MIF_BOVIN
ID MIF_BOVIN Reviewed; 115 AA.
AC P80177; Q3T190; Q9XT46;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 6.
DT 03-AUG-2022, entry version 162.
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;
DE AltName: Full=p12A;
GN Name=MIF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-115.
RC TISSUE=Brain;
RX PubMed=7925355; DOI=10.1111/j.1432-1033.1994.00417.x;
RA Galat A., Riviere S., Bouet F., Menez A.;
RT "A diversified family of 12-kDa proteins with a high amino acid sequence
RT similarity to macrophage migration-inhibitory factor (MIF).";
RL Eur. J. Biochem. 224:417-421(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-104.
RC TISSUE=Corpus luteum;
RX PubMed=10727256; DOI=10.1095/biolreprod62.4.879;
RA Bove S.E., Petroff M.G., Nishibori M., Pate J.L.;
RT "Macrophage migration inhibitory factor in the bovine corpus luteum:
RT characterization of steady-state messenger ribonucleic acid and
RT immunohistochemical localization.";
RL Biol. Reprod. 62:879-885(2000).
RN [4]
RP PROTEIN SEQUENCE OF 2-40.
RC TISSUE=Brain;
RX PubMed=8458415; DOI=10.1016/0014-5793(93)80553-7;
RA Galat A., Riviere S., Bouet F.;
RT "Purification of macrophage migration inhibitory factor (MIF) from bovine
RT brain cytosol.";
RL FEBS Lett. 319:233-236(1993).
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. Counteracts the anti-inflammatory activity
CC of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome
CC tautomerase activity (in vitro), but the physiological substrate is not
CC known. It is not clear whether the tautomerase activity has any
CC physiological relevance, and whether it is important for cytokine
CC activity. {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 (By similarity). Interacts with CXCR2 extracellular
CC domain (By similarity). Interacts with the CD74 extracellular domain,
CC USO1, COPS5 and BNIPL (By similarity). {ECO:0000250|UniProtKB:P14174,
CC ECO:0000250|UniProtKB:P34884}.
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 bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens.
CC {ECO:0000250|UniProtKB:P14174}.
CC -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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DR EMBL; BC102066; AAI02067.1; -; mRNA.
DR EMBL; AF119571; AAD38354.1; -; mRNA.
DR PIR; S32394; S32394.
DR PIR; S48158; S48158.
DR RefSeq; NP_001028780.1; NM_001033608.1.
DR AlphaFoldDB; P80177; -.
DR SMR; P80177; -.
DR STRING; 9913.ENSBTAP00000009699; -.
DR PaxDb; P80177; -.
DR PeptideAtlas; P80177; -.
DR PRIDE; P80177; -.
DR Ensembl; ENSBTAT00000009699; ENSBTAP00000009699; ENSBTAG00000007375.
DR GeneID; 280858; -.
DR KEGG; bta:280858; -.
DR CTD; 4282; -.
DR VEuPathDB; HostDB:ENSBTAG00000007375; -.
DR VGNC; VGNC:49557; MIF.
DR eggNOG; KOG1759; Eukaryota.
DR GeneTree; ENSGT00940000155608; -.
DR HOGENOM; CLU_129906_1_1_1; -.
DR InParanoid; P80177; -.
DR OMA; YINFFDM; -.
DR OrthoDB; 1451925at2759; -.
DR TreeFam; TF313853; -.
DR SABIO-RK; P80177; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000007375; Expressed in retina and 108 other tissues.
DR ExpressionAtlas; P80177; baseline and differential.
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; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Cytokine; Cytoplasm; Direct protein sequencing; Immunity;
KW Inflammatory response; Innate immunity; Isomerase; Reference proteome;
KW Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7925355,
FT ECO:0000269|PubMed:8458415"
FT CHAIN 2..115
FT /note="Macrophage migration inhibitory factor"
FT /id="PRO_0000158061"
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 MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14174"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P34884"
FT CONFLICT 99..100
FT /note="FC -> YY (in Ref. 3; AAD38354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 115 AA; 12343 MW; 750242BFF691975E CRC64;
MPMFVVNTNV PRASVPDGLL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF GGSSEPCALC
SLHSIGKIGG AQNRSYSKLL CGLLTERLRI SPDRIYINFC DMNAANVGWN GSTFA
