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P80177 (MIF_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage migration inhibitory factor

Short name=MIF
EC=5.3.2.1
Alternative name(s):
L-dopachrome isomerase
L-dopachrome tautomerase
EC=5.3.3.12
Phenylpyruvate tautomerase
p12A
Gene names
Name:MIF
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length115 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

Keto-phenylpyruvate = enol-phenylpyruvate.

L-dopachrome = 5,6-dihydroxyindole-2-carboxylate.

Subunit structure

Homotrimer. Interacts with BNIPL By similarity. Interacts with the CD74 extracellular domain. Interacts with COPS5 and with the CXCR2 extracellular domain By similarity.

Subcellular location

Secreted By similarity. Cytoplasm. 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.

Sequence similarities

Belongs to the MIF family.

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentCytoplasm
Secreted
   Molecular functionCytokine
Isomerase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

cell aging

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell aging

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

negative regulation of cellular protein metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

negative regulation of mature B cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of myeloid cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of arachidonic acid secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemokine (C-X-C motif) ligand 2 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of myeloid leukocyte cytokine production involved in immune response

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin secretion involved in immune response

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase A signaling

Inferred from electronic annotation. Source: Ensembl

prostaglandin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

protein homotrimerization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionchemoattractant activity

Inferred from electronic annotation. Source: Ensembl

dopachrome isomerase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phenylpyruvate tautomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.4
Chain2 – 115114Macrophage migration inhibitory factor
PRO_0000158061

Sites

Active site21Proton acceptor; via imino nitrogen By similarity
Binding site331Substrate By similarity
Binding site651Substrate; via amide nitrogen By similarity
Binding site981Substrate By similarity

Amino acid modifications

Modified residue781N6-acetyllysine; alternate By similarity
Modified residue781N6-succinyllysine; alternate By similarity

Experimental info

Sequence conflict99 – 1002FC → YY in AAD38354. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P80177 [UniParc].

Last modified January 23, 2007. Version 6.
Checksum: 750242BFF691975E

FASTA11512,343
        10         20         30         40         50         60 
MPMFVVNTNV PRASVPDGLL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF GGSSEPCALC 

        70         80         90        100        110 
SLHSIGKIGG AQNRSYSKLL CGLLTERLRI SPDRIYINFC DMNAANVGWN GSTFA 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[2]"A diversified family of 12-kDa proteins with a high amino acid sequence similarity to macrophage migration-inhibitory factor (MIF)."
Galat A., Riviere S., Bouet F., Menez A.
Eur. J. Biochem. 224:417-421(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-115.
Tissue: Brain.
[3]"Macrophage migration inhibitory factor in the bovine corpus luteum: characterization of steady-state messenger ribonucleic acid and immunohistochemical localization."
Bove S.E., Petroff M.G., Nishibori M., Pate J.L.
Biol. Reprod. 62:879-885(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-104.
Tissue: Corpus luteum.
[4]"Purification of macrophage migration inhibitory factor (MIF) from bovine brain cytosol."
Galat A., Riviere S., Bouet F.
FEBS Lett. 319:233-236(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-40.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC102066 mRNA. Translation: AAI02067.1.
AF119571 mRNA. Translation: AAD38354.1.
PIRS32394.
S48158.
RefSeqNP_001028780.1. NM_001033608.1.
UniGeneBt.15528.

3D structure databases

ProteinModelPortalP80177.
SMRP80177. Positions 1-115.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP80177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000009699; ENSBTAP00000009699; ENSBTAG00000007375.
GeneID280858.
KEGGbta:280858.

Organism-specific databases

CTD4282.

Phylogenomic databases

eggNOGNOG08790.
GeneTreeENSGT00730000111101.
HOGENOMHOG000112325.
HOVERGENHBG003240.
InParanoidP80177.
KOK07253.
OMAPDRIYIN.
OrthoDBEOG7GXPDN.
TreeFamTF313853.

Enzyme and pathway databases

SABIO-RKP80177.

Family and domain databases

InterProIPR001398. Macrophage_inhib_fac.
IPR019829. Macrophage_inhib_fac_CS.
IPR014347. Tautomerase/MIF_sf.
[Graphical view]
PANTHERPTHR11954. PTHR11954. 1 hit.
PfamPF01187. MIF. 1 hit.
[Graphical view]
ProDomPD004816. Macrophage_inhib_fac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF55331. SSF55331. 1 hit.
PROSITEPS01158. MIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805002.

Entry information

Entry nameMIF_BOVIN
AccessionPrimary (citable) accession number: P80177
Secondary accession number(s): Q3T190, Q9XT46
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 112 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families