ID A0A3Q2ZVE6_KRYMA Unreviewed; 518 AA.
AC A0A3Q2ZVE6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSKMAP00000007861.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000007861.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000007861.1}
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 RefSeq; XP_017269805.1; XM_017414316.1.
DR AlphaFoldDB; A0A3Q2ZVE6; -.
DR STRING; 37003.ENSKMAP00000007861; -.
DR Ensembl; ENSKMAT00000007985.1; ENSKMAP00000007861.1; ENSKMAG00000005890.1.
DR GeneID; 108234822; -.
DR KEGG; kmr:108234822; -.
DR GeneTree; ENSGT00940000155804; -.
DR OMA; ATRHYSD; -.
DR OrthoDB; 70287at2759; -.
DR Proteomes; UP000264800; 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:UP000264800};
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..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..518
FT /note="5,6-dihydroxyindole-2-carboxylic acid oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018529550"
FT TRANSMEM 466..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..220
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 385..396
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 518 AA; 57492 MW; 559205E3D3CA0DDC CRC64;
MWHFVVLFGA AAVSAQFPRE CVTPEVLRSG QCCPSPPGLP GDPCGAGAGR GQCVDVAADA
RPHGPQYPHD GQDDRERWPL RFFNRTCQCS GNFSGFDCGR CRHGWTGAAC DQRVSVVRRN
VMQLSADEKR AFVSALDQAK RTPHPDLVIA TRHYADLFGP DGNATQFENC TIYNYFVWSH
YYSVSKTFLG AGQASFGGVD FSHEGPGFLT WHRFHLQQLE RDMQDMLQDP SFALPYWNFA
IGGNSCDICT DDLMGARSSF DANALSSNSV FSQWRVVCES VDDYDTLGTI CNSTETSPIR
RNPAGNVNRP MVQRLPEPQD VADCLQVNAF DTPPYYSTSS ESFRNTIEGY SAPKGNYDPV
VRSLHNLAHL FLNGTGGQTH LSPNDPIFVL LHTYTDAIFD EWLRRHGPDS AVYPDENAPI
GHNRGYNMVP FWPPVTNSEM FVTAPENLGY SYEAEWPAQP FTLTEIITMS IVAALVVVAI
AFAATTCALR ARSKMEGHQP LLGDQYQRYD DEKSQSVV
//
