Primary Information
BoMiProt ID	Bomi141
Protein Name	Serotransferrin
Organism	Bos taurus
Uniprot ID	Q29443
Milk Fraction	Whey
Ref Sequence ID	NP_803450.2
Aminoacid Length	704
Molecular Weight	77753
FASTA Sequence	Download
Gene Name	TF
Gene ID	280705
Protein Existence Status	Reviewed: Experimental evidence at transcript level
Secondary 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;
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	NA
DisProt Annotation
TM Helix Prediction	No TM helices
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.