ID A0A093H736_STRCA Unreviewed; 522 AA.
AC A0A093H736;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=N308_03364 {ECO:0000313|EMBL:KFV77476.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV77476.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV77476.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV77476.1};
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; KL205941; KFV77476.1; -; Genomic_DNA.
DR RefSeq; XP_009665669.1; XM_009667374.1.
DR AlphaFoldDB; A0A093H736; -.
DR STRING; 441894.ENSSCUP00000004626; -.
DR Ensembl; ENSSCUT00000006129; ENSSCUP00000004626; ENSSCUG00000003418.
DR GeneID; 104139288; -.
DR KEGG; scam:104139288; -.
DR CTD; 1638; -.
DR OrthoDB; 70287at2759; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
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:UP000053584};
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_5001886875"
FT TRANSMEM 470..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; 59117 MW; 9D652BB6209AA4D4 CRC64;
MGSQGRLFWA VLGYMSCCCP PRVETQFPRV CMTVEALRLK RCCPALGLEP SNVCGMLQGK
GQCQAVHVDA QPWSGPYTLR NVDDREQWPL KFFNQSCQCT GNFAGYNCGD CKFGWTGPDC
NERKPPVVRK NIHSLTAEER EQFFDALHRA KTTIHPDYVI ATQHWMSLLG PTGMEPQIAN
CSIYNYFVWL HYYSVRDTLL GPGRPFTAID FSHQGPAFVT WHRYHLLLLE RDLQRLTGNE
SFALPYWNFA TGKNECDVCT DQLFGASWPD DPSLISPNSR FSLWQIVCNS LDDYNRLVTL
CNGTDEGPLR RGPLRTSSRQ LPTLEDIRNC LSLQEFDSPP FFRNSSFSFR NALEGFNKPD
GTLNSSVLSL HNLALSFLNG TSVLSHAAAN DPIFVVLHSF TDAIFDEWMK RFSPPDNAWP
EELAPIGHNR LYNMVPFFPP VTNDQLFLTV EQLGYTYAID LPGSSEETQA WAIIVGATLA
GALIALVMLV LLLVFFQHRR QRKGFEPLMN VSFTPKKYME EA
//
