ID A0A669D4C4_ORENI Unreviewed; 528 AA.
AC A0A669D4C4;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=5,6-dihydroxyindole-2-carboxylic acid oxidase {ECO:0000256|ARBA:ARBA00040647};
DE AltName: Full=Tyrosinase-related protein 1 {ECO:0000256|ARBA:ARBA00041445};
GN Name=TYRP1 {ECO:0000313|Ensembl:ENSONIP00000053175.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000053175.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000053175.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 5,6-dihydroxyindole-2-carboxylate + O2 = 2 H2O + 2
CC indole-5,6-quinone-2-carboxylate; Xref=Rhea:RHEA:68388,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16875,
CC ChEBI:CHEBI:177869; Evidence={ECO:0000256|ARBA:ARBA00036464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68389;
CC Evidence={ECO:0000256|ARBA:ARBA00036464};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
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 AlphaFoldDB; A0A669D4C4; -.
DR Ensembl; ENSONIT00000079337.1; ENSONIP00000053175.1; ENSONIG00000008846.2.
DR GeneTree; ENSGT00940000155804; -.
DR Proteomes; UP000005207; Linkage group LG6.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF3; 5,6-DIHYDROXYINDOLE-2-CARBOXYLIC ACID OXIDASE; 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 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:UP000005207};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..528
FT /note="5,6-dihydroxyindole-2-carboxylic acid oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025384236"
FT TRANSMEM 469..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..223
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 388..399
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 528 AA; 59396 MW; 56F28A0F5460197F CRC64;
LLWSVGLVWT LCTTLTLAQF PRECVTPEGL QSGQCCPSPT GVAGDECGSS TGRGQCVTIE
ADSRRHGPQY PYAGRDDRER WPLRFFNRTC RCNGNFTGYN CGRCRHGLTG PNCDQRISVV
RRNIMQMSTA EKQAFVNALD QAKRTVHPDL VICTRRYQEL FGPDGNTPQF ENITIYNYFV
WSHYYSVSKT YLGPGQTSFG GVDFSHEGPG FVTWHRFHLL QLERDMQDML GNPTFALPYW
NFAIGGSECD ICTDDLLGAR STFDMSSISP NSVFSQWRVI CESVDDYDTL GTICNSTESS
PIRRNPAGNV ARPMVQRLPE PKDVLDCLEI NTFDTPPYYS TSSESFRNTI EGYSAPQGMY
DPVIRSLHNL AHLFLNGTGG QTHLSPNDPI FVLLHTFTDA IFDEWLRRHQ PGDTVYPDEN
APIGHNRRFN MVPFWPPVTN AEMFVPAPEN LGYSYEVQWP ARTFTLSEII SVAVIAAVLV
VVVVGIIIAC AMRSHSYNSA EALEPLLAET YRRYSEEDRR LDKSQSVV
//
