Reviewed,
UniProtKB/Swiss-Prot O44249 (PRP1_MANSE)
Last modified
June 16, 2009.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Phenoloxidase subunit 1 EC=1.14.18.1 Alternative name(s): proPO-P1 |
| 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 | 685 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.4 Ref.1 |
| Catalytic activity | L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O. Ref.1 |
| Cofactor | Binds 2 copper ions per subunit By similarity. UniProtKB P04253 |
| Enzyme regulation | Activated by immulectin and lipopolysaccharide. Ref.3 |
| Subunit structure | Heterodimer. Forms a complex with an interleukin 1-like protein as a consequence of a host defense response. Ref.1 Ref.2 |
| Subcellular location | |
| Tissue specificity | Synthesized by oenocytoids, a type of hemocyte, and released into the hemolymph plasma. Ref.1 |
| Post-translational modification | The N-terminus is blocked. Ref.1 |
| Sequence similarities | Belongs to the tyrosinase family. |
| Mass spectrometry | Molecular mass is 78904 Da from positions 2 - 685. Determined by MALDI. Ref.1 |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Probable Ref.1 | ||||||
| Chain | 2 – 685 | 684 | Phenoloxidase subunit 1 Ref.1 | PRO_0000234110 | |||||
Sites | |||||||||
| Metal binding | 209 | 1 | Copper A By similarity UniProtKB P04253 | ||||||
| Metal binding | 213 | 1 | Copper A By similarity UniProtKB P04253 | ||||||
| Metal binding | 239 | 1 | Copper A By similarity UniProtKB P04253 | ||||||
| Metal binding | 366 | 1 | Copper B By similarity UniProtKB P04253 | ||||||
| Metal binding | 370 | 1 | Copper B By similarity UniProtKB P04253 | ||||||
| Metal binding | 406 | 1 | Copper B By similarity UniProtKB P04253 | ||||||
Sequences
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References
| [1] | "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: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BLOCKAGE OF N-TERMINUS, MASS SPECTROMETRY. 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] | "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. |
| [4] | "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 | |
|---|---|
| AF003253 mRNA. Translation: AAC05796.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OXY based on UniProtKB P04253. |
| 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. 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 | PRP1_MANSE | ||||||||
| Accession | Primary (citable) accession number: O44249 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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