ID O97047_TENMO Unreviewed; 684 AA.
AC O97047;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Prophenoloxidase {ECO:0000313|EMBL:BAA75470.1};
GN Name=ppo-5 {ECO:0000313|EMBL:BAA75470.1};
OS Tenebrio molitor (Yellow mealworm beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrio.
OX NCBI_TaxID=7067 {ECO:0000313|EMBL:BAA75470.1};
RN [1] {ECO:0000313|EMBL:BAA75470.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10050770; DOI=10.1016/S0014-5793(99)00067-8;
RA Lee H.S., Cho M.Y., Lee K.M., Kwon T.H., Homma K., Natori S., Lee B.L.;
RT "The pro-phenoloxidase of coleopteran insect, Tenebrio molitor, larvae was
RT activated during cell clump/cell adhesion of insect cellular defense
RT reactions.";
RL FEBS Lett. 444:255-259(1999).
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; AB020738; BAA75470.1; -; mRNA.
DR AlphaFoldDB; O97047; -.
DR ELM; O97047; -.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 397..408
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT COILED 285..312
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 684 AA; 79154 MW; 2E95E4E1EEB5E366 CRC64;
MASKKNILLL FDRPREPVFI AKGSKKAVFS VPNEYLADKY KPLGVALTNR FGEDADERID
VKKISIPPFG EILELSRDEN FSLFIPKHRR IAGRLIDIFL GMRNVDDLVS VAVYARDRVN
PYLFNYALSV AILHRPDTQD VDLPSFIESF PDKYVDAKVF AQAREQATVV PEGSRAPIEI
PKDYTASDLE EEHRLAYFRE DLGINLHHWH WHLVYPFEAA REVVAKNRRG ELFYYMHQQI
IARYNFERLC NKLKRATRFN DFKQAIQEAY FPKLDSLVAS RSWPARVGNQ RLKDLNREVD
QIKQDVDDLK RWSDRIYAAI HQGSATDERG RKIELTENEG IDILGNMIES SILSPNRTFY
GDMHNMGHVF ISYVHDPDHR HLESFGVMGD SATAMRDPIF YRWHSYIDDI FQEYKATLPR
YTENQLNFPG VTVSKVEVQV QGGSANTLNT FWQQSDVDMS RGMDFQPRGS VFVRFTHLQH
QPFTYKITVK NSSNGNRKGT CRIFIAPKLD ERGNPWLYRD QKNMFVELDK FTVNLKQGQN
NITRASSQSS VTIPFERTFR NLDLNRPQGG EELAQFNFCG CGWTQHMLIP KGTPEGMPCQ
LFVMISNYED DKVNQSTEGV CNDAGSYCGI KDKLYPDRRS MGYPFDRMPR NGVDTLQQFL
TSNMRVQDVT IKFTNRTVRP KSRN
//
