Full text data of DDT
DDT
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
D-dopachrome decarboxylase; 4.1.1.84 (D-dopachrome tautomerase; Phenylpyruvate tautomerase II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
D-dopachrome decarboxylase; 4.1.1.84 (D-dopachrome tautomerase; Phenylpyruvate tautomerase II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00293867
IPI00293867 D-dopachrome tautomerase Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI) soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00293867 D-dopachrome tautomerase Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI) soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P30046
ID DOPD_HUMAN Reviewed; 118 AA.
AC P30046; O00774; O60787; Q13534;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=D-dopachrome decarboxylase;
DE EC=4.1.1.84;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Thelin S., Panagopoulos I., Lassen C., Rosengren E., Aman P.,
RA Rorsman H.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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.,
RA Wistow G.;
RT "Conserved gene structure and genomic linkage for D-dopachrome
RT tautomerase (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].
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 GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
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 [11]
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.,
RA Buerckstuemmer T., 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 [12]
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.,
RA 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
CC give 5,6-dihydroxyindole (DHI).
CC -!- CATALYTIC ACTIVITY: D-dopachrome = 5,6-dihydroxyindole + CO(2).
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the MIF family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; Z84718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005971; AAH05971.1; -; mRNA.
DR EMBL; BC015508; AAH15508.1; -; mRNA.
DR PIR; G02438; G02438.
DR PIR; JE0162; JE0162.
DR RefSeq; NP_001077861.1; NM_001084392.1.
DR RefSeq; NP_001346.1; NM_001355.3.
DR UniGene; Hs.656723; -.
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 PDBsum; 1DPT; -.
DR PDBsum; 3KAN; -.
DR ProteinModelPortal; P30046; -.
DR SMR; P30046; 2-118.
DR IntAct; P30046; 1.
DR MINT; MINT-5000166; -.
DR STRING; 9606.ENSP00000215773; -.
DR PhosphoSite; P30046; -.
DR DMDM; 2828192; -.
DR SWISS-2DPAGE; P30046; -.
DR UCD-2DPAGE; P30046; -.
DR PaxDb; P30046; -.
DR PeptideAtlas; P30046; -.
DR PRIDE; P30046; -.
DR DNASU; 1652; -.
DR Ensembl; ENST00000350608; ENSP00000215773; ENSG00000099977.
DR Ensembl; ENST00000398344; ENSP00000381386; ENSG00000099977.
DR GeneID; 1652; -.
DR KEGG; hsa:1652; -.
DR UCSC; uc002zyz.4; human.
DR CTD; 1652; -.
DR GeneCards; GC22M024313; -.
DR HGNC; HGNC:2732; DDT.
DR HPA; HPA049871; -.
DR MIM; 602750; gene.
DR neXtProt; NX_P30046; -.
DR PharmGKB; PA27197; -.
DR eggNOG; NOG284179; -.
DR HOGENOM; HOG000112325; -.
DR HOVERGEN; HBG003240; -.
DR KO; K10028; -.
DR OrthoDB; EOG7GXPDN; -.
DR PhylomeDB; P30046; -.
DR BRENDA; 4.1.1.84; 2681.
DR ChiTaRS; DDT; human.
DR EvolutionaryTrace; P30046; -.
DR GeneWiki; DDT_(gene); -.
DR GenomeRNAi; 1652; -.
DR NextBio; 6800; -.
DR PRO; PR:P30046; -.
DR ArrayExpress; P30046; -.
DR Bgee; P30046; -.
DR CleanEx; HS_DDT; -.
DR Genevestigator; P30046; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033981; F:D-dopachrome decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004167; F:dopachrome isomerase activity; TAS:ProtInc.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
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 ProDom; PD004816; Macrophage_inhib_fac; 1.
DR SUPFAM; SSF55331; SSF55331; 1.
DR PROSITE; PS01158; MIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Lyase; Melanin biosynthesis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 118 D-dopachrome decarboxylase.
FT /FTId=PRO_0000158070.
FT MOD_RES 2 2 N-acetylproline (By similarity).
FT CONFLICT 3 3 F -> G (in Ref. 9; AA sequence).
FT STRAND 3 10
FT HELIX 12 14
FT HELIX 19 31
FT HELIX 35 37
FT STRAND 39 43
FT STRAND 58 70
FT HELIX 71 89
FT HELIX 93 95
FT STRAND 96 103
FT HELIX 105 107
FT HELIX 115 117
SQ SEQUENCE 118 AA; 12712 MW; 12FEF51908F342B7 CRC64;
MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL SGSTEPCAQL
SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF FPLESWQIGK IGTVMTFL
//
ID DOPD_HUMAN Reviewed; 118 AA.
AC P30046; O00774; O60787; Q13534;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=D-dopachrome decarboxylase;
DE EC=4.1.1.84;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA Thelin S., Panagopoulos I., Lassen C., Rosengren E., Aman P.,
RA Rorsman H.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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.,
RA Wistow G.;
RT "Conserved gene structure and genomic linkage for D-dopachrome
RT tautomerase (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].
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 GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
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 [11]
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.,
RA Buerckstuemmer T., 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 [12]
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.,
RA 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
CC give 5,6-dihydroxyindole (DHI).
CC -!- CATALYTIC ACTIVITY: D-dopachrome = 5,6-dihydroxyindole + CO(2).
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the MIF family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; Z84718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005971; AAH05971.1; -; mRNA.
DR EMBL; BC015508; AAH15508.1; -; mRNA.
DR PIR; G02438; G02438.
DR PIR; JE0162; JE0162.
DR RefSeq; NP_001077861.1; NM_001084392.1.
DR RefSeq; NP_001346.1; NM_001355.3.
DR UniGene; Hs.656723; -.
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 PDBsum; 1DPT; -.
DR PDBsum; 3KAN; -.
DR ProteinModelPortal; P30046; -.
DR SMR; P30046; 2-118.
DR IntAct; P30046; 1.
DR MINT; MINT-5000166; -.
DR STRING; 9606.ENSP00000215773; -.
DR PhosphoSite; P30046; -.
DR DMDM; 2828192; -.
DR SWISS-2DPAGE; P30046; -.
DR UCD-2DPAGE; P30046; -.
DR PaxDb; P30046; -.
DR PeptideAtlas; P30046; -.
DR PRIDE; P30046; -.
DR DNASU; 1652; -.
DR Ensembl; ENST00000350608; ENSP00000215773; ENSG00000099977.
DR Ensembl; ENST00000398344; ENSP00000381386; ENSG00000099977.
DR GeneID; 1652; -.
DR KEGG; hsa:1652; -.
DR UCSC; uc002zyz.4; human.
DR CTD; 1652; -.
DR GeneCards; GC22M024313; -.
DR HGNC; HGNC:2732; DDT.
DR HPA; HPA049871; -.
DR MIM; 602750; gene.
DR neXtProt; NX_P30046; -.
DR PharmGKB; PA27197; -.
DR eggNOG; NOG284179; -.
DR HOGENOM; HOG000112325; -.
DR HOVERGEN; HBG003240; -.
DR KO; K10028; -.
DR OrthoDB; EOG7GXPDN; -.
DR PhylomeDB; P30046; -.
DR BRENDA; 4.1.1.84; 2681.
DR ChiTaRS; DDT; human.
DR EvolutionaryTrace; P30046; -.
DR GeneWiki; DDT_(gene); -.
DR GenomeRNAi; 1652; -.
DR NextBio; 6800; -.
DR PRO; PR:P30046; -.
DR ArrayExpress; P30046; -.
DR Bgee; P30046; -.
DR CleanEx; HS_DDT; -.
DR Genevestigator; P30046; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033981; F:D-dopachrome decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004167; F:dopachrome isomerase activity; TAS:ProtInc.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
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 ProDom; PD004816; Macrophage_inhib_fac; 1.
DR SUPFAM; SSF55331; SSF55331; 1.
DR PROSITE; PS01158; MIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Lyase; Melanin biosynthesis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 118 D-dopachrome decarboxylase.
FT /FTId=PRO_0000158070.
FT MOD_RES 2 2 N-acetylproline (By similarity).
FT CONFLICT 3 3 F -> G (in Ref. 9; AA sequence).
FT STRAND 3 10
FT HELIX 12 14
FT HELIX 19 31
FT HELIX 35 37
FT STRAND 39 43
FT STRAND 58 70
FT HELIX 71 89
FT HELIX 93 95
FT STRAND 96 103
FT HELIX 105 107
FT HELIX 115 117
SQ SEQUENCE 118 AA; 12712 MW; 12FEF51908F342B7 CRC64;
MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL SGSTEPCAQL
SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF FPLESWQIGK IGTVMTFL
//
MIM
602750
*RECORD*
*FIELD* NO
602750
*FIELD* TI
*602750 D-DOPACHROME TAUTOMERASE; DDT
*FIELD* TX
DESCRIPTION
D-dopachrome tautomerase (DDT) converts D-dopachrome into
read more5,6-dihydroxyindole (summary by Nishihira et al., 1998).
CLONING
By screening a liver library with a rat D-dopachrome tautomerase cDNA,
Nishihira et al. (1998) identified cDNAs encoding human DDT. The
sequence of the predicted 118-amino acid DDT protein is 80% identical to
that of the rat protein. The molecular mass of recombinant DDT expressed
in bacterial cells was 13 kD by SDS-PAGE. Northern blot analysis
revealed that DDT was expressed as a 0.6-kb mRNA in all tissues tested,
with the strongest expression in liver.
GENE FUNCTION
Using site-directed mutagenesis, Nishihira et al. (1998) showed that the
N-terminal proline is essential for D-dopachrome tautomerization.
GENE STRUCTURE
Esumi et al. (1998) found that the DDT gene in human and mouse is
identical in exon structure to the MIF gene (153620). Both genes have 2
introns that are located at equivalent positions relative to a 2-fold
repeat in protein structure. Although in similar positions, the introns
are in different phases relative to the open reading frame. Other
members of this superfamily exist in nematodes and a plant, and a
related gene in C. elegans shares an intron position with MIF and DDT.
MAPPING
In addition to similarities in structure, the genes for DDT and MIF are
closely linked on human chromosome 22 and mouse chromosome 10. Esumi et
al. (1998) demonstrated the close linkage by anaphase fluorescence in
situ hybridization in the human. The DDT gene was mapped in the mouse by
interspecific backcross analysis.
*FIELD* RF
1. Esumi, N.; Budarf, M.; Ciccarelli, L.; Sellinger, B.; Kozak, C.
A.; Wistow, G.: Conserved gene structure and genomic linkage for
D-dopachrome tautomerase (DDT) and MIF. Mammalian Genome 9: 753-757,
1998.
2. Nishihira, J.; Fujinaga, M.; Kuriyama, T.; Suzuki, M.; Sugimoto,
H.; Nakagawa, A.; Tanaka, I.; Sakai, M.: Molecular cloning of human
D-dopachrome tautomerase cDNA: N-terminal proline is essential for
enzyme activation. Biochem. Biophys. Res. Commun. 243: 538-544,
1998.
*FIELD* CN
Victor A. McKusick - updated: 9/18/1998
*FIELD* CD
Rebekah S. Rasooly: 6/24/1998
*FIELD* ED
carol: 06/18/2012
carol: 6/12/2012
carol: 9/23/1998
dkim: 9/23/1998
terry: 9/18/1998
alopez: 6/24/1998
*RECORD*
*FIELD* NO
602750
*FIELD* TI
*602750 D-DOPACHROME TAUTOMERASE; DDT
*FIELD* TX
DESCRIPTION
D-dopachrome tautomerase (DDT) converts D-dopachrome into
read more5,6-dihydroxyindole (summary by Nishihira et al., 1998).
CLONING
By screening a liver library with a rat D-dopachrome tautomerase cDNA,
Nishihira et al. (1998) identified cDNAs encoding human DDT. The
sequence of the predicted 118-amino acid DDT protein is 80% identical to
that of the rat protein. The molecular mass of recombinant DDT expressed
in bacterial cells was 13 kD by SDS-PAGE. Northern blot analysis
revealed that DDT was expressed as a 0.6-kb mRNA in all tissues tested,
with the strongest expression in liver.
GENE FUNCTION
Using site-directed mutagenesis, Nishihira et al. (1998) showed that the
N-terminal proline is essential for D-dopachrome tautomerization.
GENE STRUCTURE
Esumi et al. (1998) found that the DDT gene in human and mouse is
identical in exon structure to the MIF gene (153620). Both genes have 2
introns that are located at equivalent positions relative to a 2-fold
repeat in protein structure. Although in similar positions, the introns
are in different phases relative to the open reading frame. Other
members of this superfamily exist in nematodes and a plant, and a
related gene in C. elegans shares an intron position with MIF and DDT.
MAPPING
In addition to similarities in structure, the genes for DDT and MIF are
closely linked on human chromosome 22 and mouse chromosome 10. Esumi et
al. (1998) demonstrated the close linkage by anaphase fluorescence in
situ hybridization in the human. The DDT gene was mapped in the mouse by
interspecific backcross analysis.
*FIELD* RF
1. Esumi, N.; Budarf, M.; Ciccarelli, L.; Sellinger, B.; Kozak, C.
A.; Wistow, G.: Conserved gene structure and genomic linkage for
D-dopachrome tautomerase (DDT) and MIF. Mammalian Genome 9: 753-757,
1998.
2. Nishihira, J.; Fujinaga, M.; Kuriyama, T.; Suzuki, M.; Sugimoto,
H.; Nakagawa, A.; Tanaka, I.; Sakai, M.: Molecular cloning of human
D-dopachrome tautomerase cDNA: N-terminal proline is essential for
enzyme activation. Biochem. Biophys. Res. Commun. 243: 538-544,
1998.
*FIELD* CN
Victor A. McKusick - updated: 9/18/1998
*FIELD* CD
Rebekah S. Rasooly: 6/24/1998
*FIELD* ED
carol: 06/18/2012
carol: 6/12/2012
carol: 9/23/1998
dkim: 9/23/1998
terry: 9/18/1998
alopez: 6/24/1998