Reviewed, UniProtKB/Swiss-Prot Q25519 (PRP2_MANSE)

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

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › 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	L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O.
Cofactor	Binds 2 copper ions per subunit By similarity. Ref.3
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
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
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response Ref.1 Traceable author statement. Source: UniProtKB melanin biosynthetic process from tyrosine Ref.1 Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of melanization defense response Ref.5 Non-traceable author statement. Source: UniProtKB transport Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Ref.4 Inferred from direct assay. 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 Ref.1 Traceable author statement. Source: UniProtKB oxygen transporter activity Inferred from electronic annotation. Source: InterPro
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 By similarity Ref.3
	Metal binding	219	1	Copper A By similarity Ref.3
	Metal binding	245	1	Copper A By similarity Ref.3
	Metal binding	368	1	Copper B By similarity Ref.3
	Metal binding	372	1	Copper B By similarity Ref.3
	Metal binding	408	1	Copper B By similarity Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q25519-1 [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: 7644492] [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: 8626641] [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: 9474780] [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: 10436935] [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: 16291091] [Abstract] Cited for: FUNCTION.

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	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.14.18.1. 15145.

Family and domain databases

InterPro

IPR008922. Di-copper_centre.
IPR013788. Hemocyanin.
IPR005203. Hemocyanin_C.
IPR000896. Hemocyanin_Cu.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase.
[Graphical view]

Gene3D

G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
G3DSA:2.60.40.1520. hemocyanin_C. 1 hit.
G3DSA:1.20.1370.10. hemocyanin_N. 1 hit.

PANTHER

PTHR11511. Hemocyanin. 1 hit.

Pfam

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

PRINTS

PR00187. HAEMOCYANIN.

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:	January 19, 2010
This is version 53 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)