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Macrophage migration inhibitory factor (MIF) (EC 5.3.2.1) (L-dopachrome isomerase) (L-dopachrome tautomerase) (EC 5.3.3.12) (Phenylpyruvate tautomerase) (p12A)

 MIF_BOVIN               Reviewed;         115 AA.
P80177; Q3T190; Q9XT46;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 6.
31-JAN-2018, entry version 141.
RecName: Full=Macrophage migration inhibitory factor;
Short=MIF;
EC=5.3.2.1;
AltName: Full=L-dopachrome isomerase;
AltName: Full=L-dopachrome tautomerase;
EC=5.3.3.12;
AltName: Full=Phenylpyruvate tautomerase;
AltName: Full=p12A;
Name=MIF;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 2-115.
TISSUE=Brain;
PubMed=7925355; DOI=10.1111/j.1432-1033.1994.00417.x;
Galat A., Riviere S., Bouet F., Menez A.;
"A diversified family of 12-kDa proteins with a high amino acid
sequence similarity to macrophage migration-inhibitory factor (MIF).";
Eur. J. Biochem. 224:417-421(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-104.
TISSUE=Corpus luteum;
PubMed=10727256; DOI=10.1095/biolreprod62.4.879;
Bove S.E., Petroff M.G., Nishibori M., Pate J.L.;
"Macrophage migration inhibitory factor in the bovine corpus luteum:
characterization of steady-state messenger ribonucleic acid and
immunohistochemical localization.";
Biol. Reprod. 62:879-885(2000).
[4]
PROTEIN SEQUENCE OF 2-40.
TISSUE=Brain;
PubMed=8458415; DOI=10.1016/0014-5793(93)80553-7;
Galat A., Riviere S., Bouet F.;
"Purification of macrophage migration inhibitory factor (MIF) from
bovine brain cytosol.";
FEBS Lett. 319:233-236(1993).
-!- FUNCTION: Pro-inflammatory cytokine. Involved in the innate immune
response to bacterial pathogens. The expression of MIF at sites of
inflammation suggests a role as mediator in regulating the
function of macrophages in host defense. Counteracts the anti-
inflammatory activity of glucocorticoids. Has phenylpyruvate
tautomerase and dopachrome tautomerase activity (in vitro), but
the physiological substrate is not known. It is not clear whether
the tautomerase activity has any physiological relevance, and
whether it is important for cytokine activity (By similarity).
{ECO:0000250|UniProtKB:P14174}.
-!- CATALYTIC ACTIVITY: Keto-phenylpyruvate = enol-phenylpyruvate.
-!- CATALYTIC ACTIVITY: L-dopachrome = 5,6-dihydroxyindole-2-
carboxylate.
-!- SUBUNIT: Homotrimer. Interacts with BNIPL (By similarity).
Interacts with the CD74 extracellular domain. Interacts with COPS5
and with the CXCR2 extracellular domain (By similarity).
{ECO:0000250|UniProtKB:P14174}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P14174}.
Cytoplasm {ECO:0000250|UniProtKB:P14174}. Note=Does not have a
cleavable signal sequence and is secreted via a specialized, non-
classical pathway. Secreted by macrophages upon stimulation by
bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens
(By similarity). {ECO:0000250|UniProtKB:P14174}.
-!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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EMBL; BC102066; AAI02067.1; -; mRNA.
EMBL; AF119571; AAD38354.1; -; mRNA.
PIR; S32394; S32394.
PIR; S48158; S48158.
RefSeq; NP_001028780.1; NM_001033608.1.
UniGene; Bt.15528; -.
ProteinModelPortal; P80177; -.
SMR; P80177; -.
STRING; 9913.ENSBTAP00000009699; -.
PaxDb; P80177; -.
PeptideAtlas; P80177; -.
PRIDE; P80177; -.
Ensembl; ENSBTAT00000009699; ENSBTAP00000009699; ENSBTAG00000007375.
GeneID; 280858; -.
KEGG; bta:280858; -.
CTD; 4282; -.
eggNOG; KOG1759; Eukaryota.
eggNOG; ENOG41122MF; LUCA.
GeneTree; ENSGT00840000129866; -.
HOGENOM; HOG000112325; -.
HOVERGEN; HBG003240; -.
InParanoid; P80177; -.
KO; K07253; -.
OMA; PDRIYIN; -.
OrthoDB; EOG091G0ZNJ; -.
TreeFam; TF313853; -.
Reactome; R-BTA-202733; Cell surface interactions at the vascular wall.
Reactome; R-BTA-6798695; Neutrophil degranulation.
SABIO-RK; P80177; -.
Proteomes; UP000009136; Chromosome 17.
Bgee; ENSBTAG00000007375; -.
ExpressionAtlas; P80177; baseline and differential.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0042056; F:chemoattractant activity; IEA:Ensembl.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0005126; F:cytokine receptor binding; IEA:Ensembl.
GO; GO:0004167; F:dopachrome isomerase activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0050178; F:phenylpyruvate tautomerase activity; IEA:UniProtKB-EC.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0007569; P:cell aging; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0090344; P:negative regulation of cell aging; IEA:Ensembl.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IEA:Ensembl.
GO; GO:0032269; P:negative regulation of cellular protein metabolic process; IEA:Ensembl.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IEA:Ensembl.
GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IEA:Ensembl.
GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0061081; P:positive regulation of myeloid leukocyte cytokine production involved in immune response; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0061078; P:positive regulation of prostaglandin secretion involved in immune response; IEA:Ensembl.
GO; GO:0010739; P:positive regulation of protein kinase A signaling; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:Ensembl.
GO; GO:0070207; P:protein homotrimerization; IEA:Ensembl.
Gene3D; 3.30.429.10; -; 1.
InterPro; IPR001398; Macrophage_inhib_fac.
InterPro; IPR019829; Macrophage_inhib_fac_CS.
InterPro; IPR014347; Tautomerase/MIF_sf.
PANTHER; PTHR11954; PTHR11954; 1.
Pfam; PF01187; MIF; 1.
ProDom; PD004816; Macrophage_inhib_fac; 1.
SUPFAM; SSF55331; SSF55331; 1.
PROSITE; PS01158; MIF; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytokine; Cytoplasm;
Direct protein sequencing; Immunity; Inflammatory response;
Innate immunity; Isomerase; Reference proteome; Secreted.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7925355,
ECO:0000269|PubMed:8458415}.
CHAIN 2 115 Macrophage migration inhibitory factor.
/FTId=PRO_0000158061.
ACT_SITE 2 2 Proton acceptor; via imino nitrogen.
{ECO:0000250}.
BINDING 33 33 Substrate. {ECO:0000250}.
BINDING 65 65 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 98 98 Substrate. {ECO:0000250}.
MOD_RES 78 78 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P14174}.
MOD_RES 78 78 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P34884}.
CONFLICT 99 100 FC -> YY (in Ref. 3; AAD38354).
{ECO:0000305}.
SEQUENCE 115 AA; 12343 MW; 750242BFF691975E CRC64;
MPMFVVNTNV PRASVPDGLL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF GGSSEPCALC
SLHSIGKIGG AQNRSYSKLL CGLLTERLRI SPDRIYINFC DMNAANVGWN GSTFA


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