Macrophage migration inhibitory factor

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Macrophage migration inhibitory factor (MIF)
Macrophage migration inhibitory factor (MIF)
Identifiers
Symbol	MIF
Pfam	PF01187
InterPro	IPR001398
PROSITE	PDOC00892
SCOP2	1mif / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

MIF
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1CA7, 1CGQ, 1GCZ, 1GD0, 1GIF, 1LJT, 1MIF, 1P1G, 2OOH, 2OOW, 2OOZ, 3B9S, 3CE4, 3DJH, 3DJI, 3HOF, 3IJG, 3IJJ, 3JSF, 3JSG, 3JTU, 3L5P, 3L5R, 3L5S, 3L5T, 3L5U, 3L5V, 3SMB, 3SMC, 3U18, 4ETG, 4EUI, 4EVG, 4F2K, 4GRN, 4GRO, 4GRP, 4GRQ, 4GRR, 4GRU, 3WNR, 3WNS, 3WNT, 4K9G, 4OSF, 4OYQ, 4P01, 4P0H, 4WR8, 4WRB, 4PKZ, 4PLU, 4TRF, 4TRU, 4XX7, 4XX8, 5BS9, 5BSC, 5BSI, 5EIZ, 5HVV, 5CG4, 5J7Q, 5BSJ, 5HVT, 4PKK, 5B4O, 5HVS, 5J7P
Identifiers
Aliases	MIF, GIF, GLIF, Mmacrophage migration inhibitory factor (glycosylation-inhibiting factor), macrophage migration inhibitory factor
External IDs	OMIM: 153620; MGI: 96982; HomoloGene: 55655; GeneCards: MIF; OMA:MIF - orthologs
EC number	5.3.3.12
Gene location (Human)
Chr.	Chromosome 22 (human)
End	23,895,227 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	75,696,074 bp
RNA expression pattern
	Top expressed in
	anterior pituitary; ; right adrenal gland; ; renal cortex; ; left adrenal gland; ; superior frontal gyrus; ; Brodmann area 9; ; left adrenal cortex; ; C1 segment; ; right uterine tube; ; right adrenal cortex;
	Top expressed in
	embryo; ; embryo; ; otic placode; ; otic vesicle; ; somite; ; maxillary prominence; ; abdominal wall; ; mandibular prominence; ; epiblast; ; migratory enteric neural crest cell;
	More reference expression data
	n/a
Gene ontology
Molecular function	cytokine activity; isomerase activity; protein binding; chemoattractant activity; phenylpyruvate tautomerase activity; signaling receptor binding; dopachrome isomerase activity; protease binding; cytokine receptor binding; identical protein binding;
Cellular component	vesicle; myelin sheath; nucleoplasm; extracellular region; cell surface; extracellular exosome; cytoplasm; cytosol; secretory granule lumen; ficolin-1-rich granule lumen; extracellular space;
Biological process	positive regulation of protein phosphorylation; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; positive regulation of MAP kinase activity; carboxylic acid metabolic process; positive regulation of chemokine (C-X-C motif) ligand 2 production; immune system process; positive regulation of fibroblast proliferation; DNA damage response, signal transduction by p53 class mediator; negative regulation of apoptotic process; negative regulation of mature B cell apoptotic process; negative regulation of gene expression; positive regulation of peptidyl-serine phosphorylation; protein homotrimerization; positive regulation of lipopolysaccharide-mediated signaling pathway; cell surface receptor signaling pathway; negative regulation of DNA damage response, signal transduction by p53 class mediator; regulation of cell population proliferation; positive regulation of arachidonic acid secretion; positive regulation of B cell proliferation; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of prostaglandin secretion involved in immune response; prostaglandin biosynthetic process; innate immune response; negative regulation of myeloid cell apoptotic process; inflammatory response; cell population proliferation; positive regulation of phosphorylation; positive regulation of myeloid leukocyte cytokine production involved in immune response; leukocyte migration; regulation of macrophage activation; positive regulation of protein kinase A signaling; positive chemotaxis; neutrophil degranulation; interleukin-12-mediated signaling pathway; negative regulation of macrophage chemotaxis; positive regulation of tumor necrosis factor production; positive regulation of ERK1 and ERK2 cascade; regulation of signaling receptor activity;
	Sources:Amigo / QuickGO
Orthologs
	4282
	17319
	ENSG00000276701; ENSG00000240972
	ENSMUSG00000033307
	P14174
	P34884
	NM_002415
	NM_010798
	NP_002406; NP_002406.1
	NP_034928
	Wikidata
View/Edit Human	View/Edit Mouse

Macrophage migration inhibitory factor (MIF), also known as glycosylation-inhibiting factor (GIF), L-dopachrome isomerase, or phenylpyruvate tautomerase is a protein that in humans is encoded by the MIF gene. MIF is an important regulator of innate immunity. The MIF protein superfamily also includes a second member with functionally related properties, the D-dopachrome tautomerase (D-DT). CD74 is a surface receptor for MIF.

Bacterial antigens stimulate white blood cells to release MIF into the blood stream. The circulating MIF binds to CD74 on other immune cells to trigger an acute immune response. Hence, MIF is classified as an inflammatory cytokine. Furthermore, glucocorticoids also stimulate white blood cells to release MIF and hence MIF partially counteracts the inhibitory effects that glucocorticoids have on the immune system. Finally trauma activates the anterior pituitary gland to release MIF.