IPR036959
Peptidase C12, ubiquitin carboxyl-terminal hydrolase superfamily
InterPro entry
Short name | Peptidase_C12_UCH_sf |
Overlapping entries |
Description
This group of cysteine peptidases belong to the MEROPS peptidase family C12 (ubiquitin C-terminal hydrolase family, clan CA). Families within the CA clan are loosely termed papain-like as protein fold of the peptidase unit resembles that of papain, the type example for clan CA. The type example is the human ubiquitin C-terminal hydrolase UCH-L1.
Ubiquitin is highly conserved, commonly found conjugated to proteins in eukaryotic cells, where it may act as a marker for rapid degradation, or it may have a chaperone function in protein assembly
[2]. The ubiquitin is released by cleavage from the bound protein by a protease
[2]. A number of deubiquitinising proteases are known: all are activated by thiol compounds
[2, 1], and inhibited by thiol-blocking agents and ubiquitin aldehyde
[2, 3], and as such have the properties of cysteine proteases
[2].
The deubiquitinsing proteases can be split into 2 size ranges: 20-30kDa (this entry) and 100-200kDa (
IPR001394)
[2]. The 20-30kDa group includes the yeast yuh1, which is known to be active only against small ubiquitin conjugates, being inactive against conjugated beta-galactosidase
[2]. A mammalian homologue, UCH (ubiquitin conjugate hydrolase), is one of the most abundant proteins in the brain
[2]. Only one conserved cysteine can be identified, along with two conserved histidines. The spacing between the cysteine and the second histidine is thought to be more representative of the cysteine/histidine spacing of a cysteine protease catalytic dyad
[2].
References
1.Mechanism of ubiquitin carboxyl-terminal hydrolase. Borohydride and hydroxylamine inactivate in the presence of ubiquitin. Pickart CM, Rose IA. J. Biol. Chem. 261, 10210-7, (1986). View articlePMID: 3015923
2.Families of cysteine peptidases. Rawlings ND, Barrett AJ. Meth. Enzymol. 244, 461-86, (1994). View articlePMID: 7845226
3.Ubiquitin-aldehyde: a general inhibitor of ubiquitin-recycling processes. Hershko A, Rose IA. Proc. Natl. Acad. Sci. U.S.A. 84, 1829-33, (1987). View articlePMID: 3031653
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.40.532.10
Representative structure
1xd3: Crystal structure of UCHL3-UbVME complex