[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/0014-5793(95)01041-C; PubMed=7589466 [NCBI, ExPASy, EBI, Israel, Japan] Zhang M., Aman P., Grubb A., Panagopoulos I., Hindemith A., Rosengren E., Rorsman H.; "Cloning and sequencing of a cDNA encoding rat D-dopachrome tautomerase."; FEBS Lett. 373:203-206(1995).
[2]	PROTEIN SEQUENCE OF 2-12. STRAIN=Sprague-Dawley; TISSUE=Liver; DOI=10.1006/bbrc.1993.2524; PubMed=8267597 [NCBI, ExPASy, EBI, Israel, Japan] Odh G., Hindemith A., Rosengren A.-M., Rosengren E., Rorsman H.; "Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole."; Biochem. Biophys. Res. Commun. 197:619-624(1993).
[3]	PROTEIN SEQUENCE OF 53-75; 84-95 AND 100-110, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (NOV-2006) to UniProtKB.

Comments

FUNCTION: Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).
CATALYTIC ACTIVITY: D-dopachrome = 5,6-dihydroxyindole + CO₂.
SUBUNIT: Homotrimer.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: In all organs tested, highest levels in liver.
SIMILARITY: Belongs to the MIF family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z36980; CAA85429.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00231963; -.

S68237; S68237.

NP_077045.1; -.

3D structure databases

HSSP

P30046; 1DPT. [HSSP ENTRY / PDB]

SMR

P80254; 2-118.

ModBase

P80254.

Enzyme and pathway databases

BRENDA

4.1.1.84; 248.

Organism-specific databases

RGD

61923; Ddt.

Gene expression databases

ArrayExpress

P80254; -.

GermOnline

ENSRNOG00000001239; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0033981;	Molecular function: D-dopachrome decarboxylase activity (inferred from electronic annotation from EC).
GO:0004167;	Molecular function: dopachrome isomerase activity (traceable author statement from RGD).
GO:0006954;	Biological process: inflammatory response (non-traceable author statement from RGD).
GO:0006583;	Biological process: melanin biosynthetic process from tyrosine (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001398; Macrophage_inhib_fac.
IPR019829; Macrophage_inhib_fac_CS.
IPR014347; Tautomerase.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.429.10; Tautomerase; 1.

PANTHER

PTHR11954; MIF; 1.

Pfam

PF01187; MIF; 1.
Pfam graphical view of domain structure.

ProDom

PD004816; MIF; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS01158; MIF; 1.

Proteomic databases

PRIDE

P80254; -.

Genome annotation databases

Ensembl

ENSRNOG00000001239; Rattus norvegicus. [Contig view]

GeneID

29318; -.

KEGG

rno:29318; -.

Phylogenomic databases

HOVERGEN

P80254; -.

OMA

P80254; ETNLPAS.

Other

608768; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Cytoplasm; Direct protein sequencing; Lyase; Melanin biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 118`	`117`	`D-dopachrome decarboxylase.`	`PRO_0000158072`
`MOD_RES`	`2 2`		`N-acetylproline (By similarity).`

Sequence information

Length: 118 AA [This is the length of the unprocessed precursor]

Molecular weight: 13133 Da [This is the MW of the unprocessed precursor]

CRC64: 9D841584907B8548 [This is a checksum on the sequence]

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

        70         80         90        100        110 
LISSIGVVGT AEQNRSHSSS FFKFLTEELS LDQDRIIIRF FPLEPWQIGK KGTVMTFL

P80254 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools