ID   MIFH_TRISP              Reviewed;         114 AA.
AC   P81529; Q95UI8; Q9Y063;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   04-NOV-2026, entry version 77.
DE   RecName: Full=Macrophage migration inhibitory factor homolog;
DE            Short=MIF;
DE            EC=5.3.2.1;
DE   AltName: Full=L-dopachrome isomerase;
DE   AltName: Full=L-dopachrome tautomerase;
DE            EC=5.3.3.12;
DE   AltName: Full=Phenylpyruvate tautomerase;
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-31; 64-71 AND 104-107,
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND X-RAY CRYSTALLOGRAPHY.
RC   TISSUE=Larva;
RX   PubMed=11439086; DOI=10.1042/0264-6021:3570373;
RA   Tan T.H.P., Edgerton S.A.V., Kumari R., McAlister M.S.B., Roe S.M.,
RA   Nagl S., Pearl L.H., Selkirk M.E., Bianco A.E., Totty N.F., Engwerda C.,
RA   Gray C.A., Meyer D.J., Rowe S.M.;
RT   "Macrophage migration inhibitory factor of the parasitic nematode
RT   Trichinella spiralis.";
RL   Biochem. J. 357:373-383(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=ISS314;
RX   PubMed=12880250; DOI=10.1645/0022-3395(2003)089[0507:meacoa]2.0.co;2;
RA   Wu Z., Boonmars T., Nagano I., Nakada T., Takahashi Y.;
RT   "Molecular expression and characterization of a homologue of host cytokine
RT   macrophage migration inhibitory factor from Trichinella spp.";
RL   J. Parasitol. 89:507-515(2003).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-20, FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   TISSUE=Larva;
RX   PubMed=9794786; DOI=10.1042/bj3350495;
RA   Pennock J.L., Behnke J.M., Bickle Q.D., Devaney E., Grencis R.K.,
RA   Isaac R.E., Joshua G.W.P., Selkirk M.E., Zhang Y., Meyer D.J.;
RT   "Rapid purification and characterization of L-dopachrome-methyl-ester
RT   tautomerase (macrophage migration inhibitory factor) from Trichinella
RT   spiralis, Trichuris muris and Brugia pahangi.";
RL   Biochem. J. 335:495-498(1998).
CC   -!- FUNCTION: Tautomerization of the methyl ester of L-dopachrome. Inhibits
CC       migration of human peripheral blood mononuclear cells.
CC       {ECO:0000269|PubMed:11439086, ECO:0000269|PubMed:9794786}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate;
CC         Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509;
CC         EC=5.3.3.12;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phenylpyruvate = enol-phenylpyruvate; Xref=Rhea:RHEA:17097,
CC         ChEBI:CHEBI:16815, ChEBI:CHEBI:18005; EC=5.3.2.1;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=144 uM for phenylpyruvate {ECO:0000269|PubMed:11439086};
CC         KM=783 uM for p-hydroxyphenylpyruvate {ECO:0000269|PubMed:11439086};
CC         Vmax=1026 umol/min/mg enzyme toward phenylpyruvate
CC         {ECO:0000269|PubMed:11439086};
CC         Vmax=34.6 umol/min/mg enzyme toward p-hydroxyphenylpyruvate
CC         {ECO:0000269|PubMed:11439086};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11439086}.
CC       Note=Secreted by larvae into the host.
CC   -!- DEVELOPMENTAL STAGE: Expressed in newborn larvae, precyst muscle
CC       larvae, postcyst muscle larvae and adult worms.
CC       {ECO:0000269|PubMed:12880250}.
CC   -!- INDUCTION: Inhibited by free fatty acids and haematin.
CC       {ECO:0000269|PubMed:9794786}.
CC   -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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DR   EMBL; AJ012740; CAB46354.1; -; mRNA.
DR   EMBL; AY050661; AAL12629.1; -; mRNA.
DR   PDB; 1HFO; X-ray; 1.65 A; A/B/C/D/E/F=2-114.
DR   AlphaFoldDB; P81529; -.
DR   SMR; P81529; -.
DR   eggNOG; KOG1759; Eukaryota.
DR   HOGENOM; CLU_129906_1_1_1; -.
DR   OMA; AAYIQVR; -.
DR   OrthoDB; 255819at2759; -.
DR   EvolutionaryTrace; P81529; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005125; F:cytokine activity; IEA:TreeGrafter.
DR   GO; GO:0004167; F:dopachrome isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050178; F:phenylpyruvate tautomerase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.429.10; Macrophage Migration Inhibitory Factor; 1.
DR   InterPro; IPR001398; Macrophage_inhib_fac.
DR   InterPro; IPR014347; Tautomerase/MIF_sf.
DR   PANTHER; PTHR11954; D-DOPACHROME DECARBOXYLASE; 1.
DR   PANTHER; PTHR11954:SF6; MACROPHAGE MIGRATION INHIBITORY FACTOR; 1.
DR   Pfam; PF01187; MIF; 1.
DR   SUPFAM; SSF55331; Tautomerase/MIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytokine; Direct protein sequencing; Isomerase; Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11439086,
FT                   ECO:0000269|PubMed:9794786"
FT   CHAIN           2..114
FT                   /note="Macrophage migration inhibitory factor homolog"
FT                   /id="PRO_0000158074"
FT   ACT_SITE        2
FT                   /note="Proton acceptor; via imino nitrogen"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        55
FT                   /note="K -> N (in Ref. 1; CAB46354)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   HELIX           19..31
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   STRAND          58..67
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   HELIX           70..88
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:1HFO"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:1HFO"
SQ   SEQUENCE   114 AA;  12337 MW;  8B68B33C6309FAF1 CRC64;
     MPIFTLNTNI KATDVPSDFL SSTSALVGNI LSKPGSYVAV HINTDQQLSF GGSTKPAAFG
     TLMSIGGIEP SRNRDHSAKL FDHLNKKLGI PKNRMYIHFV NLNGDDVGWN GTTF
//