ID PRP1_MANSE Reviewed; 685 AA. AC O44249; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 22-FEB-2023, entry version 93. DE RecName: Full=Phenoloxidase subunit 1; DE EC=1.14.18.1; DE AltName: Full=proPO-P1; OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Sphingidae; Sphinginae; Sphingini; Manduca. OX NCBI_TaxID=7130; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC05796.1} RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, BLOCKAGE OF N-TERMINUS, AND MASS SPECTROMETRY. RC TISSUE=Hemocyte {ECO:0000269|PubMed:9474780}; RX PubMed=9474780; DOI=10.1016/s0965-1748(97)00066-0; RA Jiang H., Wang Y., Ma C., Kanost M.R.; RT "Subunit composition of pro-phenol oxidase from Manduca sexta: molecular RT cloning of subunit ProPO-P1."; RL Insect Biochem. Mol. Biol. 27:835-850(1997). RN [2] {ECO:0000305} RP SUBUNIT. RX PubMed=8626641; DOI=10.1074/jbc.271.19.11035; RA Beck G., Cardinale S., Wang L., Reiner M., Sugumaran M.; RT "Characterization of a defense complex consisting of interleukin 1 and RT phenol oxidase from the hemolymph of the tobacco hornworm, Manduca sexta."; RL J. Biol. Chem. 271:11035-11038(1996). RN [3] {ECO:0000305} RP ACTIVITY REGULATION. RX PubMed=10436935; DOI=10.1016/s0965-1748(99)00036-3; RA Yu X.-Q., Gan H., Kanost M.R.; RT "Immulectin, an inducible C-type lectin from an insect, Manduca sexta, RT stimulates activation of plasma prophenol oxidase."; RL Insect Biochem. Mol. Biol. 29:585-597(1999). RN [4] {ECO:0000305} RP FUNCTION. RX PubMed=16291091; DOI=10.1016/j.ibmb.2005.08.007; RA Ling E., Yu X.-Q.; RT "Prophenoloxidase binds to the surface of hemocytes and is involved in RT hemocyte melanization in Manduca sexta."; RL Insect Biochem. Mol. Biol. 35:1356-1366(2005). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH COPPER IONS, RP COFACTOR, SUBUNIT, AND DISULFIDE BOND. RX PubMed=19805072; DOI=10.1073/pnas.0906095106; RA Li Y., Wang Y., Jiang H., Deng J.; RT "Crystal structure of Manduca sexta prophenoloxidase provides insights into RT the mechanism of type 3 copper enzymes."; RL Proc. Natl. Acad. Sci. U.S.A. 106:17002-17006(2009). CC -!- FUNCTION: This is a copper-containing oxidase that functions in the CC formation of pigments such as melanins and other polyphenolic CC compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, CC DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 CC quinone. Binds to the surface of hemocytes and is involved in hemocyte CC melanization. {ECO:0000269|PubMed:16291091, ECO:0000305}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, CC ChEBI:CHEBI:57924; EC=1.14.18.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924, CC ChEBI:CHEBI:58315; EC=1.14.18.1; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000269|PubMed:19805072}; CC Note=Binds 2 copper ions per subunit. {ECO:0000269|PubMed:19805072}; CC -!- ACTIVITY REGULATION: Activated by immulectin and lipopolysaccharide. CC {ECO:0000269|PubMed:10436935}. CC -!- SUBUNIT: Heterodimer. Forms a complex with an interleukin 1-like CC protein as a consequence of a host defense response. CC {ECO:0000269|PubMed:19805072, ECO:0000269|PubMed:8626641, CC ECO:0000269|PubMed:9474780}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9474780}. CC -!- TISSUE SPECIFICITY: Synthesized by oenocytoids, a type of hemocyte, and CC released into the hemolymph plasma. {ECO:0000269|PubMed:9474780}. CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9474780}. CC -!- MASS SPECTROMETRY: Mass=78904; Method=MALDI; CC Evidence={ECO:0000269|PubMed:9474780}; CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF003253; AAC05796.1; -; mRNA. DR PDB; 3HHS; X-ray; 1.97 A; B=2-685. DR PDBsum; 3HHS; -. DR AlphaFoldDB; O44249; -. DR SMR; O44249; -. DR DIP; DIP-48978N; -. DR IntAct; O44249; 1. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB. DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB. DR GO; GO:0004503; F:tyrosinase activity; TAS:UniProtKB. DR GO; GO:0006952; P:defense response; NAS:UniProtKB. DR GO; GO:0006583; P:melanin biosynthetic process from tyrosine; TAS:UniProtKB. DR GO; GO:0035008; P:positive regulation of melanization defense response; IDA:UniProtKB. 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 1: Evidence at protein level; KW 3D-structure; Copper; Disulfide bond; Melanin biosynthesis; Metal-binding; KW Monooxygenase; Oxidoreductase; Secreted. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000305" FT CHAIN 2..685 FT /note="Phenoloxidase subunit 1" FT /id="PRO_0000234110" FT ACT_SITE 351 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q8MZM3" FT BINDING 209 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 213 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 239 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 366 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 370 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 406 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:19805072" FT DISULFID 580..622 FT /evidence="ECO:0000269|PubMed:19805072" FT DISULFID 582..629 FT /evidence="ECO:0000269|PubMed:19805072" FT HELIX 4..7 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 8..12 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 24..27 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 39..44 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 45..53 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 87..102 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 106..117 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 122..135 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 147..150 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 159..170 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 192..196 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 197..200 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 203..215 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 223..226 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 231..252 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 279..282 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 308..324 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 326..328 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 339..341 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 342..351 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 359..362 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 365..374 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 375..377 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 389..391 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 393..395 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 396..398 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 400..417 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 425..428 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 433..440 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 447..458 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 460..462 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 472..480 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 484..491 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 493..495 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 497..509 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 518..521 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 522..524 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 526..535 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 537..545 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 546..548 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 550..553 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 555..557 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 583..585 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 586..588 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 598..608 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 609..611 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 626..629 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 642..645 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 646..648 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 657..660 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 665..679 FT /evidence="ECO:0007829|PDB:3HHS" SQ SEQUENCE 685 AA; 78966 MW; BE5811D145302583 CRC64; MTDAKNNLLY FFDRPNEPCF MQKGEDKVVF EIPDHYYPDK YKSLSNTLSN RFGNEATKRI PIRNITLPNL EVPMQLPYND QFSLFVPKHR TMAAKLIDIF MGMRDVEDLQ SVCSYCQLRI NPYMFNYCLS VAILHRPDTK GLSIPTFAET FPDKFMDSKV FLRAREVSNV VISGSRMPVN VPINYTANTT EPEQRVAYFR EDIGINLHHW HWHLVYPFDS ADRSIVNKDR RGELFYYMHQ QIIGRYNVER MCNGLPQVKP FSDFSAPIEE GYFPKLDSQV ASRTWPPRFA GSVFRNLDRT VDQVKIDVRK LFTWRDQFLE AIQKMAIKMP NGRELPLDEV TGIDMLGNLM ESSIISPNRG YYGDLHNMGH VFAAYTHDPD HRHLEQFGVM GDSATAMRDP FFYRWHRFVD DVFNIYKEKL TPYTNERLDF PGVRVSSVGI EGARPNTLRT LWQQSTVELG RGLDFTPRGS VLARFTHLQH DEFQYVIEVN NTTGGNLMGT VRIFMAPKVD DNGQPMSFNK QRRLMIELDK FSQALRPGTN TIRRRSVDSS VTIPYERTFR NQSERPGDPG TAGAAEFDFC GCGWPHHMLI PKGTAQGYPV VLFVMISNWN NDRIEQDLVG SCNDAASYCG IRDRKYPDKQ AMGYPFDRKM ANDAATLSDF LRPNMAVRDC SIQFSDTTVE RGQQG //