{PDOC00892}
{PS01158; MIF}
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* Macrophage migration inhibitory factor family signature *
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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.

-Consensus pattern: [DE]-P-[CLV]-[APT]-x(3)-[LIVM]-x-S-[IS]-[GT]-x-[LIVM]-
                    [GST]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2004 / Pattern and text revised.

[ 1] Bucala R.
     "Identification of MIF as a new pituitary hormone and macrophage
     cytokine and its role in endotoxic shock."
     Immunol. Lett. 43:23-26(1994).
     PubMed=7737686
[ 2] Odh G., Hindemith A., Rosengren A.-M., Rosengren E., Rorsman H.
     "Isolation of a new tautomerase monitored by the conversion of
     D-dopachrome to 5,6-dihydroxyindole."
     Biochem. Biophys. Res. Commun. 197:619-624(1993).
     PubMed=8267597
[ 3] Pearson W.R.
     "MIF proteins are not glutathione transferase homologs."
     Protein Sci. 3:525-527(1994).
     PubMed=8019423

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