Primary Information |
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| BoMiProt ID | Bomi161 |
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| Protein Name | Mucin 15 |
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| Organism | Bos taurus |
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| Uniprot ID | Q8MI01 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_788804.1 |
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| Aminoacid Length | 280 |
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| Molecular Weight | 30239 |
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| FASTA Sequence |
Download |
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| Gene Name | MUC15 |
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| Gene ID | 337919 |
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| Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | mammary gland, lungs, lymph nodes |
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| Protein Function | protection
of epithelial surfaces, immune responses, adhesion,
inflammation, tumor genesis |
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| 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; |
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| 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 |
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| 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 |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q8MI01|MUC15_BOVIN Mucin-15 OS=Bos taurus OX=9913 GN=MUC15 PE=1 SV=1
MLTSAKILLISILSSLLLFGSHGEEGQKTN*30TTESTAEDLKTMENQSVPLE
SKANLTSDKENRETSNPKASN*71FSFEDPSN*79KTHETGFYSNLSTDN*94SSRSPS
LMPTLSPRSPSTHSFVSKLPWN*122SSIADNSLLPASAPPN*138TTVPVSSEN*147FTL
SSIN*154DTMKAPDN*162SSITVSNLPSGPN*175TTSVTPMVTEGWPTTTRESMEGFTV
YQETTLHPTLKFTN*214NSKIFPNTSDPQEENRNTGVVFGAILGAILGASLLS
LVGYLLCGKRKTDSFSHRRLYDDRNEPVLRLDNAPEPYDMSFGNSSYYNP
TANDSSTSAGGENAHDSIPMDDIPPLRTSV
|
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| Predicted Disorder Regions | 22-115,164-185,279-330 |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (234-256) |
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| 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 |
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| 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. https://doi.org/10.1046/j.1432-1033.2002.02949.
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. https://doi.org/10.3168/jds.2007-0082. |
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