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Protein

Macrophage migration inhibitory factor homolog

Gene
N/A
Organism
Trichinella spiralis (Trichina worm)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.2 Publications

Catalytic activityi

L-dopachrome = 5,6-dihydroxyindole-2-carboxylate.
Keto-phenylpyruvate = enol-phenylpyruvate.

Kineticsi

  1. KM=144 µM for phenylpyruvate1 Publication
  2. KM=783 µM for p-hydroxyphenylpyruvate1 Publication
  1. Vmax=1026 µmol/min/mg enzyme toward phenylpyruvate1 Publication
  2. Vmax=34.6 µmol/min/mg enzyme toward p-hydroxyphenylpyruvate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Proton acceptor; via imino nitrogenBy similarity
Binding sitei33 – 331SubstrateBy similarity
Binding sitei65 – 651Substrate; via amide nitrogenBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage migration inhibitory factor homolog (EC:5.3.2.1)
Short name:
MIF
Alternative name(s):
L-dopachrome isomerase
L-dopachrome tautomerase (EC:5.3.3.12)
Phenylpyruvate tautomerase
OrganismiTrichinella spiralis (Trichina worm)
Taxonomic identifieri6334 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaEnopleaDorylaimiaTrichocephalidaTrichinellidaeTrichinella

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 114113Macrophage migration inhibitory factor homologPRO_0000158074Add
BLAST

Expressioni

Developmental stagei

Expressed in newborn larvae, precyst muscle larvae, postcyst muscle larvae and adult worms.1 Publication

Inductioni

Inhibited by free fatty acids and haematin.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi6334.EFV56343.

Structurei

Secondary structure

1
114
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi12 – 143Combined sources
Helixi19 – 3113Combined sources
Helixi35 – 373Combined sources
Beta strandi39 – 435Combined sources
Beta strandi47 – 504Combined sources
Beta strandi58 – 6710Combined sources
Helixi70 – 8819Combined sources
Helixi92 – 943Combined sources
Beta strandi95 – 1017Combined sources
Helixi104 – 1063Combined sources
Beta strandi107 – 1093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HFOX-ray1.65A/B/C/D/E/F2-114[»]
ProteinModelPortaliP81529.
SMRiP81529. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81529.

Family & Domainsi

Sequence similaritiesi

Belongs to the MIF family.Curated

Phylogenomic databases

eggNOGiKOG1759. Eukaryota.
ENOG41122MF. LUCA.

Family and domain databases

InterProiIPR001398. Macrophage_inhib_fac.
IPR014347. Tautomerase/MIF_sf.
[Graphical view]
PANTHERiPTHR11954. PTHR11954. 1 hit.
PfamiPF01187. MIF. 1 hit.
[Graphical view]
ProDomiPD004816. Macrophage_inhib_fac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF55331. SSF55331. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P81529-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIFTLNTNI KATDVPSDFL SSTSALVGNI LSKPGSYVAV HINTDQQLSF
60 70 80 90 100
GGSTKPAAFG TLMSIGGIEP SRNRDHSAKL FDHLNKKLGI PKNRMYIHFV
110
NLNGDDVGWN GTTF
Length:114
Mass (Da):12,337
Last modified:September 22, 2009 - v2
Checksum:i8B68B33C6309FAF1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551K → N in CAB46354 (PubMed:11439086).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012740 mRNA. Translation: CAB46354.1.
AY050661 mRNA. Translation: AAL12629.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012740 mRNA. Translation: CAB46354.1.
AY050661 mRNA. Translation: AAL12629.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HFOX-ray1.65A/B/C/D/E/F2-114[»]
ProteinModelPortaliP81529.
SMRiP81529. Positions 2-114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6334.EFV56343.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1759. Eukaryota.
ENOG41122MF. LUCA.

Miscellaneous databases

EvolutionaryTraceiP81529.

Family and domain databases

InterProiIPR001398. Macrophage_inhib_fac.
IPR014347. Tautomerase/MIF_sf.
[Graphical view]
PANTHERiPTHR11954. PTHR11954. 1 hit.
PfamiPF01187. MIF. 1 hit.
[Graphical view]
ProDomiPD004816. Macrophage_inhib_fac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF55331. SSF55331. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMIFH_TRISP
AccessioniPrimary (citable) accession number: P81529
Secondary accession number(s): Q95UI8, Q9Y063
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: September 22, 2009
Last modified: September 7, 2016
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.