ID A0A673AIS6_9TELE Unreviewed; 533 AA.
AC A0A673AIS6;
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=LOC115428756 {ECO:0000313|Ensembl:ENSSORP00005029174.1};
OS Sphaeramia orbicularis (orbiculate cardinalfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005029174.1, ECO:0000313|Proteomes:UP000472271};
RN [1] {ECO:0000313|Ensembl:ENSSORP00005029174.1}
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 AlphaFoldDB; A0A673AIS6; -.
DR Ensembl; ENSSORT00005030004.1; ENSSORP00005029174.1; ENSSORG00005013927.1.
DR InParanoid; A0A673AIS6; -.
DR OrthoDB; 70287at2759; -.
DR Proteomes; UP000472271; Unplaced.
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:UP000472271};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..533
FT /note="5,6-dihydroxyindole-2-carboxylic acid oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025399504"
FT TRANSMEM 474..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..228
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 393..404
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 533 AA; 59711 MW; 39C3ACC3F40A9CB9 CRC64;
MHSQSMWREG LLVLTLCATL TLAQFPRECV TAEGLRSGQC CPSPTGSAGD ECGSSTGRGQ
CVSIAADSRR HGPQYPYSGR DDRERWPLRF FNRTCQCNGN FTGYNCGRCR HGLTGPNCDQ
RISVVRRNIM LMTAAEKQAF VNALDQAKRT VHPEIVICTR RYQEVFGPDG NTPQFDNVTI
YNYFVWSHYY SVSKTYLGPG QTSFGGVDFS HEGPGFVTWH RFHLLQLERD MQDMLGDPTF
ALPYWNFAIG GSECDICTDD LMGARSSFDM NSISPNSVFS EWRVICESVD DYDTLGTICN
STESSPIRRN PAGNVARPMV QRLPEPKDVL DCLQLNTFDT PPYYSTSSES FRNTIEGYSA
PQGMYDPVIR SLHNLAHLFL NGTGGQTHLS PNDPIFVLLH TFTDAVFDEW LRRHQPGEVV
YPEENAPIGH NRRFNMVPFW PPVTNAEMFV SAPENLGYSY EVQWPARAFT LSEIITIAIV
AAVLVVAVVG GVIACAVRAH SYRSAEALEP LLGETFRRYS EDDRRLDKSQ SVV
//
