Summary: Macrophage migration inhibitory factor (MIF)
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Macrophage migration inhibitory factor (MIF) Provide feedback
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Sun HW, Bernhagen J, Bucala R, Lolis E; , Proc Natl Acad Sci U S A 1996;93:5191-5196.: Crystal structure at 2.6-A resolution of human macrophage migration inhibitory factor. PUBMED:8643551 EPMC:8643551
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001398
Macrophage migration inhibitory factor (MIF) is a key regulatory cytokine within innate and adaptive immune responses, capable of promoting and modulating the magnitude of the response [PUBMED:15225126]. MIF is released from T-cells and macrophages, and acts within the neuroendocrine system. MIF is capable of tautomerase activity, although its biological function has not been fully characterised. It is induced by glucocorticoid and is capable of overriding the anti-inflammatory actions of glucocorticoid [PUBMED:16331703]. MIF regulates cytokine secretion and the expression of receptors involved in the immune response. It can be taken up into target cells in order to interact with intracellular signalling molecules, inhibiting p53 function, and/or activating components of the mitogen-activated protein kinase and Jun-activation domain-binding protein-1 (Jab-1) [PUBMED:15225126]. MIF has been linked to various inflammatory diseases, such as rheumatoid arthritis and atherosclerosis [PUBMED:16628200].
The MIF homologue D-dopachrome tautomerase (EC) is involved in detoxification through the conversion of dopaminechrome (and possibly norepinephrinechrome), the toxic quinine product of the neurotransmitter dopamine (and norepinephrine), to an indole derivative that can serve as a precursor to neuromelanin [PUBMED:10644007, PUBMED:10079069].
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This clan groups 5-(carboxymethyl)-2-hydroxymuconate isomerase (CHMI) and 4-oxalocrotonate tautomerase (4-OT) with macrophage inhibitory factor (MIF). Interestingly they all share an amino-terminal proline. Members of this clan for homotrimers .
The clan contains the following 6 members:CHMI DUF1904 MIF Tautomerase Tautomerase_2 Tautomerase_3
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Curation and family details
|Author:||Finn RD, Bateman A|
|Number in seed:||6|
|Number in full:||669|
|Average length of the domain:||108.50 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||78.19 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the MIF domain has been found. There are 152 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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