DOPD_HUMAN
ID DOPD_HUMAN Reviewed; 118 AA.
AC P30046; B7Z522; O00774; O60787; Q13534;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=D-dopachrome decarboxylase;
DE EC=4.1.1.84 {ECO:0000269|PubMed:8267597, ECO:0000269|PubMed:9480844};
DE AltName: Full=D-dopachrome tautomerase;
DE AltName: Full=Phenylpyruvate tautomerase II;
GN Name=DDT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Thelin S., Panagopoulos I., Lassen C., Rosengren E., Aman P., Rorsman H.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PRO-2, AND TISSUE
RP SPECIFICITY.
RX PubMed=9480844; DOI=10.1006/bbrc.1998.8123;
RA Nishihira J., Fujinaga M., Kuriyama T., Suzuki M., Sugimoto H.,
RA Nakagawa A., Tanaka I., Sakai M.;
RT "Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal
RT proline is essential for enzyme activation.";
RL Biochem. Biophys. Res. Commun. 243:538-544(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rorsman H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Board P.G., Coggan M.A.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Pancreas;
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 [11]
RP PROTEIN SEQUENCE OF 2-22.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP PROTEIN SEQUENCE OF 2-12.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), AND SUBUNIT.
RX PubMed=10079069; DOI=10.1021/bi982184o;
RA Sugimoto H., Taniguchi M., Nakagawa A., Tanaka I., Suzuki M., Nishihira J.;
RT "Crystal structure of human D-dopachrome tautomerase, a homologue of
RT macrophage migration inhibitory factor, at 1.54-A resolution.";
RL Biochemistry 38:3268-3279(1999).
CC -!- FUNCTION: Tautomerization of D-dopachrome with decarboxylation to give
CC 5,6-dihydroxyindole (DHI). {ECO:0000269|PubMed:8267597,
CC ECO:0000269|PubMed:9480844}.
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, ECO:0000269|PubMed:9480844};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18442;
CC Evidence={ECO:0000305|PubMed:9480844};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.42 mM for D-dopachrome {ECO:0000269|PubMed:9480844};
CC Vmax=100 umol/min/mg enzyme for D-dopachrome
CC {ECO:0000269|PubMed:9480844};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10079069}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8267597}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30046-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30046-2; Sequence=VSP_056953;
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver and at lower levels
CC in the heart, lung and pancreas. {ECO:0000269|PubMed:8267597,
CC ECO:0000269|PubMed:9480844}.
CC -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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DR EMBL; U49785; AAB48546.1; -; mRNA.
DR EMBL; U84143; AAB41503.1; -; mRNA.
DR EMBL; Y11151; CAA72037.1; -; Genomic_DNA.
DR EMBL; AF012434; AAC77468.1; -; Genomic_DNA.
DR EMBL; AF012432; AAC77468.1; JOINED; Genomic_DNA.
DR EMBL; AF012433; AAC77468.1; JOINED; Genomic_DNA.
DR EMBL; AF058293; AAC13717.1; -; Genomic_DNA.
DR EMBL; CR456431; CAG30317.1; -; mRNA.
DR EMBL; AK298326; BAH12758.1; -; mRNA.
DR EMBL; AP000351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z84718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59622.1; -; Genomic_DNA.
DR EMBL; BC005971; AAH05971.1; -; mRNA.
DR EMBL; BC015508; AAH15508.1; -; mRNA.
DR CCDS; CCDS13820.1; -. [P30046-1]
DR PIR; G02438; G02438.
DR PIR; JE0162; JE0162.
DR RefSeq; NP_001077861.1; NM_001084392.1. [P30046-1]
DR RefSeq; NP_001346.1; NM_001355.3. [P30046-1]
DR PDB; 1DPT; X-ray; 1.54 A; A/B/C=2-118.
DR PDB; 3KAN; X-ray; 1.13 A; A/B/C=2-118.
DR PDB; 4Q3F; X-ray; 1.80 A; A/B/C=2-118.
DR PDB; 6C5F; X-ray; 1.40 A; A/B/C=2-118.
DR PDB; 7MRU; X-ray; 1.33 A; A/B/C=2-118.
DR PDB; 7MRV; X-ray; 1.57 A; A=2-118.
DR PDB; 7MSE; X-ray; 1.27 A; A/B/C=2-118.
DR PDB; 7MW7; X-ray; 1.10 A; A=1-118.
DR PDBsum; 1DPT; -.
DR PDBsum; 3KAN; -.
DR PDBsum; 4Q3F; -.
DR PDBsum; 6C5F; -.
DR PDBsum; 7MRU; -.
DR PDBsum; 7MRV; -.
DR PDBsum; 7MSE; -.
DR PDBsum; 7MW7; -.
DR AlphaFoldDB; P30046; -.
DR SMR; P30046; -.
DR BioGRID; 108018; 6.
DR BioGRID; 755774; 13.
DR IntAct; P30046; 4.
DR STRING; 9606.ENSP00000381386; -.
DR iPTMnet; P30046; -.
DR PhosphoSitePlus; P30046; -.
DR SwissPalm; P30046; -.
DR BioMuta; DDT; -.
DR DMDM; 2828192; -.
DR SWISS-2DPAGE; P30046; -.
DR UCD-2DPAGE; P30046; -.
DR EPD; P30046; -.
DR jPOST; P30046; -.
DR MassIVE; P30046; -.
DR MaxQB; P30046; -.
DR PaxDb; P30046; -.
DR PeptideAtlas; P30046; -.
DR PRIDE; P30046; -.
DR ProteomicsDB; 54626; -. [P30046-1]
DR ProteomicsDB; 6653; -.
DR TopDownProteomics; P30046-1; -. [P30046-1]
DR Antibodypedia; 35176; 394 antibodies from 29 providers.
DR DNASU; 1652; -.
DR Ensembl; ENST00000350608.7; ENSP00000215773.4; ENSG00000099977.15. [P30046-1]
DR Ensembl; ENST00000398344.9; ENSP00000381386.4; ENSG00000099977.15. [P30046-1]
DR Ensembl; ENST00000430101.2; ENSP00000399768.2; ENSG00000099977.15. [P30046-2]
DR Ensembl; ENST00000615721.3; ENSP00000481175.1; ENSG00000275003.3. [P30046-1]
DR Ensembl; ENST00000626871.2; ENSP00000486829.1; ENSG00000275003.3. [P30046-1]
DR Ensembl; ENST00000629401.2; ENSP00000486384.1; ENSG00000275003.3. [P30046-2]
DR GeneID; 1652; -.
DR KEGG; hsa:1652; -.
DR MANE-Select; ENST00000398344.9; ENSP00000381386.4; NM_001084392.3; NP_001077861.1.
DR UCSC; uc062cik.1; human. [P30046-1]
DR CTD; 1652; -.
DR DisGeNET; 1652; -.
DR GeneCards; DDT; -.
DR HGNC; HGNC:2732; DDT.
DR HPA; ENSG00000099977; Tissue enhanced (liver).
DR MIM; 602750; gene.
DR neXtProt; NX_P30046; -.
DR OpenTargets; ENSG00000099977; -.
DR PharmGKB; PA27197; -.
DR VEuPathDB; HostDB:ENSG00000099977; -.
DR eggNOG; KOG1759; Eukaryota.
DR GeneTree; ENSGT00940000156821; -.
DR HOGENOM; CLU_129906_2_0_1; -.
DR InParanoid; P30046; -.
DR PhylomeDB; P30046; -.
DR TreeFam; TF313853; -.
DR BRENDA; 4.1.1.84; 2681.
DR PathwayCommons; P30046; -.
DR SignaLink; P30046; -.
DR BioGRID-ORCS; 1652; 16 hits in 671 CRISPR screens.
DR ChiTaRS; DDT; human.
DR EvolutionaryTrace; P30046; -.
DR GeneWiki; DDT_(gene); -.
DR GenomeRNAi; 1652; -.
DR Pharos; P30046; Tbio.
DR PRO; PR:P30046; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P30046; protein.
DR Bgee; ENSG00000099977; Expressed in right lobe of liver and 95 other tissues.
DR ExpressionAtlas; P30046; baseline and differential.
DR Genevisible; P30046; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005126; F:cytokine receptor binding; IDA:BHF-UCL.
DR GO; GO:0033981; F:D-dopachrome decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0004167; F:dopachrome isomerase activity; TAS:ProtInc.
DR GO; GO:0050178; F:phenylpyruvate tautomerase activity; IDA:BHF-UCL.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA: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; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Lyase; Melanin biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:1286669"
FT CHAIN 2..118
FT /note="D-dopachrome decarboxylase"
FT /id="PRO_0000158070"
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 VAR_SEQ 96..118
FT /note="ILIRFFPLESWQIGKIGTVMTFL -> QVPGEVHGRLTE (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056953"
FT MUTAGEN 2
FT /note="P->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|Ref.1"
FT CONFLICT 3
FT /note="F -> G (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:7MW7"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:7MW7"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:7MW7"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:7MW7"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:7MW7"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:7MRU"
FT STRAND 58..70
FT /evidence="ECO:0007829|PDB:7MW7"
FT HELIX 71..89
FT /evidence="ECO:0007829|PDB:7MW7"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:7MW7"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:7MW7"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7MW7"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:7MRU"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:7MW7"
SQ SEQUENCE 118 AA; 12712 MW; 12FEF51908F342B7 CRC64;
MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL SGSTEPCAQL
SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF FPLESWQIGK IGTVMTFL
