P81529 (MIFH_TRISP) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 39.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Macrophage migration inhibitory factor homolog Short name=MIF EC=5.3.2.1 Alternative name(s): L-dopachrome isomerase L-dopachrome tautomerase EC=5.3.3.12 Phenylpyruvate tautomerase |
| Organism | Trichinella spiralis (Trichina worm) |
| Taxonomic identifier | 6334 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Nematoda › Enoplea › Trichocephalida › Trichinellidae › Trichinella![]() |
Protein attributes
| Sequence length | 114 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells. Ref.1 Ref.3 |
| Catalytic activity | L-dopachrome = 5,6-dihydroxyindole-2-carboxylate. Ref.1 Ref.3 |
| Subcellular location | |
| Developmental stage | Expressed in newborn larvae, precyst muscle larvae, postcyst muscle larvae and adult worms. Ref.2 |
| Induction | Inhibited by free fatty acids and haematin. Ref.3 |
| Sequence similarities | Belongs to the MIF family. |
| Biophysicochemical properties | Kinetic parameters: KM=144 µM for phenylpyruvate Ref.1 KM=783 µM for p-hydroxyphenylpyruvate Vmax=1026 µmol/min/mg enzyme toward phenylpyruvate Vmax=34.6 µmol/min/mg enzyme toward p-hydroxyphenylpyruvate |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Cytokine Isomerase |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular_component | extracellular space Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | dopachrome isomerase activity Inferred from electronic annotation. Source: EC phenylpyruvate tautomerase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.1 Ref.3 | ||||||||||||||||||||||||||||
| Chain | 2 – 114 | 113 | Macrophage migration inhibitory factor homolog | PRO_0000158074 | |||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||
| Active site | 2 | 1 | Proton acceptor; via imino nitrogen By similarity | ||||||||||||||||||||||||||||
| Binding site | 33 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||
| Binding site | 65 | 1 | Substrate; via amide nitrogen By similarity | ||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||
| Sequence conflict | 55 | 1 | K → N in CAB46354. Ref.1 | ||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| Beta strand | 3 – 10 | 8 | |||||||||||||||||||||||||||||
| Helix | 12 – 14 | 3 | |||||||||||||||||||||||||||||
| Helix | 19 – 31 | 13 | |||||||||||||||||||||||||||||
| Helix | 35 – 37 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 39 – 43 | 5 | |||||||||||||||||||||||||||||
| Beta strand | 47 – 50 | 4 | |||||||||||||||||||||||||||||
| Beta strand | 58 – 67 | 10 | |||||||||||||||||||||||||||||
| Helix | 70 – 88 | 19 | |||||||||||||||||||||||||||||
| Helix | 92 – 94 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 95 – 101 | 7 | |||||||||||||||||||||||||||||
| Helix | 104 – 106 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 107 – 109 | 3 | |||||||||||||||||||||||||||||
Sequences
References
| [1] | "Macrophage migration inhibitory factor of the parasitic nematode Trichinella spiralis." Tan T.H.P., Edgerton S.A.V., Kumari R., McAlister M.S.B., Roe S.M., Nagl S., Pearl L.H., Selkirk M.E., Bianco A.E., Totty N.F., Engwerda C., Gray C.A., Meyer D.J., Rowe S.M. Biochem. J. 357:373-383(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-31; 64-71 AND 104-107, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-114. Tissue: Larva. |
| [2] | "Molecular expression and characterization of a homologue of host cytokine macrophage migration inhibitory factor from Trichinella spp." Wu Z., Boonmars T., Nagano I., Nakada T., Takahashi Y. J. Parasitol. 89:507-515(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE. Strain: ISS314. |
| [3] | "Rapid purification and characterization of L-dopachrome-methyl-ester tautomerase (macrophage migration inhibitory factor) from Trichinella spiralis, Trichuris muris and Brugia pahangi." Pennock J.L., Behnke J.M., Bickle Q.D., Devaney E., Grencis R.K., Isaac R.E., Joshua G.W.P., Selkirk M.E., Zhang Y., Meyer D.J. Biochem. J. 335:495-498(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20, FUNCTION, CATALYTIC ACTIVITY, INDUCTION. Tissue: Larva. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AJ012740 mRNA. Translation: CAB46354.1. AY050661 mRNA. Translation: AAL12629.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P81529. | ||||||||||||
| SMR | P81529. Positions 2-114. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001398. Macrophage_inhib_fac. IPR014347. Tautomerase/MIF_sf. [Graphical view] | ||||||||||||
| PANTHER | PTHR11954. PTHR11954. 1 hit. | ||||||||||||
| Pfam | PF01187. MIF. 1 hit. [Graphical view] | ||||||||||||
| ProDom | PD004816. Macrophage_inhib_fac. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| SUPFAM | SSF55331. SSF55331. 1 hit. | ||||||||||||
| PROSITE | PS01158. MIF. False negative. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P81529. | ||||||||||||
Entry information
| Entry name | MIFH_TRISP | ||||||||
| Accession | Primary (citable) accession number: P81529 Secondary accession number(s): Q95UI8, Q9Y063 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
