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Database: UniProt
Entry: A0A0D2VFA6_GOSRA
LinkDB: A0A0D2VFA6_GOSRA
Original site: A0A0D2VFA6_GOSRA 
ID   A0A0D2VFA6_GOSRA        Unreviewed;       567 AA.
AC   A0A0D2VFA6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00497, ECO:0000259|PROSITE:PS00498};
GN   ORFNames=B456_010G254900 {ECO:0000313|EMBL:KJB68615.1}, Gorai_008523
GN   {ECO:0000313|EMBL:MBA0598777.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB68615.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB68615.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
RN   [2] {ECO:0000313|EMBL:MBA0598777.1, ECO:0000313|Proteomes:UP000593578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8 {ECO:0000313|EMBL:MBA0598777.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:MBA0598777.1};
RX   PubMed=30476109;
RA   Grover C.E., Arick M.A. 2nd, Thrash A., Conover J.L., Sanders W.S.,
RA   Peterson D.G., Frelichowski J.E., Scheffler J.A., Scheffler B.E.,
RA   Wendel J.F.;
RT   "Insights into the Evolution of the New World Diploid Cottons (Gossypium,
RT   Subgenus Houzingenia) Based on Genome Sequencing.";
RL   Genome Biol. Evol. 11:53-71(2019).
RN   [3] {ECO:0000313|EMBL:MBA0598777.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=8 {ECO:0000313|EMBL:MBA0598777.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:MBA0598777.1};
RA   Grover C.E., Arick M.A. II, Thrash A., Conover J.L., Sanders W.S.,
RA   Peterson D.G., Scheffler J.A., Scheffler B.E., Wendel J.F.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000290-1};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000256|PIRSR:PIRSR000290-
CC       1};
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
CC       {ECO:0000256|ARBA:ARBA00009928}.
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DR   EMBL; CM001749; KJB68615.1; -; Genomic_DNA.
DR   EMBL; JABEZZ010000010; MBA0598777.1; -; Genomic_DNA.
DR   RefSeq; XP_012449470.1; XM_012594016.1.
DR   AlphaFoldDB; A0A0D2VFA6; -.
DR   STRING; 29730.A0A0D2VFA6; -.
DR   EnsemblPlants; KJB68615; KJB68615; B456_010G254900.
DR   GeneID; 105772626; -.
DR   Gramene; KJB68615; KJB68615; B456_010G254900.
DR   KEGG; gra:105772626; -.
DR   eggNOG; ENOG502QVBP; Eukaryota.
DR   OMA; LNYGGTD; -.
DR   OrthoDB; 4070889at2759; -.
DR   Proteomes; UP000032304; Chromosome 10.
DR   Proteomes; UP000593578; Unassembled WGS sequence.
DR   GO; GO:0004097; F:catechol oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046148; P:pigment biosynthetic process; IEA:InterPro.
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; IPR016213; Polyphenol_oxidase.
DR   InterPro; IPR022740; Polyphenol_oxidase_C.
DR   InterPro; IPR022739; Polyphenol_oxidase_cen.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF94; POLYPHENOL OXIDASE, CHLOROPLASTIC-LIKE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF12142; PPO1_DWL; 1.
DR   Pfam; PF12143; PPO1_KFDV; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PIRSF; PIRSF000290; PPO_plant; 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|PIRSR:PIRSR000290-1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR000290-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000290-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW   Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT   DOMAIN          181..198
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          341..352
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   BINDING         160
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         181
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         190
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         314
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         318
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   BINDING         348
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT   DISULFID        84..99
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT   DISULFID        98..161
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT   CROSSLNK        164..181
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ   SEQUENCE   567 AA;  64768 MW;  AA686A2F414D6DFB CRC64;
     MATISPSITS SFLPKKSKYS IIKNPKFKNP KSIPCKAING EQEHPKHKFD RRDVLIGLGG
     LYYGAASLND AMAAPISAPE MEKCGRADVP EGVQTTDCCP PVSKRILDFK PPFSNSPVRV
     RPAAHLVDDE YIRKYSKAIE LMKALPHDDP RSFMQQANVH CAYCEGAYDQ VGFPNLELQV
     HNSWLFFPFH RYYLYFFERI LGHLIDDPTF GLPFWNWDSP AGMWMPDMFM DTNSSLYDKF
     RNSRHYPPTM VDLDYNGEDE HETKMNKDQV KSNLSIMYRQ MVSNAKTPRL FLGGPFRAGD
     EPYQGSGSIE NVPHGPVHVW CGDDKQPNGE DMGTFYSAAR DPIFYAHHSN VDRMWSVWKT
     IENINRKDFD DPDWLNASFL FYDENANLVR VKVRDCLDHR NLGYVYQFVD LPWLKEKPTP
     RKLTKKNKAP PPPVSSTEFV LDKPVRVNVE RPRKSRSKTE KEEKEEILVI DIELKGDLFV
     KFDVYVNDED DAGSNIGSEN TEFAGSYVNV PNKHKQGKTL KTRLRLGLTD LLEDLGADDD
     DGIVVTLVPK YGKGNIKISG IKIEFDN
//
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