CATH Classification

Domain Context

CATH Clusters

Functional Family E3 ubiquitin-protein ligase ZNRF3

Enzyme Information
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q5SSZ7
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC -!- Cf. EC

UniProtKB Entries (1)

Mus musculus
E3 ubiquitin-protein ligase ZNRF3

PDB Structure

External Links
Primary Citation
Structural and Molecular Basis of Znrf3/Rnf43 Transmembrane Ubiquitin Ligase Inhibition by the Wnt Agonist R-Spondin.
Zebisch, M., Xu, Y., Krastev, C., Macdonald, B.T., Chen, M., Gilbert, R.J.C., He, X., Jones, E.Y.