Primary Information |
|---|
| BoMiProt ID | Bomi8229 |
|---|
| Protein Name | Pro-cathepsin H |
|---|
| Organism | Bos taurus |
|---|
| Uniprot ID | Q3T0I2 |
|---|
| Milk Fraction | Whey |
|---|
| Ref Sequence ID | NP_001029557.1 |
|---|
| Aminoacid Length | 335 |
|---|
| Molecular Weight | 37351 |
|---|
| FASTA Sequence |
Download |
|---|
| 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,
Phosphorylation
| >sp|Q3T0I2|CATH_BOVIN Pro-cathepsin H OS=Bos taurus OX=9913 GN=CTSH PE=2 SV=1
MWAVLPLLCAGAWLLGAPACGAAELAANSLEKFHFQSWMVQHQKKYSSEEYYHRLQAFAS
NLREINAHNARN*72HTFKMGLNQFSDMSFDELKRKYLWSEPQN*101CSATKSNYLRGTGPYPPSM
DWRKKGNFVTPVKNQGSCGSCWTFSTTGALESAVAIATGKLPFLAEQQLVDCAQNFNNHG
CQGGLPSQAFEYIRYNKGIMGEDTYPYRGQDGDCKYQPSKAIAFVKDVAN*230ITLNDEEAMV
EAVALHNPVSFAFEVTADFMMYRKGIYSSTSCHKTPDKVNHAVLAVGYGEEKGIPYWIVK
NSWGPNWGMKGYFLIERGKNMCGLAACASFPIPLV
|
|---|
| 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. https://doi.org/10.1371/journal.pone.0200374 |