Search by BoMiProt ID - Bomi10431


Primary Information

BoMiProt ID Bomi10431
Protein Name Uroplakin-2/Uroplakin II/UPII/UP2
Organism Bos taurus
Uniprot IdQ08537
Milk Fractionwhey
Ref Sequence Id NP_776639.1
Aminoacid Length 185
Molecular Weight 19619
Fasta Sequence https://www.uniprot.org/uniprot/Q08537.fasta
Gene Name UPK2
Gene Id 281569
Protein Existence Status reviewed

Secondary Information

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.
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.
PTMs Glycosylation,Proteolytic cleavage
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
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction TMHs; (7-25), (44-62), (159-181)
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.
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.