ID C0LV93_LOCMI Unreviewed; 697 AA.
AC C0LV93;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Pro-phenoloxidase 1 {ECO:0000313|EMBL:ACN81830.1};
GN Name=PPO1 {ECO:0000313|EMBL:ACN81830.1};
OS Locusta migratoria (Migratory locust).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Oedipodinae; Locusta.
OX NCBI_TaxID=7004 {ECO:0000313|EMBL:ACN81830.1};
RN [1] {ECO:0000313|EMBL:ACN81830.1}
RP NUCLEOTIDE SEQUENCE.
RA Zheng H.Z., Xu Q., Huang S.J., Tang B., Wang S.G.;
RT "Characterization and expression patterns of a pro-phenoloxidase 1 gene
RT from Locusta migratoria.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR EMBL; FJ771025; ACN81830.1; -; mRNA.
DR AlphaFoldDB; C0LV93; -.
DR SMR; C0LV93; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004503; F:tyrosinase activity; IEA:UniProt.
DR GO; GO:0006582; P:melanin metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 2.60.40.1520; Hemocyanin, C-terminal domain; 1.
DR Gene3D; 1.20.1370.10; Hemocyanin, N-terminal domain; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR013788; Hemocyanin/hexamerin.
DR InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR InterPro; IPR005203; Hemocyanin_C.
DR InterPro; IPR037020; Hemocyanin_C_sf.
DR InterPro; IPR005204; Hemocyanin_N.
DR InterPro; IPR036697; Hemocyanin_N_sf.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11511; LARVAL STORAGE PROTEIN/PHENOLOXIDASE; 1.
DR PANTHER; PTHR11511:SF4; PHENOLOXIDASE 2-RELATED; 1.
DR Pfam; PF03723; Hemocyanin_C; 1.
DR Pfam; PF00372; Hemocyanin_M; 1.
DR Pfam; PF03722; Hemocyanin_N; 1.
DR PRINTS; PR00187; HAEMOCYANIN.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48050; Hemocyanin, N-terminal domain; 1.
DR PROSITE; PS00209; HEMOCYANIN_1; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 401..412
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 678..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 80817 MW; 1FC256D8120F77BD CRC64;
MAFNNPNNIL YLFDRVAEPL FLPKGEENKV VFKLPTEYLT PRYQSIVSEI TDRWGGVQNR
MEINVKPITL PDLSLPMTLD RRDNFSPFLP YHRQMASRLV ETFLGMRTYE DFLSLSIYCR
DRINPYMYTY ALSIAMLHRQ DTNKLPLPPL TEVFPDKYMD GAVFSRARQE ANVVSSGNRL
PIVIPLDYTA SDLDPEHRVA YFREDIGINL LHWQWHLYYP FSDMMEIVKK DRRGELFYYF
HQQIVARYNF ERLSNNLARV KRLLNWREPV EEGYFPKLDN IVSSRVWPPR NSFTTLRDIN
RELDQIKFDI QDLERWRDRI YEAIHSGSVV NEKKQLVELT ENEGIDILGN MIDASILSVN
PNLYGDLHNL GHVMMGFCHD PDARHLETFG VIADPATALR DPLFYRWHAF IDGIFQEHKK
VIPRYTLQQL SFDKVRVTGV EVLSEKSPKN EFSTFWQQND IDLSRGLDFA PRGPVFVRFT
HLQHAPFVTK IQVENGGPPR VGTVRIFMAP KYDERGLPML LRGQRSLFIE IDKFPVQLKS
GSNIIQRRSD ESSVAIPFER TFRNLTGVRE SQQVAEYTYC GCGWPQHMLI PKGHQEGLPA
EFFVMVSDGS VDKVEQPPPV QGCHAAHSYC GLHKRLYPDR RSMGYPFDRV PRDGVNTLRE
FMTPNMAVIE VKIRHSETAV GPGPGNTPGV PANWRQL
//
