ID A0A384BBQ9_BALAS Unreviewed; 519 AA.
AC A0A384BBQ9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=L-dopachrome tautomerase {ECO:0000256|ARBA:ARBA00039823};
DE EC=5.3.3.12 {ECO:0000256|ARBA:ARBA00038932};
DE AltName: Full=L-dopachrome Delta-isomerase {ECO:0000256|ARBA:ARBA00042019};
DE AltName: Full=Tyrosinase-related protein 2 {ECO:0000256|ARBA:ARBA00041443};
GN Name=DCT {ECO:0000313|RefSeq:XP_007196918.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007196918.1};
RN [1] {ECO:0000313|RefSeq:XP_007196918.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007196918.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate;
CC Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509;
CC EC=5.3.3.12; Evidence={ECO:0000256|ARBA:ARBA00036823};
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_007196918.1; XM_007196856.1.
DR AlphaFoldDB; A0A384BBQ9; -.
DR GeneID; 103009988; -.
DR CTD; 1638; -.
DR OrthoDB; 70287at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:SF4; L-DOPACHROME TAUTOMERASE; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..519
FT /note="L-dopachrome tautomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016896412"
FT TRANSMEM 469..493
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 389..400
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 519 AA; 59052 MW; 8D8E9FEFA4F1FFEB CRC64;
MSPLRWGLLL GCLGCALPPR VRAQFPRVCM TVGSLQAKEC CPPLGADTAD VCGSREGRGQ
CAEVQTDTRP WSGPYVLRNQ DDRERWPRKF FDRTCRCTGN FAGYNCGDCK FGWTGPNCDQ
KKPLVVRQNI HSLTPQEREQ FLGSLDLAKN TPHPDYVITT QHWLGLLGTN GTQPQIANCS
IYDFFVWLHY YSVRDTLLGP GRPYKAIDFS HQGPAFVTWH RYHLLWLERD LQRLTGNESF
ALPYWNFATG RNECDVCTDQ LLGAARQDDP TLISQNSRFS SWEIVCDSLD DYNRRVTLCN
GTYEGLLRRN QVGRSSEKLP TLKDIQDCLS LKKFDNPPFF QNSTFSFRNA LEGFDKADGT
LDSQVMNLHN LVHSFLNGTN ALPHSAANDP VFVVLHSFTD AVFDEWMKRF NPPADAWPQE
LAPIGHNRMY NMVPFFPPVT NEELFLTADQ LGYSYAIDLP VSVEETSDWT TTLSVVMGML
VVLVGLFALL IFLQYRRLRK GYTPLMETQL SNKRYTEEA
//
