H
IPR042299

Ufd1-like, Nn domain

InterPro entry
Short nameUfd1-like_Nn
Overlapping entries
 

Description

This entry includes Ubiquitin fusion degradation protein Ufd1 from fungi and Ufd1-like proteins from animals and plants.

Ufd1 is part of the Ufd1-Npl4 complex that functions as the substrate-recruiting cofactor for Cdc48 segregase. The Cdc48-Ufd1-Npl4 complex is involved in degradation of misfolded ER proteins
[3]
. The Ufd1-Npl4 complex has been found to recruit Cdc48 to ubiquitylated CMG (Cdc45-MCM-GINS) helicase at the end of chromosome replication, thereby driving the disassembly reaction
[4]
.

In humans, Npl4-Ufd1 acts as a cofactor in reducing antiviral innate immune responses by facilitating proteasomal degradation of RIG-I (a viral RNA sensor)
[2]
.

The Ufd1 N-terminal fragment is composed of two readily identifiable subdomains designated as Nn and Nc subdomains. The Nn subdomain adapts a double-psi β-barrel fold, and the Nc subdomain has a mixed α/β roll structure
[1]
. This superfamily represents the Nn domain found in Ufd1 proteins.

References

1.Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Park S, Isaacson R, Kim HT, Silver PA, Wagner G. Structure 13, 995-1005, (2005). View articlePMID: 16004872

2.A non-canonical role of the p97 complex in RIG-I antiviral signaling. Hao Q, Jiao S, Shi Z, Li C, Meng X, Zhang Z, Wang Y, Song X, Wang W, Zhang R, Zhao Y, Wong CC, Zhou Z. EMBO J. 34, 2903-20, (2015). View articlePMID: 26471729

3.The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase. Barbin L, Eisele F, Santt O, Wolf DH. Biochem. Biophys. Res. Commun. 394, 335-41, (2010). View articlePMID: 20206597

4.Ufd1-Npl4 Recruit Cdc48 for Disassembly of Ubiquitylated CMG Helicase at the End of Chromosome Replication. Maric M, Mukherjee P, Tatham MH, Hay R, Labib K. Cell Rep 18, 3033-3042, (2017). View articlePMID: 28355556

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