PROSITE documentation PDOC51532PITH domain profile
Description
The proteasome-interacting thioredoxin (PITH) domain is a general proteasome-interacting module [1].
The PITH domain is dominated by a jelly roll β-sandwich structure (see <PDB:1XOY>). The β-sandwich is formed by face-to-face packing of two anti-parallel β-sheets. Another two-stranded β-sheet seals off one end of the β-barrel [2,3].
Some proteins known to contain a PITH domain are listed below:
- Human Txnl1 or TRP32, a thioredoxin-like protein implicated in endocytosis and in protection against glucose deprivation-induced cytotoxicity.
- Human C1ORF28, an uncharacterized protein that does not contain any other known protein domains, but has been found to associate with 26S proteasomes.
- Arabidopsis thaliana At3g04780, a single domain protein.
The profile we developed covers the entire PITH domain.
Last update:March 2011 / First entry.
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Technical section
PROSITE method (with tools and information) covered by this documentation:
References
1 | Authors | Andersen K.M. Madsen L. Prag S. Johnsen A.H. Semple C.A. Hendil K.B. Hartmann-Petersen R. |
Title | Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome. | |
Source | J. Biol. Chem. 284:15246-15254(2009). | |
PubMed ID | 19349277 | |
DOI | 10.1074/jbc.M900016200 |
2 | Authors | Song J. Tyler R.C. Wrobel R.L. Frederick R.O. Vojtek F.C. Jeon W.B. Lee M.S. Markley J.L. |
Title | Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein. | |
Source | Protein Sci. 14:1059-1063(2005). | |
PubMed ID | 15741346 | |
DOI | 10.1110/ps.041246805 |
3 | Authors | Goroncy A.K. Koshiba S. Tochio N. Tomizawa T. Inoue M. Tanaka A. Sugano S. Kigawa T. Yokoyama S. |
Title | Solution structure of the C-terminal DUF1000 domain of the human thioredoxin-like 1 protein. | |
Source | Proteins 78:2176-2180(2010). | |
PubMed ID | 20455272 | |
DOI | 10.1002/prot.22719 |
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