MIFH_TRISP
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 03-AUG-2022, entry version 71.
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 (1.65 ANGSTROMS) OF 2-114.
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 PDBsum; 1HFO; -.
DR AlphaFoldDB; P81529; -.
DR SMR; P81529; -.
DR STRING; 6334.EFV56343; -.
DR eggNOG; KOG1759; Eukaryota.
DR HOGENOM; CLU_129906_1_1_1; -.
DR EvolutionaryTrace; P81529; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR001398; Macrophage_inhib_fac.
DR InterPro; IPR014347; Tautomerase/MIF_sf.
DR PANTHER; PTHR11954; PTHR11954; 1.
DR Pfam; PF01187; MIF; 1.
DR SUPFAM; SSF55331; SSF55331; 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
