Search by BoMiProt ID - Bomi161

Primary Information

BoMiProt ID Bomi161
Protein Name Mucin 15
Organism Bos taurus
Uniprot IDQ8MI01
Milk FractionWhey
Ref Sequence ID NP_788804.1
Aminoacid Length 280
Molecular Weight 30239
FASTA Sequence Download
Gene Name MUC15
Gene ID 337919
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Presence in other biological fluids/tissue/cells mammary gland, lungs, lymph nodes
Protein Function protection of epithelial surfaces, immune responses, adhesion, inflammation, tumor genesis
Biochemical Properties predominant amino acids - serine, threonine and proline; derived from a precursor sequence including a signal peptide, a serine/threonine/proline-rich extracellular region, a hydrophobic transmembrane domain and a cytoplasmic tail;
Significance in milk associated with the milk fat globule membrane; function as a protective mucin, perhaps as a coconstituent with gel-forming mucins in mucus, or it may act at the apical cell surfaces as a ligand for other cell surface molecules
PTMs Heavily O-glycosylated; glycans are composed of fucose, galactose, mannose, N-acetylgalactosamine, N-acetylglycosamine, and sialic acid; hybrid-type N-glycans - sialylated and contain terminal poly-lactosamine structures; O-linked glycans were found to constitute some unsubstituted Core- 1 structures and a substantial number of sialylated Core-1 O-linked glycans; complex O-glycans contain high amounts N-acetylglucosamine residues and a small subset of is decorated with lactosamine on their terminal ends
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
>sp|Q8MI01|MUC15_BOVIN Mucin-15 OS=Bos taurus OX=9913 GN=MUC15 PE=1 SV=1
Predicted Disorder Regions 22-115,164-185,279-330
DisProt Annotation
TM Helix Prediction 1TMH; (234-256)
Significance of PTMs dense glycosylation in the mucin domain may primarily be to change the biophysical properties of the mucin; mucin glycans provide protective barriers, provide lubrication because of their water-binding capacity, and change the overall structure of the glycosylated region into an extended conformation
Bibliography 1. Pallesen, L. T., Berglund, L., Rasmussen, L. K., Petersen, T. E., & Rasmussen, J. T. (2002). Isolation and characterization of MUC15, a novel cell membrane-associated mucin. European Journal of Biochemistry, 269(11), 2755–2763.
2. Pallesen, L. T., Pedersen, L. R. L., Petersen, T. E., & Rasmussen, J. T. (2007). Characterization of carbohydrate structures of bovine MUC15 and distribution of the mucin in bovine milk. Journal of Dairy Science, 90(7), 3143–3152.