Phenoloxidase subunit 2 - Manduca sexta (Tobacco hawkmoth)

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Q25519 (PRP2_MANSE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 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 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

Removed Probable Ref.3

Chain

2 – 695

694

Phenoloxidase subunit 2 Ref.3

PRO_0000234111

Sites

Metal binding

215

Copper A By similarity Ref.3

Metal binding

219

Copper A By similarity Ref.3

Metal binding

245

Copper A By similarity Ref.3

Metal binding

368

Copper B By similarity Ref.3

Metal binding

372

Copper B By similarity Ref.3

Metal binding

408

Copper B By similarity Ref.3

Secondary structure

695

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q25519 [UniParc].

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

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

« 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: 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.
+	Additional computationally mapped references.

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

InterPro

IPR013788. Hemocyanin.
IPR005203. Hemocyanin_C.
IPR000896. Hemocyanin_Cu.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[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.

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:	September 21, 2011
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents