ID PRP2_MANSE Reviewed; 695 AA. AC Q25519; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 22-FEB-2023, entry version 91. DE RecName: Full=Phenoloxidase subunit 2; DE EC=1.14.18.1; DE AltName: Full=proPO-p2; GN Name=ppo {ECO:0000312|EMBL:AAC37243.1}; 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:AAC37243.1} RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-51 AND 401-406. RC TISSUE=Hemocyte {ECO:0000269|PubMed:7644492}; RX PubMed=7644492; DOI=10.1073/pnas.92.17.7764; RA Hall M., Scott T., Sugumaran M., Soderhall K., Law J.H.; RT "Proenzyme of Manduca sexta phenol oxidase: purification, activation, RT substrate specificity of the active enzyme, and molecular cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7764-7768(1995). 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 BLOCKAGE OF N-TERMINUS, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND MASS SPECTROMETRY. 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 [4] {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 [5] {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 [6] 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=79791; 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; L42556; AAC37243.1; -; mRNA. DR PDB; 3HHS; X-ray; 1.97 A; A=2-695. DR PDBsum; 3HHS; -. DR AlphaFoldDB; Q25519; -. DR SMR; Q25519; -. DR DIP; DIP-48979N; -. DR IntAct; Q25519; 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; TAS:UniProtKB. DR GO; GO:0006583; P:melanin biosynthetic process from tyrosine; TAS:UniProtKB. DR GO; GO:0035008; P:positive regulation of melanization defense response; NAS: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; Direct protein sequencing; Disulfide bond; KW Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase; KW Secreted. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000305" FT CHAIN 2..695 FT /note="Phenoloxidase subunit 2" FT /id="PRO_0000234111" FT ACT_SITE 353 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q8MZM3" FT BINDING 215 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 219 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 245 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 368 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 372 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:19805072" FT BINDING 408 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000269|PubMed:19805072" FT DISULFID 586..630 FT /evidence="ECO:0000269|PubMed:19805072" FT DISULFID 588..637 FT /evidence="ECO:0000269|PubMed:19805072" FT HELIX 4..10 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 24..27 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 28..31 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 42..44 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 45..53 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 90..105 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 111..124 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 127..140 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 165..175 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 198..202 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 203..206 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 209..221 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 229..232 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 237..257 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 258..260 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 285..287 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 303..305 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 306..308 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 314..330 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 340..342 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 345..353 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 361..364 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 367..376 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 395..397 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 398..400 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 402..419 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 422..424 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 430..433 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 438..447 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 454..465 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 467..469 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 479..487 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 490..498 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 504..515 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 524..527 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 528..530 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 532..540 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 543..551 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 552..554 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 561..564 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 589..591 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 592..594 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 600..602 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 604..614 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 615..618 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 634..637 FT /evidence="ECO:0007829|PDB:3HHS" FT TURN 650..653 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 654..656 FT /evidence="ECO:0007829|PDB:3HHS" FT HELIX 664..667 FT /evidence="ECO:0007829|PDB:3HHS" FT STRAND 673..688 FT /evidence="ECO:0007829|PDB:3HHS" SQ SEQUENCE 695 AA; 80061 MW; 93DB6D7F2490A386 CRC64; MADIFDSFEL LYDRPGEPMI NTKGEDKVLF ELTEQFLTPE YANNGLELNN RFGDEEEVSR KIILKNLDKI PEFPKAKQLP NDADFSLFLP SHQEMANEVI DVLMSVTENQ LQELLSTCVY ARINLNPQLF NYCYTVAIMH RRDTGKVRVQ NYAEIFPAKF LDSQVFTQAR EAAAVIPKTI PRTPIIIPRD YTATDLEEEH RLAYWREDLG INLHHWHWHL VYPFSASDEK IVAKDRRGEL FFYMHQQIIA RYNCERLCNS LKRVKKFSDW REPIPEAYYP KLDSLTSARG WPPRQAGMRW QDLKRPVDGL NVTIDDMERY RRNIEEAIAT GNVILPDKST KKLDIDMLGN MMEASVLSPN RDLYGSIHNN MHSFSAYMHD PEHRYLESFG VIADEATTMR DPFFYRVHAW VDDIFQSFKE APHNVRPYSR SQLENPGVQV TSVAVESAGG QQNVLNTFWM QSDVNLSKGL DFSDRGPVYA RFTHLNHRPF RYVIKANNTA SARRTTVRIF IAPKTDERNL PWALSDQRKM FIEMDRFVVP LSAGENTITR QSTESSLTIP FEQTFRDLSI QGSDPRRSEL AAFNYCGCGW PQHMLVPKGT VGGVAYQLFV MLSNYELDKI EQPDGRELSC VEASMFCGLK DKKYPDARPM GYPFDRPSNS ATNIEDFSAM SNMGLQDIVI KLSDVTEPNP RNPPA //