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 16-JUN-2009, entry version 51. 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; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Sphingidae; Sphinginae; Sphingini; Manduca. OX NCBI_TaxID=7130; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, BLOCKAGE OF N-TERMINUS, AND MASS SPECTROMETRY. RC TISSUE=Hemocyte; RX MEDLINE=98135121; 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: RT molecular cloning of subunit ProPO-P1."; RL Insect Biochem. Mol. Biol. 27:835-850(1997). RN [2] 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 RT sexta."; RL J. Biol. Chem. 271:11035-11038(1996). RN [3] RP ENZYME REGULATION. RX MEDLINE=99365988; 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] 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). CC -!- FUNCTION: This is a copper-containing oxidase that functions in CC the formation of pigments such as melanins and other polyphenolic CC compounds. Catalyzes the rate-limiting conversions of tyrosine to CC DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to CC indole-5'6 quinone. Binds to the surface of hemocytes and is CC involved in hemocyte melanization. CC -!- CATALYTIC ACTIVITY: L-tyrosine + L-dopa + O(2) = L-dopa + CC dopaquinone + H(2)O. CC -!- COFACTOR: Binds 2 copper ions per subunit (By similarity). CC -!- ENZYME REGULATION: Activated by immulectin and lipopolysaccharide. CC -!- SUBUNIT: Heterodimer. Forms a complex with an interleukin 1-like CC protein as a consequence of a host defense response. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Synthesized by oenocytoids, a type of CC hemocyte, and released into the hemolymph plasma. CC -!- PTM: The N-terminus is blocked. CC -!- MASS SPECTROMETRY: Mass=78904; Method=MALDI; Range=2-685; CC Source=PubMed:9474780; CC -!- SIMILARITY: Belongs to the tyrosinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF003253; AAC05796.1; -; mRNA. DR HSSP; P04253; 1OXY. DR BRENDA; 1.14.18.1; 15145. 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:monophenol monooxygenase activity; TAS:UniProtKB. DR GO; GO:0005344; F:oxygen transporter activity; IEA:InterPro. DR GO; GO:0006952; P:defense response; NAS:UniProtKB. DR GO; GO:0006583; P:melanin biosynthetic process from tyrosine; TAS:UniProtKB. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0035008; P:positive regulation of melanization defense...; IDA:UniProtKB. DR GO; GO:0006810; P:transport; IEA:InterPro. DR InterPro; IPR008922; Di-copper_centre. DR InterPro; IPR013788; Hemocyanin. DR InterPro; IPR005203; Hemocyanin_C. DR InterPro; IPR000896; Hemocyanin_Cu. DR InterPro; IPR005204; Hemocyanin_N. DR InterPro; IPR002227; Tyrosinase. DR Gene3D; G3DSA:1.10.1280.10; Di-copper_centre; 1. DR Gene3D; G3DSA:2.60.40.1520; hemocyanin_C; 1. DR Gene3D; G3DSA:1.20.1370.10; hemocyanin_N; 1. DR PANTHER; PTHR11511; Hemocyanin; 1. DR Pfam; PF03723; Hemocyanin_C; 1. DR Pfam; PF00372; Hemocyanin_M; 1. DR Pfam; PF03722; Hemocyanin_N; 1. DR PRINTS; PR00187; HAEMOCYANIN. DR PROSITE; PS00209; HEMOCYANIN_1; 1. DR PROSITE; PS00210; HEMOCYANIN_2; 1. DR PROSITE; PS00497; TYROSINASE_1; FALSE_NEG. DR PROSITE; PS00498; TYROSINASE_2; 1. PE 1: Evidence at protein level; KW Copper; Melanin biosynthesis; Metal-binding; Monooxygenase; KW Oxidoreductase; Secreted. FT INIT_MET 1 1 Removed (Probable). FT CHAIN 2 685 Phenoloxidase subunit 1. FT /FTId=PRO_0000234110. FT METAL 209 209 Copper A (By similarity). FT METAL 213 213 Copper A (By similarity). FT METAL 239 239 Copper A (By similarity). FT METAL 366 366 Copper B (By similarity). FT METAL 370 370 Copper B (By similarity). FT METAL 406 406 Copper B (By similarity). 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 //