MIF_XENTR
ID MIF_XENTR Reviewed; 115 AA.
AC A9JSE7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Macrophage migration inhibitory factor;
DE Short=MIF;
DE EC=5.3.2.1 {ECO:0000250|UniProtKB:P14174};
DE AltName: Full=L-dopachrome isomerase;
DE AltName: Full=L-dopachrome tautomerase;
DE EC=5.3.3.12 {ECO:0000250|UniProtKB:P14174};
DE AltName: Full=Phenylpyruvate tautomerase;
GN Name=mif;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pro-inflammatory cytokine. Involved in the innate immune
CC response to bacterial pathogens. The expression of MIF at sites of
CC inflammation suggests a role as mediator in regulating the function of
CC macrophages in host defense. Has phenylpyruvate tautomerase and
CC dopachrome tautomerase activity (in vitro), but the physiological
CC substrate is not known. It is not clear whether the tautomerase
CC activity has any physiological relevance, and whether it is important
CC for cytokine activity (By similarity). {ECO:0000250|UniProtKB:P14174}.
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 Evidence={ECO:0000250|UniProtKB:P14174};
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; Evidence={ECO:0000250|UniProtKB:P14174};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q76BK2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P14174}.
CC Cytoplasm {ECO:0000250|UniProtKB:P14174}. Note=Does not have a
CC cleavable signal sequence and is secreted via a specialized, non-
CC classical pathway. Secreted by macrophages upon stimulation (By
CC similarity). {ECO:0000250|UniProtKB:P14174}.
CC -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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DR EMBL; BC156031; AAI56032.1; -; mRNA.
DR RefSeq; NP_001107147.1; NM_001113675.1.
DR AlphaFoldDB; A9JSE7; -.
DR SMR; A9JSE7; -.
DR STRING; 8364.ENSXETP00000029260; -.
DR PaxDb; A9JSE7; -.
DR GeneID; 100134996; -.
DR KEGG; xtr:100134996; -.
DR CTD; 4282; -.
DR Xenbase; XB-GENE-487448; mif.
DR eggNOG; KOG1759; Eukaryota.
DR InParanoid; A9JSE7; -.
DR OrthoDB; 1451925at2759; -.
DR Reactome; R-XTR-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-XTR-6798695; Neutrophil degranulation.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000030275; Expressed in brain and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0004167; F:dopachrome isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0050178; F:phenylpyruvate tautomerase activity; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR Gene3D; 3.30.429.10; -; 1.
DR InterPro; IPR001398; Macrophage_inhib_fac.
DR InterPro; IPR019829; Macrophage_inhib_fac_CS.
DR InterPro; IPR014347; Tautomerase/MIF_sf.
DR PANTHER; PTHR11954; PTHR11954; 1.
DR Pfam; PF01187; MIF; 1.
DR SUPFAM; SSF55331; SSF55331; 1.
DR PROSITE; PS01158; MIF; 1.
PE 3: Inferred from homology;
KW Cytokine; Cytoplasm; Immunity; Inflammatory response; Innate immunity;
KW Isomerase; Reference proteome; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P14174"
FT CHAIN 2..115
FT /note="Macrophage migration inhibitory factor"
FT /id="PRO_0000344371"
FT ACT_SITE 2
FT /note="Proton acceptor; via imino nitrogen"
FT /evidence="ECO:0000250|UniProtKB:P34884"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14174"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14174"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14174"
SQ SEQUENCE 115 AA; 12524 MW; F8EEDB313BF97710 CRC64;
MPTFTVCTNV CRDSMPDTLL SDLTKLLAKA TGKPAEYIAI HIMPDQMMSF GDSTDPCAVC
SLSSIGKIGG PQNKSYSKLL CDYLTKQMNI PANRVYINFH DLNPANVGWN GSTFA