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PROSITE documentation PDOC51532

PITH 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:

PITH, PS51532; PITH domain profile  (MATRIX)


References

1AuthorsAndersen K.M. Madsen L. Prag S. Johnsen A.H. Semple C.A. Hendil K.B. Hartmann-Petersen R.
TitleThioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome.
SourceJ. Biol. Chem. 284:15246-15254(2009).
PubMed ID19349277
DOI10.1074/jbc.M900016200

2AuthorsSong J. Tyler R.C. Wrobel R.L. Frederick R.O. Vojtek F.C. Jeon W.B. Lee M.S. Markley J.L.
TitleSolution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein.
SourceProtein Sci. 14:1059-1063(2005).
PubMed ID15741346
DOI10.1110/ps.041246805

3AuthorsGoroncy A.K. Koshiba S. Tochio N. Tomizawa T. Inoue M. Tanaka A. Sugano S. Kigawa T. Yokoyama S.
TitleSolution structure of the C-terminal DUF1000 domain of the human thioredoxin-like 1 protein.
SourceProteins 78:2176-2180(2010).
PubMed ID20455272
DOI10.1002/prot.22719



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