Primary Information |
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BoMiProt ID | Bomi10431 |
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Protein Name | Uroplakin-2/Uroplakin II/UPII/UP2 |
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Organism | Bos taurus |
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Uniprot ID | Q08537 |
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Milk Fraction | whey |
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Ref Sequence ID | NP_776639.1 |
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Aminoacid Length | 185 |
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Molecular Weight | 19619 |
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FASTA Sequence |
Download |
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Gene Name | UPK2 |
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Gene ID | 281569 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in regulating the assembly of the AUM. |
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Biochemical Properties | t UPII is primarily synthesized as a 19-kDa non-glycosylated prepro-UPII precursor.It comprises three parts of linked sequences: 1) a N-terminal 26–28 amino acids fragment (2-kDa), 2) a middle fragment located at 59 amino acids propeptide with three asparagines, the potential sites for N-glycosylation and 3) a 100 amino acids polypeptide (15-kDa) corresponding to the mature native form of UPII.The precursor of bovine pro-UPII which carries complex N-glycans does not contain exposed sites susceptible for degradation by exoproteases, but has four furino-like endoproteases. For efficient cleavage, the furin-cleavage site requires some arginines in signature sequence: Arg − 4-Xaa − 3-(Lys/Arg) − 2-Arg − 1.The released mature bovine UPII (15-kDa) does not possess the asparagines/s able to be N-glycosylated. |
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PTMs | Glycosylation,Proteolytic cleavage |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q08537|UPK2_BOVIN Uroplakin-2 OS=Bos taurus OX=9913 GN=UPK2 PE=1 SV=1
MASPWPVWTLSWILILLAVLVPGAAADFN*29ISSLSGLLSPVMTESLLVALPPCHLTGGN*58AT
LTVRRAN*67DSKVVRSSFVVPPCRGRRELVSVVDSGSGFTVTRLSAYQVTNLAPGTKYYISY
LVTKGASTESSREIPMSTFPRRKAESIGLAMARTGGMVVITVLLSVAMFLLVLGLIIALA
LGARK
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | TMHs; (7-25), (44-62), (159-181) |
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Significance of PTMs | In ER the signal sequence is cut-off from the 19-kDa prepro-UPII precursor. A propeptide is further glycosylated by addition of three attached high-mannose N-glycans. The attachment of sugar chains to pro-UPII causes an increase in the molecular weight of the immature form of UPII to 29-kDa. Glycosylation changes in uroplakins correlate with and might reflect progressive stages of pathological conditions of the urothelium such as cancer, urinary tract infections, interstitial cystitis and others. |
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Bibliography | 1.Kątnik-Prastowska, I., Lis, J., & Matejuk, A. (2014). Glycosylation of uroplakins. Implications for bladder physiopathology. Glycoconjugate journal, 31(9), 623–636. https://doi.org/10.1007/s10719-014-9564-4 2.Lin, J. H., Wu, X. R., Kreibich, G., & Sun, T. T. (1994). Precursor sequence, processing, and urothelium-specific expression of a major 15-kDa protein subunit of asymmetric unit membrane. The Journal of biological chemistry, 269(3), 1775–1784. |