Primary Information | |
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BoMiProt ID | Bomi19 |
Protein Name | Calmodulin |
Organism | Bos taurus |
Uniprot ID | P62157 |
Milk Fraction | Whey |
Ref Sequence ID | NP_001039714.1 |
Aminoacid Length | 149 |
Molecular Weight | 16838 |
FASTA Sequence | Download |
Gene Name | CALM |
Gene ID | 617095 |
Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
Presence in other biological fluids/tissue/cells | bovine mammary tissue, CNS, testes, |
Protein Function | Calcium and calmodulin are involved in regulation of many biochemical processes - muscle contraction, stimulussecretion coupling, microtubule disassembly, and several enzymatic activities; helps in large transcellular calcium flux in mammary tissue during lactation; In brain, calmodulin may function to govern the release of neurotransmitters from vesicular stores |
Biochemical Properties | CaM binds tightly to membranes and of heat-stable inhibitor proteins occurring in bovine brain |
Significance in milk | CaM appears to increase prior to onset of lactation; increases in CaM during lactogenesis when mammary epithelial cells are proliferating; increase of calmodulin in milk with SCC greater or equal to 1,000,000 |
PTMs | Trimethyllysine, which is amino acid residue 115 in beef calmodulin, occurs as the result of posttranslational N-methylation catalyzed by S-adenosylmethionine:calmodulin (lysine) N-methyltransferase; substrate for protein carboxylmethyltransferase; calmodulin converting enzyme clips the carboxyl terminal lysine from calmodulin; undergoes acetylation of its N-terminal amino acid residue (alanine)4 |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
Predicted Disorder Regions | 1-88,91-149 |
DisProt Annotation | |
TM Helix Prediction | No TM helices |
Significance of PTMs | calmodulin converting enzyme causes a change in its electrophoretic mobility |
PDB ID | 1A29, 1AK8, 1CDM, 1CM1, 1CM4, 1CMF, 1CMG, 1DEG, 1FW4, 1LIN, 1PRW, 1QIV, 1QIW, 1XA5, 2CLN, 2F2O, 2F2P, 2FOT, 3IF7, 6O20, |
Additional Comments | CaM concentrations double during the G1-S phase boundary of cell growth in CHO-K1 cell line; |
Bibliography | 1. Alston-Mills, B., Barefield, K. L., Corrado, L. J., & Douglass, L. W. (1988). Evidence of calmodulin in bovine milk with high somatic cell counts. Journal of Dairy Science, 71(8), 2246–2249. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/3170865. 2. Riss, T. L., & Baumrucker, C. R. (1982). Calmodulin purification and quantitation from bovine mammary tissue. Journal of Dairy Science, 65(9), 1722–1728. https://doi.org/10.3168/jds.S0022-0302(82)82407-7. 3. Murtaugh, T. J., Rowe, P. M., Vincent, P. L., Wright, L. S., & Siegel, F. L. (1983). Posttranslational modification of calmodulin. Methods in Enzymology, 102, 158–170. https://doi.org/10.1016/s0076-6879(83)02017-0. 4. Murtaugh, T. J., Wright, L. S., & Siegel, F. L. (1986). Posttranslational modification of calmodulin in rat brain and pituitary. Journal of Neurochemistry, 47(1), 164–172. https://doi.org/10.1111/j.1471-4159.1986.tb02845. |