ID A0A087X5L9_POEFO Unreviewed; 530 AA.
AC A0A087X5L9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:ENSPFOP00000001072.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000001072.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000001072.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; AYCK01010072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087X5L9; -.
DR STRING; 48698.ENSPFOP00000001072; -.
DR Ensembl; ENSPFOT00000001074.1; ENSPFOP00000001072.1; ENSPFOG00000001047.1.
DR eggNOG; ENOG502QRNA; Eukaryota.
DR GeneTree; ENSGT00940000155804; -.
DR OMA; ATRHYSD; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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:UP000028760};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..530
FT /note="5,6-dihydroxyindole-2-carboxylic acid oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001832350"
FT TRANSMEM 477..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..231
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 396..407
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 530 AA; 59047 MW; 2F82676D11A957F7 CRC64;
ITLPSLFLPM WPYCVSMLVC AVLVSAQFPR ECVTPEGLRS GQCCPAPPGF PGDPCGASAG
RGQCVSISAD ARPHGPQYPH DGRDDRERWP VRFFNRTCQC TGNFSGYNCG RCRHGWTGAN
CDQRISVVRR NVMQLSSEEK RAFVNALNQA KRTVHPDLVI ATRHYSDIFG PDGNTTQFEN
VTVYNYFVWS HYYSVSKTFL GAGQASFGGV DFSHEGPGFL TWHRFHLLQL ERDMQDMLQD
PSFALPYWNF AIGGNTCDIC TDDLMGARSS FDINSLSPNS IFSEWRVVCE SVEDYDTLGT
ICNSTETSPI RRNPAGNVNR PMVQRLPEPQ DVADCLQVGT FDTPPFYSTS SESFRNTVEG
YSAPKGNYDP IVRSLHNLAH LFLNGTGGQT HLSPNDPIFV LLHTFTDAIF DEWLRRHGPD
LAVYPEENAP IGHNRGYNMV PFWPPVTNAE MFVTAPENLG YSYEAEWPGT PFSLTEIITI
AIVAALVLVA VIFAATTCAV RARSRKMEGH QPLLGDQYQR YDDDKGQSVV
//
