Search by BoMiProt ID - Bomi240


Primary Information

BoMiProt ID Bomi240
Protein Name Carbonic anhydrase 4
Organism Bos taurus
Uniprot IdQ95323
Milk FractionMFGM
Ref Sequence Id NP_776322.1
Amino Acid Lenth 312
Molecular Weight 35151
Fasta Sequence https://www.uniprot.org/uniprot/Q95323.fasta
Gene Name CA4
Gene Id 280741
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondry Information

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
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
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.