PROSITE documentation PDOC00892
Macrophage migration inhibitory factor family signature


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.


Technical section

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

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


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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