ID   TYRO_PINMA              Reviewed;         456 AA.
AC   P86952;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Tyrosinase-like protein;
DE   AltName: Full=Tyrosinase-2;
DE   Flags: Precursor;
OS   Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=104660;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000269|PubMed:19915030};
RX   PubMed=19915030; DOI=10.1093/molbev/msp278;
RA   Jackson D.J., McDougall C., Woodcroft B., Moase P., Rose R.A., Kube M.,
RA   Reinhardt R., Rokhsar D.S., Montagnani C., Joubert C., Piquemal D.,
RA   Degnan B.M.;
RT   "Parallel evolution of nacre building gene sets in molluscs.";
RL   Mol. Biol. Evol. 27:591-608(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 165-172; 214-239; 244-252 AND 370-384, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA   Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA   Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT   "Different secretory repertoires control the biomineralization processes of
RT   prism and nacre deposition of the pearl oyster shell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:P06845};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:P06845};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC   -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level).
CC       {ECO:0000269|PubMed:23213212}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000255}.
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DR   EMBL; GT278854; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281565; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281776; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT282052; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EZ420237; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86952; -.
DR   SMR; P86952; -.
DR   PRIDE; P86952; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016716; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, another compound as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.1280.10; -; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR015559; Tyr-like.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF21; PTHR11474:SF21; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..456
FT                   /note="Tyrosinase-like protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000413088"
FT   BINDING         145
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT   BINDING         154
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   BINDING         163
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   BINDING         295
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   BINDING         299
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   BINDING         322
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   CONFLICT        359
FT                   /note="N -> H (in Ref. 1; GT281565)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   456 AA;  52851 MW;  3805F30FAC36428C CRC64;
     MNTMTLLGKV FLLQFLIGVG FCMLMQDPKR NDTKGTYAAC FRSQPQGNEP ASPDCLKAFM
     AYAEDMKNIF HFTKEQINYL WSLERETQSL LHNHRRRKRQ AVYLPVRKEC RLLSELERQN
     LFYTVRSLKM DTSNPNEYDT LANLHRGAVQ PHAHDGSNFL GWHRVYLMYY ERALRRIRGD
     VTLCFWDTTM EFNLGMDNWE YTAVFSSDFF GNRRGQVITG PFRDWPLPPG LTESDYLYRN
     MTRGRGMPFD SRAASSIFYN PNTIIHSTIT WEGFGFDTIT NSQGQTRNIT IEGEHNNVHN
     WVGGAMGFLD PAPQDPIFFF HHCYIDYVWE RFREKMRRYF RDPTTDYPGH GNETLHDANY
     PMIGFEWYRN IDGYSDYFTQ NVYRYESPTC QACYYSPYTV CGQGNQCIAR MNYPGTEIEE
     GPQVPNGPVA AFSVAGGTMM MSASNGRGFI ATSNSE