PRP2_MANSE
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 03-AUG-2022, entry version 89.
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}.
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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; -; 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; 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
