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O35215 (DOPD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
D-dopachrome decarboxylase

EC=4.1.1.84
Alternative name(s):
D-dopachrome tautomerase
Gene names
Name:Ddt
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI) By similarity.

Catalytic activity

D-dopachrome = 5,6-dihydroxyindole + CO2.

Subunit structure

Homotrimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the MIF family.

Ontologies

Keywords
   Biological processMelanin biosynthesis
   Cellular componentCytoplasm
   Molecular functionLyase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processmelanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionD-dopachrome decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 118117D-dopachrome decarboxylase
PRO_0000158071

Amino acid modifications

Modified residue21N-acetylproline Ref.4

Secondary structure

........................ 118
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35215 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0440692D5413FC81

FASTA11813,077
        10         20         30         40         50         60 
MPFVELETNL PASRIPAGLE NRLCAATATI LDKPEDRVSV TIRPGMTLLM NKSTEPCAHL 

        70         80         90        100        110 
LVSSIGVVGT AEQNRTHSAS FFKFLTEELS LDQDRIVIRF FPLEAWQIGK KGTVMTFL 

« Hide

References

« Hide 'large scale' references
[1]"Conserved gene structure and genomic linkage for D-dopachrome tautomerase (DDT) and MIF."
Esumi N., Budarf M., Ciccarelli L., Sellinger B., Kozak C.A., Wistow G.
Mamm. Genome 9:753-757(1998) [PubMed: 9716662] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning of the mouse gene for D-dopachrome tautomerase."
Kuriyama T., Fujinaga M., Koda T., Nishihira J.
Biochim. Biophys. Acta 1388:506-512(1998) [PubMed: 9858785] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[4]Bienvenut W.V.
Submitted (JUL-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-37 AND 84-95, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT PRO-2, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF012431 Genomic DNA. Translation: AAC77467.1.
AF068199 Genomic DNA. Translation: AAC32825.1.
BC010753 mRNA. Translation: AAH10753.1.
IPIIPI00230034.
RefSeqNP_034157.1. NM_010027.1.
UniGeneMm.298947.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KERX-ray2.78A/B/C/D2-118[»]
ProteinModelPortalO35215.
SMRO35215. Positions 2-118.
ModBaseSearch...

Protein-protein interaction databases

STRINGO35215.

PTM databases

PhosphoSiteO35215.

2D gel databases

SWISS-2DPAGEO35215.
REPRODUCTION-2DPAGEO35215.
UCD-2DPAGEO35215.

Proteomic databases

PRIDEO35215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001716; ENSMUSP00000001716; ENSMUSG00000001666.
GeneID13202.
KEGGmmu:13202.

Organism-specific databases

CTD1652.
MGIMGI:1298381. Ddt.

Phylogenomic databases

eggNOGroNOG17526.
HOGENOMHBG629499.
HOVERGENHBG003240.
InParanoidO35215.
OMASMGKPRE.
OrthoDBEOG46T330.
PhylomeDBO35215.

Enzyme and pathway databases

BRENDA4.1.1.84. 3474.

Gene expression databases

ArrayExpressO35215.
BgeeO35215.
CleanExMM_DDT.
GenevestigatorO35215.
GermOnlineENSMUSG00000001666. Mus musculus.

Family and domain databases

InterProIPR001398. Macrophage_inhib_fac.
IPR019829. Macrophage_inhib_fac_CS.
IPR014347. Tautomerase.
[Graphical view]
Gene3DG3DSA:3.30.429.10. Tautomerase. 1 hit.
KOK10028.
PANTHERPTHR11954. MIF. 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

NextBio283354.
SOURCESearch...

Entry information

Entry nameDOPD_MOUSE
AccessionPrimary (citable) accession number: O35215
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families