P30046 (DOPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-dopachrome decarboxylase
EC=4.1.1.84

Alternative name(s):
D-dopachrome tautomerase
Phenylpyruvate tautomerase II

Gene names

Name:

DDT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	118 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 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

Keywords
Biological process	Melanin biosynthesis
Cellular component	Cytoplasm
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	D-dopachrome decarboxylase activity Inferred from electronic annotation. Source: EC dopachrome isomerase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9 Ref.10

Chain

2 – 118

117

D-dopachrome decarboxylase

PRO_0000158070

Amino acid modifications

Modified residue

2

1

N-acetylproline By similarity

Experimental info

Sequence conflict

3

1

F → G AA sequence Ref.9

Secondary structure

1

.

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118

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Helix

12 – 14

3

Helix

19 – 31

13

Helix

35 – 37

3

Beta strand

39 – 43

5

Beta strand

58 – 70

13

Helix

71 – 89

19

Helix

93 – 95

3

Beta strand

96 – 103

8

Helix

105 – 107

3

Helix

115 – 117

3

Sequences

	Sequence		Length	Mass (Da)
	P30046 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 12FEF51908F342B7	FASTA	118	12,712
	10 20 30 40 50 60 MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL SGSTEPCAQL 70 80 90 100 110 SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF FPLESWQIGK IGTVMTFL

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00293867.

PIR

G02438.
JE0162.

RefSeq

NP_001077861.1. NM_001084392.1.
NP_001346.1. NM_001355.3.

UniGene

Hs.656723.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DPT	X-ray	1.54	A/B/C	2-118	[»]
3KAN	X-ray	1.13	A/B/C	2-118	[»]

ProteinModelPortal

P30046.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30046. 1 interaction.

STRING

9606.ENSP00000215773.

PTM databases

PhosphoSite

P30046.

Polymorphism databases

DMDM

2828192.

2D gel databases

SWISS-2DPAGE

P30046.

UCD-2DPAGE

P30046.

Proteomic databases

PaxDb

P30046.

PeptideAtlas

P30046.

PRIDE

P30046.

Protocols and materials databases

DNASU

1652.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000350608; ENSP00000215773; ENSG00000099977.
ENST00000398344; ENSP00000381386; ENSG00000099977.

GeneID

1652.

KEGG

hsa:1652.

UCSC

uc002zyz.4. human.

Organism-specific databases

CTD

1652.

GeneCards

GC22M024313.

HGNC

HGNC:2732. DDT.

HPA

HPA049871.

MIM

602750. gene.

neXtProt

NX_P30046.

PharmGKB

PA27197.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG284179.

HOGENOM

HOG000112325.

HOVERGEN

HBG003240.

KO

K10028.

OrthoDB

EOG46T330.

PhylomeDB

P30046.

Enzyme and pathway databases

BRENDA

4.1.1.84. 2681.

Gene expression databases

ArrayExpress

P30046.

Bgee

P30046.

CleanEx

HS_DDT.

Genevestigator

P30046.

GermOnline

ENSG00000099977. Homo sapiens.

Family and domain databases

InterPro

IPR001398. Macrophage_inhib_fac.
IPR019829. Macrophage_inhib_fac_CS.
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. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DDT. human.

EvolutionaryTrace

P30046.

GenomeRNAi

1652.

NextBio

6800.

SOURCE

Search...

Entry information

Entry name

DOPD_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.