ID A0A5D2ULX1_GOSMU Unreviewed; 599 AA.
AC A0A5D2ULX1;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00497, ECO:0000259|PROSITE:PS00498};
GN ORFNames=E1A91_D06G153500v1 {ECO:0000313|EMBL:TYI77610.1};
OS Gossypium mustelinum (Cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=34275 {ECO:0000313|EMBL:TYI77610.1, ECO:0000313|Proteomes:UP000323597};
RN [1] {ECO:0000313|EMBL:TYI77610.1, ECO:0000313|Proteomes:UP000323597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1408120.09 {ECO:0000313|EMBL:TYI77610.1};
RA Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT "WGS assembly of Gossypium mustelinum.";
RL Submitted (JUL-2019) 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; CM017654; TYI77610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D2ULX1; -.
DR Proteomes; UP000323597; Chromosome d06.
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:SF87; POLYPHENOL OXIDASE CHLOROPLASTIC; 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|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:UP000323597};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 204..221
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 361..372
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 435..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 204
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 213
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 334
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 338
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT BINDING 368
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-1"
FT DISULFID 104..123
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT DISULFID 122..184
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-2"
FT CROSSLNK 187..204
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000290-3"
SQ SEQUENCE 599 AA; 67609 MW; 475084F0B9D26CA5 CRC64;
MGSTVNSPST PIIIPSSPLQ TSFIPKTSQL SIFKKKKPFN FASKKLVSCK ASDRNQNNAD
SSSLNRFDRR DILLGLGGLY GATNLVSDPF ASAAPIAAPD LSLCENSTVT SSSSGTSISV
PCCPPKATNI IDFKPPRFSN IRLRPAAHLV DANYLEKFTK AMELMKALPD DDPRSFKQQA
NVHCAYCNGA YDHVGFPDQQ LQIHFSWLFF PFHRFYLYFY ERILGKLIGD PNFVMPFWNW
DSPPGMVIPD IYVDPTSPLY DEKRNVDHQP PKMLDLDYAG TEELLSKRDQ IKSNLSVMYR
QMVTYKTPSL FHGAAYRAGD NPSPGMGSVE NNPHTAVHRW VGDKREPFSE DMGNFYSAGR
DPLFYAHHCN VDRLWNIWKS LPGKKRTDFT DTDWLDSSFL FYDDNANLVR VKVRDCLNSR
TLGYDYQKVN IPWLKNKPTP RRPGRGSGSG SAMAAETNTK TVIRNAFPIV LDKLVRIEVP
RTKKSRTKVE KENEEEVLVL QNIRVDRDVA VKFDVYINDE DDETPTEPED SEFAGSFTNI
PHNHHNPAVK LDTNLTLPLS DLLEDLDIER DDNIVVTLVP KEGKGLVSIG NIKIDFVRD
//
