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P30046 (DOPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Phenylpyruvate tautomerase II
Gene names
Name:DDT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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).

Catalytic activity

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

Subunit structure

Homotrimer. Ref.12

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the MIF family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9 Ref.10
Chain2 – 118117D-dopachrome decarboxylase
PRO_0000158070

Amino acid modifications

Modified residue21N-acetylproline By similarity
Modified residue331N6-acetyllysine By similarity

Experimental info

Sequence conflict31F → G AA sequence Ref.9

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P30046 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 12FEF51908F342B7

FASTA11812,712
        10         20         30         40         50         60 
MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL SGSTEPCAQL 

        70         80         90        100        110 
SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF FPLESWQIGK IGTVMTFL 

« Hide

References

« Hide 'large scale' references
[1]Thelin S., Panagopoulos I., Lassen C., Rosengren E., Aman P., Rorsman H.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation."
Nishihira J., Fujinaga M., Kuriyama T., Suzuki M., Sugimoto H., Nakagawa A., Tanaka I., Sakai M.
Biochem. Biophys. Res. Commun. 243:538-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Rorsman H.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]Board P.G., Coggan M.A.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Pancreas.
[9]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-22.
Tissue: Platelet.
[10]"Human liver protein map: a reference database established by microsequencing and gel comparison."
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12.
Tissue: Liver.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54-A resolution."
Sugimoto H., Taniguchi M., Nakagawa A., Tanaka I., Suzuki M., Nishihira J.
Biochemistry 38:3268-3279(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49785 mRNA. Translation: AAB48546.1.
U84143 mRNA. Translation: AAB41503.1.
Y11151 Genomic DNA. Translation: CAA72037.1.
AF012434, AF012432, AF012433 Genomic DNA. Translation: AAC77468.1.
AF058293 Genomic DNA. Translation: AAC13717.1.
CR456431 mRNA. Translation: CAG30317.1.
Z84718 Genomic DNA. No translation available.
BC005971 mRNA. Translation: AAH05971.1.
BC015508 mRNA. Translation: AAH15508.1.
CCDSCCDS13820.1.
PIRG02438.
JE0162.
RefSeqNP_001077861.1. NM_001084392.1.
NP_001346.1. NM_001355.3.
UniGeneHs.656723.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPTX-ray1.54A/B/C2-118[»]
3KANX-ray1.13A/B/C2-118[»]
ProteinModelPortalP30046.
SMRP30046. Positions 2-118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108018. 3 interactions.
IntActP30046. 1 interaction.
MINTMINT-5000166.
STRING9606.ENSP00000215773.

PTM databases

PhosphoSiteP30046.

Polymorphism databases

DMDM2828192.

2D gel databases

SWISS-2DPAGEP30046.
UCD-2DPAGEP30046.

Proteomic databases

MaxQBP30046.
PaxDbP30046.
PeptideAtlasP30046.
PRIDEP30046.

Protocols and materials databases

DNASU1652.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000350608; ENSP00000215773; ENSG00000099977.
ENST00000398344; ENSP00000381386; ENSG00000099977.
GeneID1652.
KEGGhsa:1652.
UCSCuc002zyz.4. human.

Organism-specific databases

CTD1652.
GeneCardsGC22M024313.
HGNCHGNC:2732. DDT.
HPAHPA049871.
MIM602750. gene.
neXtProtNX_P30046.
PharmGKBPA27197.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG284179.
HOGENOMHOG000112325.
HOVERGENHBG003240.
KOK10028.
OrthoDBEOG7GXPDN.
PhylomeDBP30046.
TreeFamTF313853.

Enzyme and pathway databases

BRENDA4.1.1.84. 2681.

Gene expression databases

ArrayExpressP30046.
BgeeP30046.
CleanExHS_DDT.
GenevestigatorP30046.

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

ChiTaRSDDT. human.
EvolutionaryTraceP30046.
GeneWikiDDT_(gene).
GenomeRNAi1652.
NextBio6800.
PROP30046.
SOURCESearch...

Entry information

Entry nameDOPD_HUMAN
AccessionPrimary (citable) accession number: P30046
Secondary accession number(s): O00774, O60787, Q13534
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM