ID H0ZLV3_TAEGU Unreviewed; 522 AA.
AC H0ZLV3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=L-dopachrome tautomerase {ECO:0000256|ARBA:ARBA00039823};
DE EC=5.3.3.12 {ECO:0000256|ARBA:ARBA00038932};
DE AltName: Full=L-dopachrome Delta-isomerase {ECO:0000256|ARBA:ARBA00042019};
DE AltName: Full=Tyrosinase-related protein 2 {ECO:0000256|ARBA:ARBA00041443};
GN Name=DCT {ECO:0000313|Ensembl:ENSTGUP00000011576.1};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000011576.1, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000011576.1, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000011576.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate;
CC Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509;
CC EC=5.3.3.12; Evidence={ECO:0000256|ARBA:ARBA00036823};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037907}.
CC -!- SUBCELLULAR LOCATION: Melanosome membrane
CC {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004573}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR RefSeq; XP_002199385.1; XM_002199349.2.
DR AlphaFoldDB; H0ZLV3; -.
DR STRING; 59729.ENSTGUP00000011576; -.
DR Ensembl; ENSTGUT00000011701.2; ENSTGUP00000011576.1; ENSTGUG00000011227.2.
DR GeneID; 100230498; -.
DR KEGG; tgu:100230498; -.
DR CTD; 1638; -.
DR GeneTree; ENSGT00940000156856; -.
DR HOGENOM; CLU_038693_1_0_1; -.
DR InParanoid; H0ZLV3; -.
DR OMA; FFNRTCK; -.
DR OrthoDB; 70287at2759; -.
DR TreeFam; TF315865; -.
DR Proteomes; UP000007754; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004167; F:dopachrome isomerase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:0048066; P:developmental pigmentation; IEA:Ensembl.
DR GO; GO:0006583; P:melanin biosynthetic process from tyrosine; IEA:Ensembl.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0009637; P:response to blue light; IEA:Ensembl.
DR GO; GO:0021847; P:ventricular zone neuroblast division; IEA:Ensembl.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF4; L-DOPACHROME TAUTOMERASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..522
FT /note="L-dopachrome tautomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003547433"
FT TRANSMEM 471..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..230
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 391..402
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 522 AA; 59295 MW; 0B1D34B30AFDE99A CRC64;
MGALRWLFWA GLGYLSCCCP PQVQAQFPRA CMTVEALRLK RCCPALGTEP GNICGSLQGR
GRCEGVLADT QPWSGPYTLQ NVDDREWWPL KFFNHSCQCT GNFAGYNCGE CKFGWTGPEC
NRRKPAVVRK DIHALTAEER EQFFDALDRA KTAIHPDYVI ATQHWRSLLG PSGEEPQIAN
CSIYNYFVWL HYYSVRDTLL GPGRPFKGID FSHQGPAFVT WHRYHLLWLE RELQRLMGNE
SFALPYWNFA TGRNECDVCT DQLFGAPRPD DPGLINLSSR FSRWQVVCNS LDDYNRLVTL
CNGTDEGPLR RRPPHGSSEQ LPTVEDVRRC LSLQEFDRPP FFRNSSFSFR NALEGFDKPD
GALDSPMLSL HNLVHSFLNG TSALPHAAAN DPIFVVLHSF TDAIFDEWMK RFKPPDNAWP
EELAPIGHNR LYNMVPFFPP VTNQELFQTA EQLGYTYAID LPDSLDETQA WAVMVGSTIG
GVLTALAVLV LLLVLFQHRR HRRGFEPLMN VSFSPKKYMG EA
//