Search by BoMiProt ID - Bomi141


Primary Information

BoMiProt ID Bomi141
Protein Name Serotransferrin
Organism Bos taurus
Uniprot IdQ29443
Milk FractionWhey
Ref Sequence Id NP_803450.2
Amino Acid Lenth 704
Molecular Weight 77753
Fasta Sequence http://www.uniprot.org/uniprot/Q29443.fasta
Gene Name TF
Gene Id 280705
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondry Information

Presence in other biological fluids/tissue/cells serum, milk
Protein Function Role in iron metabolism; delivers iron to cells via receptor mediated endocytosis; remove toxic free iron from blood; antibacterial;
Biochemical Properties Binding of iron at terminals are pH dependant; affinity for Fe3+ decreases at lower pH; Glycan chains enhances solubility by virtue of their hydrophilic groups and increased charges;
Significance in milk Resistant to gastric hydrolysis; render biological activity in gastrointestinal tract
PTMs Glycosylated; carbohydrate content varies from 3 to 11.8% of total protein weight; biantennary structure; presence of branched, hetero N-glycan chains; each glycan consists of two sialic acid, two galactose, three mannose and four N-acetylglucosamine residues;
Bibliography 1. Britton, J. R. and Koldovský, O. (1989) Gastric luminal digestion of lactoferrin and transferrin by preterm infants. Early Hum. Dev. 19, 127–135.
2. 1. Britton, J. R. and Koldovský, O. (1989) Gastric luminal digestion of lactoferrin and transferrin by preterm infants. Early Hum. Dev. 19, 127–135.
3. 1. MacGillivray, R. T., Mendez, E., Sinha, S. K., Sutton, M. R., Lineback-Zins, J., and Brew, K. (1982) The complete amino acid sequence of human serum transferrin. Proc. Natl. Acad. Sci. U. S. A. 79, 2504–2508.
4. 1. Kerckaert, J. P. and Bayard, B. (1982) Glycan uniformity within molecular variants of transferrin with distinct affinity for concanavalin A. Biochem. Biophys. Res. Commun. 105, 1023–1030.
5. 1. Aisen, P. and Listowsky, I. (1980) Iron transport and storage proteins. Annu. Rev. Biochem. 49, 357–393.
6. 1. Princiotto, J. V and Zapolski, E. J. (1975) Difference between the two iron-binding sites of transferrin. Nature 255, 87–88.
7. 1. Thakurta, P. G., Choudhury, D., Dasgupta, R., and Dattagupta, J. K. (2004) Tertiary structural changes associated with iron binding and release in hen serum transferrin: a crystallographic and spectroscopic study. Biochem. Biophys. Res. Commun. 316, 1124–1131.