DOPD_MOUSE
ID DOPD_MOUSE Reviewed; 118 AA.
AC O35215;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=D-dopachrome decarboxylase;
DE EC=4.1.1.84 {ECO:0000250|UniProtKB:P30046};
DE AltName: Full=D-dopachrome tautomerase;
GN Name=Ddt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9716662; DOI=10.1007/s003359900858;
RA Esumi N., Budarf M., Ciccarelli L., Sellinger B., Kozak C.A., Wistow G.;
RT "Conserved gene structure and genomic linkage for D-dopachrome tautomerase
RT (DDT) and MIF.";
RL Mamm. Genome 9:753-757(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9858785; DOI=10.1016/s0167-4838(98)00214-3;
RA Kuriyama T., Fujinaga M., Koda T., Nishihira J.;
RT "Cloning of the mouse gene for D-dopachrome tautomerase.";
RL Biochim. Biophys. Acta 1388:506-512(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-37 AND 84-95, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT PRO-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Tautomerization of D-dopachrome with decarboxylation to give
CC 5,6-dihydroxyindole (DHI). {ECO:0000250|UniProtKB:P30046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-dopachrome + H(+) = 5,6-dihydroxyindole + CO2;
CC Xref=Rhea:RHEA:18441, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:27404, ChEBI:CHEBI:58782; EC=4.1.1.84;
CC Evidence={ECO:0000250|UniProtKB:P30046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18442;
CC Evidence={ECO:0000250|UniProtKB:P30046};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P30046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30046}.
CC -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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DR EMBL; AF012431; AAC77467.1; -; Genomic_DNA.
DR EMBL; AF068199; AAC32825.1; -; Genomic_DNA.
DR EMBL; BC010753; AAH10753.1; -; mRNA.
DR CCDS; CCDS23930.1; -.
DR RefSeq; NP_034157.1; NM_010027.1.
DR PDB; 3KER; X-ray; 2.78 A; A/B/C/D=2-118.
DR PDBsum; 3KER; -.
DR AlphaFoldDB; O35215; -.
DR SMR; O35215; -.
DR BioGRID; 199082; 1.
DR STRING; 10090.ENSMUSP00000001716; -.
DR iPTMnet; O35215; -.
DR PhosphoSitePlus; O35215; -.
DR SwissPalm; O35215; -.
DR REPRODUCTION-2DPAGE; O35215; -.
DR SWISS-2DPAGE; O35215; -.
DR UCD-2DPAGE; O35215; -.
DR CPTAC; non-CPTAC-3458; -.
DR EPD; O35215; -.
DR jPOST; O35215; -.
DR PaxDb; O35215; -.
DR PeptideAtlas; O35215; -.
DR PRIDE; O35215; -.
DR ProteomicsDB; 279471; -.
DR DNASU; 13202; -.
DR Ensembl; ENSMUST00000001716; ENSMUSP00000001716; ENSMUSG00000001666.
DR GeneID; 13202; -.
DR KEGG; mmu:13202; -.
DR UCSC; uc007fra.1; mouse.
DR CTD; 1652; -.
DR MGI; MGI:1298381; Ddt.
DR VEuPathDB; HostDB:ENSMUSG00000001666; -.
DR eggNOG; KOG1759; Eukaryota.
DR GeneTree; ENSGT00940000156821; -.
DR InParanoid; O35215; -.
DR OMA; HSAKIFG; -.
DR OrthoDB; 1515400at2759; -.
DR PhylomeDB; O35215; -.
DR TreeFam; TF313853; -.
DR BRENDA; 4.1.1.84; 3474.
DR BioGRID-ORCS; 13202; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ddt; mouse.
DR EvolutionaryTrace; O35215; -.
DR PRO; PR:O35215; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O35215; protein.
DR Bgee; ENSMUSG00000001666; Expressed in right kidney and 71 other tissues.
DR ExpressionAtlas; O35215; baseline and differential.
DR Genevisible; O35215; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005126; F:cytokine receptor binding; ISO:MGI.
DR GO; GO:0033981; F:D-dopachrome decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0050178; F:phenylpyruvate tautomerase activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:BHF-UCL.
DR Gene3D; 3.30.429.10; -; 1.
DR InterPro; IPR001398; Macrophage_inhib_fac.
DR InterPro; IPR019829; Macrophage_inhib_fac_CS.
DR InterPro; IPR014347; Tautomerase/MIF_sf.
DR PANTHER; PTHR11954; PTHR11954; 1.
DR Pfam; PF01187; MIF; 1.
DR SUPFAM; SSF55331; SSF55331; 1.
DR PROSITE; PS01158; MIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Lyase;
KW Melanin biosynthesis; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..118
FT /note="D-dopachrome decarboxylase"
FT /id="PRO_0000158071"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80254"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:3KER"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3KER"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:3KER"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3KER"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3KER"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3KER"
FT STRAND 58..70
FT /evidence="ECO:0007829|PDB:3KER"
FT HELIX 71..89
FT /evidence="ECO:0007829|PDB:3KER"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3KER"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3KER"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3KER"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3KER"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3KER"
SQ SEQUENCE 118 AA; 13077 MW; 0440692D5413FC81 CRC64;
MPFVELETNL PASRIPAGLE NRLCAATATI LDKPEDRVSV TIRPGMTLLM NKSTEPCAHL
LVSSIGVVGT AEQNRTHSAS FFKFLTEELS LDQDRIVIRF FPLEAWQIGK KGTVMTFL
