TYR3_CAEEL
ID TYR3_CAEEL Reviewed; 693 AA.
AC Q19673;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 5.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Putative tyrosinase-like protein tyr-3;
DE Flags: Precursor;
GN Name=tyr-3; ORFNames=F21C3.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; Z71261; CAA95805.2; -; Genomic_DNA.
DR PIR; T21192; T21192.
DR RefSeq; NP_492055.2; NM_059654.4.
DR AlphaFoldDB; Q19673; -.
DR SMR; Q19673; -.
DR BioGRID; 37914; 1.
DR STRING; 6239.F21C3.2; -.
DR PaxDb; Q19673; -.
DR PeptideAtlas; Q19673; -.
DR EnsemblMetazoa; F21C3.2.1; F21C3.2.1; WBGene00009001.
DR GeneID; 172472; -.
DR KEGG; cel:CELE_F21C3.2; -.
DR UCSC; F21C3.2; c. elegans.
DR CTD; 172472; -.
DR WormBase; F21C3.2; CE42097; WBGene00009001; tyr-3.
DR eggNOG; ENOG502QRET; Eukaryota.
DR HOGENOM; CLU_020332_0_0_1; -.
DR InParanoid; Q19673; -.
DR OMA; WTNEFMG; -.
DR OrthoDB; 313578at2759; -.
DR PhylomeDB; Q19673; -.
DR Reactome; R-CEL-5662702; Melanin biosynthesis.
DR PRO; PR:Q19673; -.
DR Proteomes; UP000001940; Chromosome I.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR003582; ShKT_dom.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF01549; ShK; 4.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SMART; SM00254; ShKT; 4.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS51670; SHKT; 4.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Copper; Disulfide bond; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..693
FT /note="Putative tyrosinase-like protein tyr-3"
FT /id="PRO_0000035898"
FT DOMAIN 472..506
FT /note="ShKT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 516..550
FT /note="ShKT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 591..625
FT /note="ShKT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 634..667
FT /note="ShKT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT BINDING 142
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 152
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 281
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 285
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 308
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 472..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 479..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 488..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 516..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 523..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 532..547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 591..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 598..618
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 607..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 634..667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 641..660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 650..664
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 693 AA; 77717 MW; E72C7837BB66FFF6 CRC64;
MIRYIILLVY FLIFEVNSQL DCSKAPTPAI RIMCNQIQRW DQKARATPSL SGDVKTPGIA
GKAMAAEFSP IASNVFQCMD IACLCVFFRG TGGNNCVVQG RPLGKVVRKE YRMLSDDERQ
RLHQAFRTLK QNGEYDRLAR VHAQYSESGA AHSGPAFLPW HREFVKRMEF LIRQVDPSLH
LPYWDSSLDQ NLPDSKDSIL WTNEFMGDAN GEVNNGPFRS WKTVENKPAI TRAVGAQGKG
YSEDEINTML GQTDIAQVLA FSAPQRGCPY QPNFNVPEYT HGNPHIYVGG DMLETSTAAN
DPIFWMHHSF VDLLWEMYRQ SKQTRATRET AYPADNRQCS SEHHFRAAFM RPFTPMRNAD
GLSNMYTDNL YSYAPRPSCN AGPTCGSPYL FCDKSHGAPR CAVRMKPEGN CASFKNGEDA
CYQGSCQSGK CVAGSQNVTP PPTIQPTKPV VTVEVFSETC LKIRLKFFQT SCFNENECCG
PWSAKGECQK NPVYMNVWCK ASCRQCTPNY NINEECSDRH TNCAMWSRSG ECNKNPLWMS
ENCRSSCQKC GRSRAATCGG GGGADSISNP TTMPPATNNG QQNTPCDSPM CYNEDQCCPI
WAQRGQCRSN PGYMTCQCKV SCGVCRPNYV YGPCADYHYD CAAWARRGEC LKNKWMPENC
RRSCNTCVNQ QQLAARCATR IVRSAFLELI RMK
