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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC00892
Macrophage migration inhibitory factor family signature


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00892

Description

A protein called macrophage migration inhibitory factor (MIF) [1] seems to exerts an important role in host inflammatory responses. It play a pivotal role in the host response to endotoxic shock and appears to serve as a pituitary "stress" hormone that regulates systemic inflammatory responses. MIF is a secreted protein of 115 residues which is not processed from a larger precursor.

D-dopachrome tautomerase [2] is a mammalian cytoplasmic enzyme involved in melanin biosynthesis and that tautomerizes D-dopachrome with concomitant decarboxylation to give 5,6-dihydroxyindole (DHI). It is a protein of 117 residues highly related to MIF.

It must be noted that MIF binds glutathione and has been said to be related to glutathione S-transferases. This assertion has been later disproved [3].

As a signature pattern for these proteins, we selected a conserved region located in the central section.

Last update:

December 2004 / Pattern and text revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

MIF, PS01158; Macrophage migration inhibitory factor family signature  (PATTERN)


References

1AuthorsBucala R.
TitleIdentification of MIF as a new pituitary hormone and macrophage cytokine and its role in endotoxic shock.
SourceImmunol. Lett. 43:23-26(1994).
PubMed ID7737686

2AuthorsOdh G. Hindemith A. Rosengren A.-M. Rosengren E. Rorsman H.
TitleIsolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole.
SourceBiochem. Biophys. Res. Commun. 197:619-624(1993).
PubMed ID8267597

3AuthorsPearson W.R.
TitleMIF proteins are not glutathione transferase homologs.
SourceProtein Sci. 3:525-527(1994).
PubMed ID8019423



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