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O44249 (PRP1_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 1

EC=1.14.18.1
Alternative name(s):
proPO-P1
OrganismManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifier7130 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

Protein attributes

Sequence length685 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.1 Ref.4

Catalytic activity

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.

L-tyrosine + O2 = dopaquinone + H2O.

Cofactor

Binds 2 copper ions per subunit. Ref.5

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 Ref.5

Subcellular location

Secreted Ref.1.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable Ref.1
Chain2 – 685684Phenoloxidase subunit 1 Ref.1
PRO_0000234110

Sites

Metal binding2091Copper A UniProtKB P04253
Metal binding2131Copper A UniProtKB P04253
Metal binding2391Copper A UniProtKB P04253
Metal binding3661Copper B UniProtKB P04253
Metal binding3701Copper B UniProtKB P04253
Metal binding4061Copper B UniProtKB P04253

Amino acid modifications

Disulfide bond580 ↔ 622 Ref.5
Disulfide bond582 ↔ 629 Ref.5

Secondary structure

.............................................................................................................. 685
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O44249 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BE5811D145302583

FASTA68578,966
        10         20         30         40         50         60 
MTDAKNNLLY FFDRPNEPCF MQKGEDKVVF EIPDHYYPDK YKSLSNTLSN RFGNEATKRI 

        70         80         90        100        110        120 
PIRNITLPNL EVPMQLPYND QFSLFVPKHR TMAAKLIDIF MGMRDVEDLQ SVCSYCQLRI 

       130        140        150        160        170        180 
NPYMFNYCLS VAILHRPDTK GLSIPTFAET FPDKFMDSKV FLRAREVSNV VISGSRMPVN 

       190        200        210        220        230        240 
VPINYTANTT EPEQRVAYFR EDIGINLHHW HWHLVYPFDS ADRSIVNKDR RGELFYYMHQ 

       250        260        270        280        290        300 
QIIGRYNVER MCNGLPQVKP FSDFSAPIEE GYFPKLDSQV ASRTWPPRFA GSVFRNLDRT 

       310        320        330        340        350        360 
VDQVKIDVRK LFTWRDQFLE AIQKMAIKMP NGRELPLDEV TGIDMLGNLM ESSIISPNRG 

       370        380        390        400        410        420 
YYGDLHNMGH VFAAYTHDPD HRHLEQFGVM GDSATAMRDP FFYRWHRFVD DVFNIYKEKL 

       430        440        450        460        470        480 
TPYTNERLDF PGVRVSSVGI EGARPNTLRT LWQQSTVELG RGLDFTPRGS VLARFTHLQH 

       490        500        510        520        530        540 
DEFQYVIEVN NTTGGNLMGT VRIFMAPKVD DNGQPMSFNK QRRLMIELDK FSQALRPGTN 

       550        560        570        580        590        600 
TIRRRSVDSS VTIPYERTFR NQSERPGDPG TAGAAEFDFC GCGWPHHMLI PKGTAQGYPV 

       610        620        630        640        650        660 
VLFVMISNWN NDRIEQDLVG SCNDAASYCG IRDRKYPDKQ AMGYPFDRKM ANDAATLSDF 

       670        680 
LRPNMAVRDC SIQFSDTTVE RGQQG 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"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
AF003253 mRNA. Translation: AAC05796.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HHSX-ray1.97B2-685[»]
ProteinModelPortalO44249.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48978N.

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 namePRP1_MANSE
AccessionPrimary (citable) accession number: O44249
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