Search by BoMiProt ID - Bomi19


Primary Information

BoMiProt ID Bomi19
Protein Name Calmodulin
Organism Bos taurus
Uniprot IDP62157
Milk FractionWhey
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.