MIF_XENLA
ID MIF_XENLA Reviewed; 115 AA.
AC Q76BK2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS),
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=15024012; DOI=10.1074/jbc.m311416200;
RA Suzuki M., Takamura Y., Maeno M., Tochinai S., Iyaguchi D., Tanaka I.,
RA Nishihira J., Ishibashi T.;
RT "Xenopus laevis macrophage migration inhibitory factor is essential for
RT axis formation and neural development.";
RL J. Biol. Chem. 279:21406-21414(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) 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 (By similarity). Has phenylpyruvate
CC tautomerase and dopachrome tautomerase activity (in vitro), but the
CC physiological substrate is not known. It is not clear whether the
CC tautomerase activity has any physiological relevance, and whether it is
CC important for cytokine activity. Required for normal neural development
CC during embryogenesis. {ECO:0000250|UniProtKB:P14174,
CC ECO:0000269|PubMed:15024012}.
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:0000269|PubMed:15024012}.
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 -!- TISSUE SPECIFICITY: Ubiquitous. Detected throughout embryogenesis.
CC Detected in adult spleen, liver, kidney, heart, brain, intestine,
CC testis and lung. {ECO:0000269|PubMed:15024012}.
CC -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB111063; BAD02463.1; -; mRNA.
DR EMBL; BC097727; AAH97727.1; -; mRNA.
DR RefSeq; NP_001083650.1; NM_001090181.1.
DR PDB; 1UIZ; X-ray; 2.50 A; A/B/C/D=1-115.
DR PDBsum; 1UIZ; -.
DR AlphaFoldDB; Q76BK2; -.
DR SMR; Q76BK2; -.
DR MaxQB; Q76BK2; -.
DR DNASU; 399041; -.
DR GeneID; 399041; -.
DR KEGG; xla:399041; -.
DR CTD; 399041; -.
DR Xenbase; XB-GENE-487452; mif.L.
DR OrthoDB; 1451925at2759; -.
DR EvolutionaryTrace; Q76BK2; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 399041; Expressed in brain and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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 1: Evidence at protein level;
KW 3D-structure; Cytokine; Cytoplasm; Immunity; Inflammatory response;
KW Innate immunity; 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_0000344370"
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"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1UIZ"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1UIZ"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:1UIZ"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1UIZ"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1UIZ"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1UIZ"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:1UIZ"
FT HELIX 70..88
FT /evidence="ECO:0007829|PDB:1UIZ"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1UIZ"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1UIZ"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1UIZ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1UIZ"
SQ SEQUENCE 115 AA; 12500 MW; FE04E099E97B52BB CRC64;
MPVFTIRTNV CRDSVPDTLL SDLTKQLAKA TGKPAEYIAI HIVPDQIMSF GDSTDPCAVC
SLCSIGKIGG PQNKSYTKLL CDILTKQLNI PANRVYINYY DLNAANVGWN GSTFA
