DOPD_RAT
ID DOPD_RAT Reviewed; 118 AA.
AC P80254;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=D-dopachrome decarboxylase;
DE EC=4.1.1.84 {ECO:0000269|PubMed:8267597};
DE AltName: Full=D-dopachrome tautomerase;
GN Name=Ddt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7589466; DOI=10.1016/0014-5793(95)01041-c;
RA Zhang M., Aman P., Grubb A., Panagopoulos I., Hindemith A., Rosengren E.,
RA Rorsman H.;
RT "Cloning and sequencing of a cDNA encoding rat D-dopachrome tautomerase.";
RL FEBS Lett. 373:203-206(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-12, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8267597; DOI=10.1006/bbrc.1993.2524;
RA Odh G., Hindemith A., Rosengren A.-M., Rosengren E., Rorsman H.;
RT "Isolation of a new tautomerase monitored by the conversion of D-dopachrome
RT to 5,6-dihydroxyindole.";
RL Biochem. Biophys. Res. Commun. 197:619-624(1993).
RN [3]
RP PROTEIN SEQUENCE OF 53-75; 84-95 AND 100-110, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Tautomerization of D-dopachrome with decarboxylation to give
CC 5,6-dihydroxyindole (DHI). {ECO:0000269|PubMed:8267597}.
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:0000269|PubMed:8267597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18442;
CC Evidence={ECO:0000305|PubMed:8267597};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for D-dopachrome {ECO:0000269|PubMed:8267597};
CC Vmax=0.5 mmol/min/mg enzyme for D-dopachrome
CC {ECO:0000269|PubMed:8267597};
CC pH dependence:
CC Optimum pH is 6-9. {ECO:0000269|PubMed:8267597};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:8267597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8267597}.
CC -!- TISSUE SPECIFICITY: In all organs tested, highest levels in liver.
CC {ECO:0000269|PubMed:8267597}.
CC -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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DR EMBL; Z36980; CAA85429.1; -; mRNA.
DR PIR; S68237; S68237.
DR RefSeq; NP_077045.1; NM_024131.1.
DR AlphaFoldDB; P80254; -.
DR SMR; P80254; -.
DR STRING; 10116.ENSRNOP00000001664; -.
DR iPTMnet; P80254; -.
DR PhosphoSitePlus; P80254; -.
DR SwissPalm; P80254; -.
DR jPOST; P80254; -.
DR PaxDb; P80254; -.
DR PRIDE; P80254; -.
DR Ensembl; ENSRNOT00000119257; ENSRNOP00000079844; ENSRNOG00000068887.
DR GeneID; 29318; -.
DR KEGG; rno:29318; -.
DR UCSC; RGD:61923; rat.
DR CTD; 1652; -.
DR RGD; 61923; Ddt.
DR eggNOG; KOG1759; Eukaryota.
DR GeneTree; ENSGT00940000156821; -.
DR HOGENOM; CLU_129906_2_0_1; -.
DR InParanoid; P80254; -.
DR OMA; HSAKIFG; -.
DR OrthoDB; 1515400at2759; -.
DR PhylomeDB; P80254; -.
DR TreeFam; TF313853; -.
DR BRENDA; 4.1.1.84; 5301.
DR BRENDA; 5.3.3.12; 5301.
DR PRO; PR:P80254; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000001239; Expressed in liver and 20 other tissues.
DR ExpressionAtlas; P80254; baseline and differential.
DR Genevisible; P80254; RN.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005126; F:cytokine receptor binding; ISO:RGD.
DR GO; GO:0033981; F:D-dopachrome decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0004167; F:dopachrome isomerase activity; TAS:RGD.
DR GO; GO:0050178; F:phenylpyruvate tautomerase activity; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; NAS:RGD.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
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 Acetylation; Cytoplasm; Direct protein sequencing; Lyase;
KW Melanin biosynthesis; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8267597"
FT CHAIN 2..118
FT /note="D-dopachrome decarboxylase"
FT /id="PRO_0000158072"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:O35215"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35215"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 118 AA; 13133 MW; 9D841584907B8548 CRC64;
MPFVELETNL PASRIPAGLE NRLCAATATI LDKPEDRVSV TIRPGMTLLM NKSTEPCAHL
LISSIGVVGT AEQNRSHSSS FFKFLTEELS LDQDRIIIRF FPLEPWQIGK KGTVMTFL
