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Q25519 (PRP2_MANSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenoloxidase subunit 2

EC=1.14.18.1
Alternative name(s):
proPO-p2
Gene names
Name:ppo
OrganismManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifier7130 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

Protein attributes

Sequence length695 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable Ref.3
Chain2 – 695694Phenoloxidase subunit 2 Ref.3
PRO_0000234111

Sites

Metal binding2151Copper A UniProtKB P04253
Metal binding2191Copper A UniProtKB P04253
Metal binding2451Copper A UniProtKB P04253
Metal binding3681Copper B UniProtKB P04253
Metal binding3721Copper B UniProtKB P04253
Metal binding4081Copper B UniProtKB P04253

Amino acid modifications

Disulfide bond586 ↔ 630 Ref.6
Disulfide bond588 ↔ 637 Ref.6

Secondary structure

............................................................................................................. 695
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q25519 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 93DB6D7F2490A386

FASTA69580,061
        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 

« Hide

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3HHSX-ray1.97A2-695[»]
ProteinModelPortalQ25519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48979N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERPTHR11511. PTHR11511. 1 hit.
PfamPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSPR00187. HAEMOCYANIN.
SUPFAMSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRP2_MANSE
AccessionPrimary (citable) accession number: Q25519
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references