Q25519 (PRP2_MANSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenoloxidase subunit 2
EC=1.14.18.1

Alternative name(s):
proPO-p2

Gene names

Name:

ppo

Organism

Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)

Taxonomic identifier

7130 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Amphiesmenoptera › Lepidoptera › Glossata › Neolepidoptera › Heteroneura › Ditrysia › Obtectomera › Bombycoidea › Sphingidae › Sphinginae › Sphingini › Manduca

Protein attributes

Sequence length	695 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization. Ref.5
Catalytic activity	2 L-dopa + O2 = 2 dopaquinone + 2 H2O. L-tyrosine + O2 = dopaquinone + H2O.
Cofactor	Binds 2 copper ions per subunit. Ref.6
Enzyme regulation	Activated by immulectin and lipopolysaccharide. Ref.4
Subunit structure	Heterodimer. Forms a complex with an interleukin 1-like protein as a consequence of a host defense response. Ref.2 Ref.3 Ref.6
Subcellular location	Secreted Ref.3.
Tissue specificity	Synthesized by oenocytoids, a type of hemocyte, and released into the hemolymph plasma. Ref.3
Post-translational modification	The N-terminus is blocked. Ref.3
Sequence similarities	Belongs to the tyrosinase family.
Mass spectrometry	Molecular mass is 79791 Da from positions 2 - 695. Determined by MALDI. Ref.3

Ontologies

Keywords
Biological process	Melanin biosynthesis
Cellular component	Secreted
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	defense response Traceable author statement Ref.1. Source: UniProtKB melanin biosynthetic process from tyrosine Traceable author statement Ref.1. Source: UniProtKB positive regulation of melanization defense response Non-traceable author statement Ref.5. Source: UniProtKB
Cellular_component	extracellular region Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	chloride ion binding Inferred from sequence or structural similarity. Source: UniProtKB copper ion binding Inferred from sequence or structural similarity. Source: UniProtKB monophenol monooxygenase activity Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Probable Ref.3

Chain

2 – 695

694

Phenoloxidase subunit 2 Ref.3

PRO_0000234111

Sites

Metal binding

215

1

Copper A UniProtKB P04253

Metal binding

219

1

Copper A UniProtKB P04253

Metal binding

245

1

Copper A UniProtKB P04253

Metal binding

368

1

Copper B UniProtKB P04253

Metal binding

372

1

Copper B UniProtKB P04253

Metal binding

408

1

Copper B UniProtKB P04253

Amino acid modifications

Disulfide bond

586 ↔ 630

Ref.6

Disulfide bond

588 ↔ 637

Ref.6

Secondary structure

1

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695

Helix Strand Turn

Details...

Helix

4 – 10

7

Beta strand

19 – 21

3

Turn

24 – 27

4

Beta strand

28 – 31

4

Helix

34 – 36

3

Helix

39 – 41

3

Turn

42 – 44

3

Helix

45 – 53

9

Beta strand

60 – 63

4

Helix

76 – 78

3

Helix

90 – 105

16

Helix

111 – 124

14

Helix

127 – 140

14

Beta strand

141 – 143

3

Helix

152 – 155

4

Helix

157 – 159

3

Helix

165 – 175

11

Helix

198 – 202

5

Helix

203 – 206

4

Helix

209 – 221

13

Helix

229 – 232

4

Helix

237 – 257

21

Turn

258 – 260

3

Turn

285 – 287

3

Beta strand

303 – 305

3

Helix

306 – 308

3

Beta strand

310 – 312

3

Helix

314 – 330

17

Beta strand

331 – 334

4

Beta strand

340 – 342

3

Helix

345 – 353

9

Helix

361 – 364

4

Helix

367 – 376

10

Helix

391 – 393

3

Turn

395 – 397

3

Helix

398 – 400

3

Helix

402 – 419

18

Turn

422 – 424

3

Helix

430 – 433

4

Beta strand

438 – 447

10

Beta strand

454 – 465

12

Helix

467 – 469

3

Beta strand

479 – 487

9

Beta strand

490 – 498

9

Beta strand

504 – 515

12

Helix

524 – 527

4

Turn

528 – 530

3

Beta strand

532 – 540

9

Beta strand

543 – 551

9

Helix

552 – 554

3

Helix

561 – 564

4

Beta strand

589 – 591

3

Helix

592 – 594

3

Beta strand

600 – 602

3

Beta strand

604 – 614

11

Helix

615 – 618

4

Helix

634 – 637

4

Turn

650 – 653

4

Beta strand

654 – 656

3

Helix

664 – 667

4

Beta strand

673 – 688

16

Sequences

	Sequence		Length	Mass (Da)
	Q25519 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 93DB6D7F2490A386	FASTA	695	80,061
	10 20 30 40 50 60 MADIFDSFEL LYDRPGEPMI NTKGEDKVLF ELTEQFLTPE YANNGLELNN RFGDEEEVSR 70 80 90 100 110 120 KIILKNLDKI PEFPKAKQLP NDADFSLFLP SHQEMANEVI DVLMSVTENQ LQELLSTCVY 130 140 150 160 170 180 ARINLNPQLF NYCYTVAIMH RRDTGKVRVQ NYAEIFPAKF LDSQVFTQAR EAAAVIPKTI 190 200 210 220 230 240 PRTPIIIPRD YTATDLEEEH RLAYWREDLG INLHHWHWHL VYPFSASDEK IVAKDRRGEL 250 260 270 280 290 300 FFYMHQQIIA RYNCERLCNS LKRVKKFSDW REPIPEAYYP KLDSLTSARG WPPRQAGMRW 310 320 330 340 350 360 QDLKRPVDGL NVTIDDMERY RRNIEEAIAT GNVILPDKST KKLDIDMLGN MMEASVLSPN 370 380 390 400 410 420 RDLYGSIHNN MHSFSAYMHD PEHRYLESFG VIADEATTMR DPFFYRVHAW VDDIFQSFKE 430 440 450 460 470 480 APHNVRPYSR SQLENPGVQV TSVAVESAGG QQNVLNTFWM QSDVNLSKGL DFSDRGPVYA 490 500 510 520 530 540 RFTHLNHRPF RYVIKANNTA SARRTTVRIF IAPKTDERNL PWALSDQRKM FIEMDRFVVP 550 560 570 580 590 600 LSAGENTITR QSTESSLTIP FEQTFRDLSI QGSDPRRSEL AAFNYCGCGW PQHMLVPKGT 610 620 630 640 650 660 VGGVAYQLFV MLSNYELDKI EQPDGRELSC VEASMFCGLK DKKYPDARPM GYPFDRPSNS 670 680 690 ATNIEDFSAM SNMGLQDIVI KLSDVTEPNP RNPPA

References

[1]	"Proenzyme of Manduca sexta phenol oxidase: purification, activation, substrate specificity of the active enzyme, and molecular cloning." Hall M., Scott T., Sugumaran M., Soderhall K., Law J.H. Proc. Natl. Acad. Sci. U.S.A. 92:7764-7768(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-51 AND 401-406. Tissue: Hemocyte.
[2]	"Characterization of a defense complex consisting of interleukin 1 and phenol oxidase from the hemolymph of the tobacco hornworm, Manduca sexta." Beck G., Cardinale S., Wang L., Reiner M., Sugumaran M. J. Biol. Chem. 271:11035-11038(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[3]	"Subunit composition of pro-phenol oxidase from Manduca sexta: molecular cloning of subunit ProPO-P1." Jiang H., Wang Y., Ma C., Kanost M.R. Insect Biochem. Mol. Biol. 27:835-850(1997) [PubMed] [Europe PMC] [Abstract] Cited for: BLOCKAGE OF N-TERMINUS, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY.
[4]	"Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase." Yu X.-Q., Gan H., Kanost M.R. Insect Biochem. Mol. Biol. 29:585-597(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[5]	"Prophenoloxidase binds to the surface of hemocytes and is involved in hemocyte melanization in Manduca sexta." Ling E., Yu X.-Q. Insect Biochem. Mol. Biol. 35:1356-1366(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes." Li Y., Wang Y., Jiang H., Deng J. Proc. Natl. Acad. Sci. U.S.A. 106:17002-17006(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH COPPER IONS, COFACTOR, SUBUNIT, DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42556 mRNA. Translation: AAC37243.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HHS	X-ray	1.97	A	2-695	[»]

ProteinModelPortal

Q25519.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48979N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.

InterPro

IPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]

PANTHER

PTHR11511. PTHR11511. 1 hit.

Pfam

PF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]

PRINTS

PR00187. HAEMOCYANIN.

SUPFAM

SSF48056. Di-copper_centre. 1 hit.
SSF48050. Hemocyanin_N. 1 hit.
SSF81296. Ig_E-set. 1 hit.

PROSITE

PS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00497. TYROSINASE_1. False negative.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PRP2_MANSE

Accession

Primary (citable) accession number: Q25519

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)