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P30046

- DOPD_HUMAN

UniProt

P30046 - DOPD_HUMAN

Protein

D-dopachrome decarboxylase

Gene

DDT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).

    Catalytic activityi

    D-dopachrome = 5,6-dihydroxyindole + CO2.

    GO - Molecular functioni

    1. D-dopachrome decarboxylase activity Source: UniProtKB-EC
    2. dopachrome isomerase activity Source: ProtInc

    GO - Biological processi

    1. melanin biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Melanin biosynthesis

    Enzyme and pathway databases

    BRENDAi4.1.1.84. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-dopachrome decarboxylase (EC:4.1.1.84)
    Alternative name(s):
    D-dopachrome tautomerase
    Phenylpyruvate tautomerase II
    Gene namesi
    Name:DDT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:2732. DDT.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27197.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 118117D-dopachrome decarboxylasePRO_0000158070Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylprolineBy similarity
    Modified residuei33 – 331N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30046.
    PaxDbiP30046.
    PeptideAtlasiP30046.
    PRIDEiP30046.

    2D gel databases

    SWISS-2DPAGEP30046.
    UCD-2DPAGEP30046.

    PTM databases

    PhosphoSiteiP30046.

    Expressioni

    Gene expression databases

    ArrayExpressiP30046.
    BgeeiP30046.
    CleanExiHS_DDT.
    GenevestigatoriP30046.

    Organism-specific databases

    HPAiHPA049871.

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    BioGridi108018. 3 interactions.
    IntActiP30046. 1 interaction.
    MINTiMINT-5000166.
    STRINGi9606.ENSP00000215773.

    Structurei

    Secondary structure

    1
    118
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Helixi12 – 143
    Helixi19 – 3113
    Helixi35 – 373
    Beta strandi39 – 435
    Beta strandi58 – 7013
    Helixi71 – 8919
    Helixi93 – 953
    Beta strandi96 – 1038
    Helixi105 – 1073
    Helixi115 – 1173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DPTX-ray1.54A/B/C2-118[»]
    3KANX-ray1.13A/B/C2-118[»]
    4Q3FX-ray1.80A/B/C2-118[»]
    ProteinModelPortaliP30046.
    SMRiP30046. Positions 2-118.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30046.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MIF family.Curated

    Phylogenomic databases

    eggNOGiNOG284179.
    HOGENOMiHOG000112325.
    HOVERGENiHBG003240.
    KOiK10028.
    OrthoDBiEOG7GXPDN.
    PhylomeDBiP30046.
    TreeFamiTF313853.

    Family and domain databases

    InterProiIPR001398. Macrophage_inhib_fac.
    IPR019829. Macrophage_inhib_fac_CS.
    IPR014347. Tautomerase/MIF_sf.
    [Graphical view]
    PANTHERiPTHR11954. PTHR11954. 1 hit.
    PfamiPF01187. MIF. 1 hit.
    [Graphical view]
    ProDomiPD004816. Macrophage_inhib_fac. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF55331. SSF55331. 1 hit.
    PROSITEiPS01158. MIF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P30046-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL    50
    SGSTEPCAQL SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF 100
    FPLESWQIGK IGTVMTFL 118
    Length:118
    Mass (Da):12,712
    Last modified:January 23, 2007 - v3
    Checksum:i12FEF51908F342B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31F → G AA sequence (PubMed:12665801)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49785 mRNA. Translation: AAB48546.1.
    U84143 mRNA. Translation: AAB41503.1.
    Y11151 Genomic DNA. Translation: CAA72037.1.
    AF012434, AF012432, AF012433 Genomic DNA. Translation: AAC77468.1.
    AF058293 Genomic DNA. Translation: AAC13717.1.
    CR456431 mRNA. Translation: CAG30317.1.
    Z84718 Genomic DNA. No translation available.
    BC005971 mRNA. Translation: AAH05971.1.
    BC015508 mRNA. Translation: AAH15508.1.
    CCDSiCCDS13820.1.
    PIRiG02438.
    JE0162.
    RefSeqiNP_001077861.1. NM_001084392.1.
    NP_001346.1. NM_001355.3.
    UniGeneiHs.656723.

    Genome annotation databases

    EnsembliENST00000350608; ENSP00000215773; ENSG00000099977.
    ENST00000398344; ENSP00000381386; ENSG00000099977.
    GeneIDi1652.
    KEGGihsa:1652.
    UCSCiuc002zyz.4. human.

    Polymorphism databases

    DMDMi2828192.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49785 mRNA. Translation: AAB48546.1 .
    U84143 mRNA. Translation: AAB41503.1 .
    Y11151 Genomic DNA. Translation: CAA72037.1 .
    AF012434 , AF012432 , AF012433 Genomic DNA. Translation: AAC77468.1 .
    AF058293 Genomic DNA. Translation: AAC13717.1 .
    CR456431 mRNA. Translation: CAG30317.1 .
    Z84718 Genomic DNA. No translation available.
    BC005971 mRNA. Translation: AAH05971.1 .
    BC015508 mRNA. Translation: AAH15508.1 .
    CCDSi CCDS13820.1.
    PIRi G02438.
    JE0162.
    RefSeqi NP_001077861.1. NM_001084392.1.
    NP_001346.1. NM_001355.3.
    UniGenei Hs.656723.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DPT X-ray 1.54 A/B/C 2-118 [» ]
    3KAN X-ray 1.13 A/B/C 2-118 [» ]
    4Q3F X-ray 1.80 A/B/C 2-118 [» ]
    ProteinModelPortali P30046.
    SMRi P30046. Positions 2-118.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108018. 3 interactions.
    IntActi P30046. 1 interaction.
    MINTi MINT-5000166.
    STRINGi 9606.ENSP00000215773.

    PTM databases

    PhosphoSitei P30046.

    Polymorphism databases

    DMDMi 2828192.

    2D gel databases

    SWISS-2DPAGE P30046.
    UCD-2DPAGE P30046.

    Proteomic databases

    MaxQBi P30046.
    PaxDbi P30046.
    PeptideAtlasi P30046.
    PRIDEi P30046.

    Protocols and materials databases

    DNASUi 1652.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000350608 ; ENSP00000215773 ; ENSG00000099977 .
    ENST00000398344 ; ENSP00000381386 ; ENSG00000099977 .
    GeneIDi 1652.
    KEGGi hsa:1652.
    UCSCi uc002zyz.4. human.

    Organism-specific databases

    CTDi 1652.
    GeneCardsi GC22M024313.
    HGNCi HGNC:2732. DDT.
    HPAi HPA049871.
    MIMi 602750. gene.
    neXtProti NX_P30046.
    PharmGKBi PA27197.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG284179.
    HOGENOMi HOG000112325.
    HOVERGENi HBG003240.
    KOi K10028.
    OrthoDBi EOG7GXPDN.
    PhylomeDBi P30046.
    TreeFami TF313853.

    Enzyme and pathway databases

    BRENDAi 4.1.1.84. 2681.

    Miscellaneous databases

    ChiTaRSi DDT. human.
    EvolutionaryTracei P30046.
    GeneWikii DDT_(gene).
    GenomeRNAii 1652.
    NextBioi 6800.
    PROi P30046.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30046.
    Bgeei P30046.
    CleanExi HS_DDT.
    Genevestigatori P30046.

    Family and domain databases

    InterProi IPR001398. Macrophage_inhib_fac.
    IPR019829. Macrophage_inhib_fac_CS.
    IPR014347. Tautomerase/MIF_sf.
    [Graphical view ]
    PANTHERi PTHR11954. PTHR11954. 1 hit.
    Pfami PF01187. MIF. 1 hit.
    [Graphical view ]
    ProDomi PD004816. Macrophage_inhib_fac. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF55331. SSF55331. 1 hit.
    PROSITEi PS01158. MIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Thelin S., Panagopoulos I., Lassen C., Rosengren E., Aman P., Rorsman H.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation."
      Nishihira J., Fujinaga M., Kuriyama T., Suzuki M., Sugimoto H., Nakagawa A., Tanaka I., Sakai M.
      Biochem. Biophys. Res. Commun. 243:538-544(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Rorsman H.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Conserved gene structure and genomic linkage for D-dopachrome tautomerase (DDT) and MIF."
      Esumi N., Budarf M., Ciccarelli L., Sellinger B., Kozak C.A., Wistow G.
      Mamm. Genome 9:753-757(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Board P.G., Coggan M.A.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain and Pancreas.
    9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-22.
      Tissue: Platelet.
    10. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12.
      Tissue: Liver.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54-A resolution."
      Sugimoto H., Taniguchi M., Nakagawa A., Tanaka I., Suzuki M., Nishihira J.
      Biochemistry 38:3268-3279(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiDOPD_HUMAN
    AccessioniPrimary (citable) accession number: P30046
    Secondary accession number(s): O00774, O60787, Q13534
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3