ID A0A4W4EP59_ELEEL Unreviewed; 532 AA.
AC A0A4W4EP59;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:ENSEEEP00000014014.1};
OS Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000014014.1, ECO:0000313|Proteomes:UP000314983};
RN [1] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24970089;
RA Gallant J.R., Traeger L.L., Volkening J.D., Moffett H., Chen P.H.,
RA Novina C.D., Phillips G.N.Jr., Anand R., Wells G.B., Pinch M., Guth R.,
RA Unguez G.A., Albert J.S., Zakon H.H., Samanta M.P., Sussman M.R.;
RT "Nonhuman genetics. Genomic basis for the convergent evolution of electric
RT organs.";
RL Science 344:1522-1525(2014).
RN [2] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28695212;
RA Traeger L.L., Sabat G., Barrett-Wilt G.A., Wells G.B., Sussman M.R.;
RT "A tail of two voltages: Proteomic comparison of the three electric organs
RT of the electric eel.";
RL Sci. Adv. 3:e1700523-e1700523(2017).
RN [3] {ECO:0000313|Ensembl:ENSEEEP00000014014.1}
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; A0A4W4EP59; -.
DR Ensembl; ENSEEET00000014185.1; ENSEEEP00000014014.1; ENSEEEG00000006871.1.
DR GeneTree; ENSGT00940000155804; -.
DR Proteomes; UP000314983; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000314983};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 212..229
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 532 AA; 59730 MW; AC208BE2B4881439 CRC64;
AHLGFYGLCL LESSFLKKCE LVRAQFPREC VTPEILRSAQ CCPSLFGQVN NPCGVNTGRG
QCVPVRVDLR PHGPQYPHDG RDDRERWPFK FFNRTCQCNS NFSGYNCGRC RHGFTGLNCD
QPVPVVRRNV MTLSPAEKRA FVNALDRAKR ATHPDVVIAT RRYEEVFGPD GNSTQFQNIS
VYNYFVWAHY YSVSKTFLGG GQPSFGGVDF SHEGPGFLTW HRYHLLQLER DMQDPGFALP
YWDFAIGGNQ CDICTDDLMG ARSSFDDGAI SSNSIFSRWL VICESVDDYD TLGTENGPIR
RNPAGNVARP MVQKLPEPQD IKACLEVQDF DTPPFYSTSS ESFRNTIEGY SAPEGIYDPI
VRSLHNLAHL FLNGTGGTTH LSPNDPIFVL LHTFTDAVFD EWLRRHPGKS AVYPLENAPI
GHNRHHNMVP FWPPVSNAEM FATASENLGY SYEAEWPGGN CSVALVLTLY DIQTDLMNQA
TLIVVAIIFT VTTCIVRTSS NKTEGRQPLL GEQYQCYDDQ DSRHNDKTQS VV
//
