ID A0A091FU06_9AVES Unreviewed; 520 AA.
AC A0A091FU06;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=N303_12337 {ECO:0000313|EMBL:KFO72481.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO72481.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO72481.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO72481.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL447346; KFO72481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FU06; -.
DR STRING; 55661.A0A091FU06; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
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:UP000053760};
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..520
FT /note="L-dopachrome tautomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001873476"
FT TRANSMEM 468..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 210..227
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 389..400
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 520 AA; 59087 MW; 44B82113DA764FDB CRC64;
MVTLRWLFWA GLGYLSCCYP PQVQAQFPRA CMTVDALRLK RCCPPLGTEP GNVCGSLQGR
GQCQEVQVDT QPWSGLYTLR NVDDRERWPL KFFNQSCRCT AGYNCGDCKF GWTGPDCNTR
KPPVVRKDIH SLTAEEREQF FDALDRAKTT IHPDYVIATQ HWLSLLGPTG AEPQIANCSI
YNYFVWLHYY SVRDTLLGPG RPFTAIDFSH QGPAFVTWHR YHLLLLERDL QRLMGNDSFA
LPYWNFATGR NECDVCTDQL FGASRPGDLG LISQSSRFSR WQIVCNSLDD YNRLVTLCNG
SDEGPLRRRL LEGSSEQLPT AEDVKKCLSL QEFDSPPFFR NSSFSFRNAL EGFNKPDGAL
NSPMLSLHNN LVPSFLNGTS VLPHAAANDP IFVVLHSFTD AIFDEWMKRF NPPDKAWPEE
LAPIGHNRLY NMVPFFPPVT NNELFQTAEE LGYTYAVDLP DSLEETQMWA VVVGSTIGGA
IIALTMLILL LVLFQHRRRR RGFEPLMNVS FSPKKYMEEA
//
