Search by BoMiProt ID - Bomi4470


Primary Information

BoMiProt ID Bomi4470
Protein Name Carbonic anhydrase 3/Carbonate dehydratase III/Carbonic anhydrase III/CA-III
Organism Bos taurus
Uniprot IDQ3SZX4
Milk FractionWhey
Ref Sequence ID NP_001029609.1
Aminoacid Length 260
Molecular Weight 29370
FASTA Sequence Download
Gene Name CA3
Gene ID 513212
Protein Existence Status reviewed

Secondary Information

Protein Function metalloenzymes catalyze the reversible hydration of carbon dioxide and bicarbonate.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. A proportion of carriers of Duchenne muscle dystrophy have a higher CA3 level than normal. The gene spans 10.3 kb and contains seven exons and six introns.
Biochemical Properties catalyses the rapid hydration and dehydration of CO2 and H2CO3, respectively, is widely distributed in mammalian tissues
Significance in milk participates in physiological systems such as respiration, acid-base balance, ion transport, bone resorption, signal transduction, ureagenesis, gluconeogenesis, and lipogenesis.
PTMs Acetylation on Ala, Glutathionylation on Cys, Phosphorylation on Ser ,Thr ,Tyr
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q3SZX4|CAH3_BOVIN Carbonic anhydrase 3 OS=Bos taurus OX=9913 GN=CA3 PE=2 SV=3 MAKEWGYADHNGPDHWHELFPNAKGENQS*29PIELNTKEISHDPS*43LKPWTAS*50YDPGS*55AKTIL NNGKTCRVVFDDT*73YDRSMLRGGPLAAPYRLRQFHLHWGSSDDHGSEHSVDGVKYAAELHL VHWNSKY*127NSYATALKHADGIAVVGVFLKIGREKGEFQLLLDALDKIKTKGKEAPFNNFNP SCLFPACRDYWTYHGSFTTPPCEECIVWLLLKEPIT*216VSS*219DQIAKLRTLYSSAENEPPVPL VRNWRPPQPIKGRIVKASFK
Predicted Disorder Regions 1 disordered segment; (1-29), disordered residues-36,44,237,260
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs S-glutathionylated in hepatocytes under oxidative stress
Additional Comments Carbonic anhydrase III (CA III) exhibits low carbon dioxide hydratase activity in cancer. CA III promotes EMT and cell migration and is potentially related to the FAK/Src signaling pathway in oral cancer.
Linking IDs
Bibliography 1.Kitade K, Nishita T, Yamato M, Sakamoto K, Hagino A, Katoh K, Obara Y. Expression and localization of carbonic anhydrase in bovine mammary gland and secretion in milk. Comp Biochem Physiol A Mol Integr Physiol. 2003 Feb;134(2):349-54. doi: 10.1016/s1095-6433(02)00268-4. PMID: 12547264. 2.Chu YH, Su CW, Hsieh YS, Chen PN, Lin CW, Yang SF. Carbonic Anhydrase III Promotes Cell Migration and Epithelial-Mesenchymal Transition in Oral Squamous Cell Carcinoma. Cells. 2020 Mar 13;9(3):704. doi: 10.3390/cells9030704. PMID: 32183030; PMCID: PMC7140601.