TYR1_CAEEL
ID TYR1_CAEEL Reviewed; 601 AA.
AC P34269; P34270;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Putative tyrosinase-like protein tyr-1;
DE Flags: Precursor;
GN Name=tyr-1; ORFNames=C02C2.1/C02C2.2;
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
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 -!- INTERACTION:
CC P34269; Q965F9: par-2; NbExp=2; IntAct=EBI-312495, EBI-11465387;
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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 EMBL; FO080276; CCD62528.1; -; Genomic_DNA.
DR PIR; S44739; S44739.
DR PIR; S44740; S44740.
DR RefSeq; NP_498711.1; NM_066310.4.
DR AlphaFoldDB; P34269; -.
DR SMR; P34269; -.
DR BioGRID; 41313; 3.
DR DIP; DIP-24673N; -.
DR IntAct; P34269; 3.
DR MINT; P34269; -.
DR STRING; 6239.C02C2.1; -.
DR PaxDb; P34269; -.
DR PeptideAtlas; P34269; -.
DR EnsemblMetazoa; C02C2.1.1; C02C2.1.1; WBGene00015332.
DR GeneID; 176105; -.
DR KEGG; cel:CELE_C02C2.1; -.
DR UCSC; C02C2.1; c. elegans.
DR CTD; 176105; -.
DR WormBase; C02C2.1; CE06754; WBGene00015332; tyr-1.
DR eggNOG; ENOG502QRET; Eukaryota.
DR HOGENOM; CLU_020332_0_0_1; -.
DR InParanoid; P34269; -.
DR OMA; QEWDSAA; -.
DR OrthoDB; 518234at2759; -.
DR PhylomeDB; P34269; -.
DR Reactome; R-CEL-5662702; Melanin biosynthesis.
DR SignaLink; P34269; -.
DR PRO; PR:P34269; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015332; Expressed in larva and 2 other tissues.
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; 2.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SMART; SM00254; ShKT; 2.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS51670; SHKT; 2.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW Copper; Disulfide bond; Glycoprotein; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..601
FT /note="Putative tyrosinase-like protein tyr-1"
FT /id="PRO_0000035897"
FT DOMAIN 480..514
FT /note="ShKT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 523..557
FT /note="ShKT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT REGION 453..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 158
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 167
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 289
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 293
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 316
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 480..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 487..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 496..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 523..557
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 530..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 539..554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 601 AA; 68429 MW; 9F2ADD849BCE6D38 CRC64;
MGRLRAFLLF SGTLAVISTV HADFNCSQAP DSDMVQTCHM LQEWDSAARK AIRKRQAFNA
GAPGVQGFSP SNPPRFAPSA QGCMNIACIC PYMGGRMANG CILPNGQPYL MAYRKEYRMM
SDNERQRWHN ALIQLKRSGE YDRLSVMHRQ VGSASGAHSG PGFLVWHREY MKRMEIALRM
IDPGISMPYW DSVLESYLPD PRDSIMFGPQ FMGMTDASGQ LVSGPFAGFR TLEGRPNIIR
RMATEGKMFT EQNINNLMAQ NDLVSVMAFT APQGGCPFRP YFGALEYTHA SIHLWMGGDM
KPPSTSANDP VFFLHHTFVD FIWEMWRQNH QNRFARENQY PPDIAACANS QHFSYAQMRP
WDKINRDGLS NAYTDNLYHY APRPTCNRNN ANCGSQYLFC DTRGNPHCVA KVKPGGLCRG
FEGLDSCYMG TCVAGWCRGG QQFQQPAQTT AVATVQQPQQ QPQQQQPQQQ RPATTPQSNC
YNEDPCCNQW SRQNECRTNT VYMNRYCRKS CGLCQSNDNN RGCHDRHISC AYWRGQNFCT
RRRQWMAENC QATCGWCNMN EAQLCASVAR QSRRVRRNAK FWLTEPDADD FVDDFMLDYG
R
