PRP1_MANSE
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 03-AUG-2022, entry version 91.
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}.
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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; -; 1.
DR Gene3D; 1.20.1370.10; -; 1.
DR Gene3D; 2.60.40.1520; -; 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; PTHR11511; 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; SSF48050; SSF48050; 1.
DR SUPFAM; SSF48056; SSF48056; 1.
DR SUPFAM; SSF81296; SSF81296; 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
