InterPro : IPR015644

Name  Peptidase C1A, cathepsin K Short Name  Peptidase_C1A_cathepsin-K
Type  Family Description  Cysteine peptidases have characteristic molecular topologies, which can be seen not only in their three-dimensional structures, but commonly also in the two-dimensional structures. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins whichare evolutionary related), and further sub-divided into families, on the basis of the architecture of their catalytic dyad or triad []. This group of cysteine peptidases belong to the MEROPS peptidase family C1, sub-family C1A (papain family, clan CA).Cathepsin K is a cysteine protease expressed predominantly in osteoclasts. Activated cathepsin K cleaves key bone matrix proteins and is believed to play an important role in degrading the organic phase of bone during bone resorption. Cathepsin K is essential for normal bone resorption; Homo sapiens(Human) lacking cathepsin K exhibit pycnodysostosis, which is characterised by short stature and osteosclerosis []. Histological and radiographic analysis of the cathepsin K-deficient Mus musculus(Mouse) revealed osteoporosis of the long bones and vertebrae, and abnormal joint morphology [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

3 Contains

Id Name Short Name Type
IPR000668 Peptidase C1A, papain C-terminal Peptidase_C1A_C Domain
IPR013201 Proteinase inhibitor I29, cathepsin propeptide Prot_inhib_I29 Domain
IPR000169 Cysteine peptidase, cysteine active site Pept_cys_AS Active_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR013128 Peptidase C1A Peptidase_C1A Family

3 Publications

First Author Title Year Journal Volume Pages
Barrett AJ Evolutionary lines of cysteine peptidases. 2001 Biol Chem 382 727-33
Troen BR The role of cathepsin K in normal bone resorption. 2004 Drug News Perspect 17 19-28
Gowen M Cathepsin K knockout mice develop osteopetrosis due to a deficit in matrix degradation but not demineralization. 1999 J Bone Miner Res 14 1654-63



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)