ID   TYRO2_PINMG             Reviewed;         456 AA.
AC   H2A0L1;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Tyrosinase-like protein 2;
DE            EC=1.14.18.-;
DE   AltName: Full=Tyrosinase 2;
DE   Flags: Precursor;
OS   Margaritifera margaritifera (Freshwater pearl mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=102329;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle;
RX   PubMed=21040589; DOI=10.1186/1471-2164-11-613;
RA   Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F.,
RA   Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.;
RT   "Transcriptome and proteome analysis of Pinctada margaritifera calcifying
RT   mantle and shell: focus on biomineralization.";
RL   BMC Genomics 11:613-613(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 112-126; 130-146; 165-172; 215-239 AND 370-384,
RP   SUBCELLULAR 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}.
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DR   EMBL; HE610378; CCE46152.1; -; mRNA.
DR   AlphaFoldDB; H2A0L1; -.
DR   SMR; H2A0L1; -.
DR   PRIDE; H2A0L1; -.
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; Oxidoreductase; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..456
FT                   /note="Tyrosinase-like protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417980"
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"
SQ   SEQUENCE   456 AA;  53060 MW;  7E72744925EC96C9 CRC64;
     MNTMALFGKV ILLQFLIGVG FCMLMQDPKR NDTKSTYATC FRSQPQGNEP ASPDCVKAFM
     AYAEDMKNIF HFTKEQINYL WSLERETQSL FHNHRRRKRQ AVFLPVRKEC RLLSEFERQN
     LFYTIRSLKM DTSNPNEYDT LANLHRGAVQ PHAHDGSNFL GWHRVYLMYY ERALRRIRGD
     VTLCFWDTTM DFNLGMDNWE YTAVFSSDFF GNRRGQVITG PFRDWPLPPG LTESDYLYRN
     MTRGRGMPFD SRAASSIFYN PNTIIHSTVT WEGFGFDTIT NSQGQTRNIT IEGEHNNVHN
     WVGGAMEFLD PAPQDPVFFF HHCYIDYVWE RFREKMRRYF RDPTTDYPGH GNETLHDANY
     PMIGFEWFRN IDGYSDYFIQ NVYRYESPTC QACYYSPYTV CGQGNQCIAR MNYPGTEIEE
     GPQVPNSPVV AFSVAGGTML MSAFNGRGFI ATSNSE