ID G3TGJ7_LOXAF Unreviewed; 530 AA.
AC G3TGJ7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Tyrosinase {ECO:0000256|ARBA:ARBA00039304};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
DE AltName: Full=Monophenol monooxygenase {ECO:0000256|ARBA:ARBA00042251};
GN Name=TYR {ECO:0000313|Ensembl:ENSLAFP00000013606.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000013606.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000013606.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013606.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000013606.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013606.3};
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 -!- SUBUNIT: Forms an OPN3-dependent complex with DCT in response to blue
CC light in melanocytes. {ECO:0000256|ARBA:ARBA00038813}.
CC -!- SUBCELLULAR LOCATION: Melanosome membrane
CC {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004573}.
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_003418603.1; XM_003418555.2.
DR AlphaFoldDB; G3TGJ7; -.
DR STRING; 9785.ENSLAFP00000013606; -.
DR Ensembl; ENSLAFT00000016209.3; ENSLAFP00000013606.3; ENSLAFG00000016209.3.
DR GeneID; 100676924; -.
DR KEGG; lav:100676924; -.
DR CTD; 7299; -.
DR eggNOG; ENOG502QRET; Eukaryota.
DR GeneTree; ENSGT00940000155336; -.
DR HOGENOM; CLU_038693_1_0_1; -.
DR InParanoid; G3TGJ7; -.
DR OMA; CSQLEEY; -.
DR OrthoDB; 70287at2759; -.
DR TreeFam; TF315865; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004503; F:tyrosinase activity; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0009637; P:response to blue light; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
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:SF124; TYROSINASE; 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 Copper {ECO:0000256|ARBA:ARBA00023008};
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:UP000007646};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..530
FT /note="Tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003455386"
FT TRANSMEM 474..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 202..219
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 383..394
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 530 AA; 60449 MW; 2DABB19A6ED04A45 CRC64;
MRLVVLYCLL WSFHTSAGHF PRACVSSKSM MEKECCPPWS GDGSPCGQLS GRGSCQDVLL
SNAPLGPQFP FTGVDDRESW PSVFYNRTCQ CSGNFMGFDC GNCRFGFWGP NCTERRLLVR
RNIFDLSVPE KNKFLAYLTL AKHTTSADYV IPTGTYGQMN NGSRPMFRDI NIYDLFVWMH
YYVSRDTLLG GSEIWSDIDF AHEAPGFLPW HRLFLLQWEK EIQRLTGDEN FTIPYWDWRD
AEDCDICTDE YMGGHHPANP NLLSPASFFS SWQIVCSRME EYNSRQALCD GTPEGPLLRN
PGNHDKARTP RLPSSADVEF CLSLTQYESG SMNKAANFSF RNTLEGFASP LTGIADASQS
SMHNALHIYM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRYHPLQEV YPEANAPIGH
NRESYMVPFI PLYRNGDFFI SSRELGYDYS YLRDSEPDSF QDYIKSYLEQ ASQIWQWLLG
AAVVGAVLTA VLGRLASLLC RCRRKQLPEE KQPLLMEKDD YHSLLSQSHL
//
