Search by BoMiProt ID - Bomi8229

Primary Information

BoMiProt ID Bomi8229
Protein Name Pro-cathepsin H
Organism Bos taurus
Uniprot IdQ3T0I2
Milk FractionWhey
Ref Sequence Id NP_001029557.1
Aminoacid Length 335
Molecular Weight 37351
Fasta Sequence
Gene Name CTSH
Gene Id 510524
Protein Existence Status reviewed

Secondary Information

Protein Function Important for the overall degradation of proteins in lysosomes. lysosomal cysteine protease of the papain superfamily involved in protein degradation.
Biochemical Properties Hydrolysis of proteins, acting as an aminopeptidase.A mini-chain (the octapeptide EPQNCSAT from the prodomain) remains bound to cathepsin H through a disulfide bond and is essential for the aminopeptidase activity.N-terminal prodomain (Ala1P-Pro93P) and a C-terminal mature domain (Tyr1-Val220) with a disulfide bridge between Cys212 and the mini-chain Cys80P.he prodomain of procathepsin H has an N-terminal helical subdomain (Ala1P-Ser75P) and an extended portion (Glu76P-Pro93P) that links the helical subdomain to Tyr1 of the mature domain. The helical subdomain is positioned on top of the right domain of the mature domain while the C-terminal extended portion traverses the substrate binding cleft toward the N-terminus of the mature domain, preventing access of the substrates to the active site.
Significance in milk Involved in milk protein proteolysis
PTMs Disulfide bond formation, Glycoprotein,Proteolytic cleavage
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Glycans could be assigned unambiguously in procathepsin H for the two glycosylation sites, Asn79P on the mini-chain of the prodomain and Asn115 on the mature domain.glycosylation of Asn115 is also observed in cathepsin H.However, no glycan was built for Asn79P in cathepsin H due to poor electron density, although it was glycosylated.Maturation of procathepsin H involves at least three cleavages of the prodomain: at the N terminus of the mature domain and at both termini of the mini-chain. During this processing, the N-terminal helical subdomain (Ala1P-Ser75P) preceding the mini-chain and the C-terminal linker (Lys84P-Pro93) connecting the mini-chain with the N-terminus of the mature domain, are removed while the mini-chain remains attached to the mature domain only by means of the disulfide bond.
Bibliography Hao, Y., Purtha, W., Cortesio, C., Rui, H., Gu, Y., Chen, H., Sickmier, E. A., Manzanillo, P., & Huang, X. (2018). Crystal structures of human procathepsin H. PloS one, 13(7), e0200374.