Primary Information |
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| BoMiProt ID | Bomi240 |
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| Protein Name | Carbonic anhydrase 4 |
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| Organism | Bos taurus |
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| Uniprot ID | Q95323 |
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| Milk Fraction | MFGM |
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| Ref Sequence ID | NP_776322.1 |
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| Aminoacid Length | 312 |
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| Molecular Weight | 35151 |
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| FASTA Sequence |
Download |
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| Gene Name | CA4 |
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| Gene ID | 280741 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | found in a
number of animal tissues, including kidney and brain |
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| 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. |
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| 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. |
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| Significance in milk | CA VI is an essential factor in normal growth and development of the infant alimentary tract |
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| PTMs | Glycosylated: Rabbit kidney CA IV had two N-glycosylation sites and was sialated |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (289-311) |
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| 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. |
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