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Protein

Phenoloxidase 3

Gene

PPO3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi209Copper ABy similarity1
Metal bindingi213Copper ABy similarity1
Metal bindingi239Copper ABy similarity1
Metal bindingi366Copper BBy similarity1
Metal bindingi370Copper BBy similarity1
Metal bindingi406Copper BBy similarity1

GO - Molecular functioni

  • dopamine monooxygenase activity Source: FlyBase
  • L-DOPA monooxygenase activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW
  • monophenol monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  • dopamine metabolic process Source: FlyBase
  • melanin biosynthetic process Source: UniProtKB-KW
  • melanotic encapsulation of foreign target Source: FlyBase

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processMelanin biosynthesis
LigandCopper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phenoloxidase 3 (EC:1.14.18.1)
Alternative name(s):
Diphenol oxidase A3
Diphenoloxidase subunit A3
Prophenoloxidase 59
Tyrosinase A3
Gene namesi
Name:PPO3
Synonyms:Dox-3, Dox-A3, proPO59
ORF Names:CG42640
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0261363. PPO3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000359051 – 48By similarityAdd BLAST48
ChainiPRO_000003590651 – 683Phenoloxidase 3Add BLAST633

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi358N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi492N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi546N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi574 ↔ 617By similarity
Disulfide bondi576 ↔ 624By similarity

Post-translational modificationi

Upon activation, a trypsin type protease cleaves prophenol oxidase to yield the active enzyme.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9W1V6.
PRIDEiQ9W1V6.

Expressioni

Developmental stagei

Expression is very low during all stages of development.1 Publication

Gene expression databases

BgeeiFBgn0261363.
ExpressionAtlasiQ9W1V6. differential.
GenevisibleiQ9W1V6. DM.

Interactioni

Protein-protein interaction databases

BioGridi69098. 1 interactor.
STRINGi7227.FBpp0291496.

Structurei

3D structure databases

ProteinModelPortaliQ9W1V6.
SMRiQ9W1V6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Phylogenomic databases

eggNOGiENOG410IKED. Eukaryota.
ENOG4111KTW. LUCA.
InParanoidiQ9W1V6.
KOiK00505.
OMAiDRKSMGF.
OrthoDBiEOG091G03VO.
PhylomeDBiQ9W1V6.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiView protein in InterPro
IPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR037020. Hemocyanin_C_sf.
IPR005204. Hemocyanin_N.
IPR036697. Hemocyanin_N_sf.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiView protein in Pfam
PF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
PRINTSiPR00187. HAEMOCYANIN.
SUPFAMiSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiView protein in PROSITE
PS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9W1V6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADKKNLLLL FDHPTEPVFM DKGGNGTVFD VPDSYVTDRY NQMCKKVQRR
60 70 80 90 100
VSSASEKNVQ VKEIAIPDLS CSMRLGRSEQ FSIFLKSHRK MASHLIEIFT
110 120 130 140 150
KMQTVDELQS VAVYARDRVN PVLFNYALSV ALLHRPDTKD LELPAFAQTF
160 170 180 190 200
PDRFIDSKML RSMREESFVV ERSAARLPVV SSVKYTASDL DVEHRLWYFR
210 220 230 240 250
EDLGVNLHHW HWHLVYPIEA PDRSIVDKDR RGELFYYMHQ QIIARYNAER
260 270 280 290 300
LSNHMARVQP FNNLDEPIAE GYFPKMDSLV ASRAYPPRFD NTRLSDVDRP
310 320 330 340 350
NNQLRVGIDD MKRWRERIYE AIHQGYVLDT NNEKIVLDDA KGIDILGNII
360 370 380 390 400
EASDLTPNST LYGDFHNMGH ILIAYSHDPT NKHLEYAGVM GDASTAMRDP
410 420 430 440 450
IFYKWHAFID NMFQEHKRLL SPYEKQELSF PDVRVESIQV ESQGQVNRLT
460 470 480 490 500
TFWQESDVDM SRGLDFVPRG HVLARFTHLQ HHEFSYTIKV ENSSEATRYG
510 520 530 540 550
YVRIFLAPKL DDRNAPMLLE QQRLMMVELD KFVVTMPPGS HTITRNSTES
560 570 580 590 600
SVTIPFERTF RNLDKLEELQ NFLCGCGWPQ HMLIPKGRPE GLRFELFVMV
610 620 630 640 650
SNYEEDKVDQ TVADCGCSIA ASYCGLRDRL YPDRKSMGFP FDRKPRRGSE
660 670 680
ILENFLTPNM CAVEVIITHE DRTEKLREVP ARS
Length:683
Mass (Da):79,314
Last modified:May 1, 2000 - v1
Checksum:i437CBDD9E8A278BF
GO

Sequence cautioni

The sequence BAB43866 differs from that shown. Chimeric cDNA. It is a chimera between Dox-A3 and CG8193.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti246Y → N in AAL29172 (PubMed:12537569).Curated1
Sequence conflicti491E → D in AAL29172 (PubMed:12537569).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF46946.1.
AY061624 mRNA. Translation: AAL29172.1.
AB055857 Genomic DNA. Translation: BAB43866.1. Sequence problems.
RefSeqiNP_524760.1. NM_080021.4.

Genome annotation databases

EnsemblMetazoaiFBtr0302290; FBpp0291496; FBgn0261363.
GeneIDi44513.
KEGGidme:Dmel_CG42640.

Similar proteinsi

Entry informationi

Entry nameiPPO3_DROME
AccessioniPrimary (citable) accession number: Q9W1V6
Secondary accession number(s): Q95R43, Q9BLD9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2000
Last modified: October 25, 2017
This is version 118 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families