in the fluted giant clam Tridacna squamosa. Gene. 2019 Jan 30;683:101-112. doi: 10.1016/j.gene.2018.10.023. Epub 2018 Oct 11. PMID: 30316924.