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Q9W1V6

- PRPD3_DROME

UniProt

Q9W1V6 - PRPD3_DROME

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Protein
Diphenoloxidase subunit A3
Gene
proPO59, Dox-3, Dox-A3, CG42640
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Binds 2 copper ions per subunit By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi209 – 2091Copper A By similarityBy similarity
Metal bindingi213 – 2131Copper A By similarityBy similarity
Metal bindingi239 – 2391Copper A By similarityBy similarity
Metal bindingi366 – 3661Copper B By similarityBy similarity
Metal bindingi370 – 3701Copper B By similarityBy similarity
Metal bindingi406 – 4061Copper B By similarityBy similarity

GO - Molecular functioni

  1. L-DOPA monooxygenase activity Source: FlyBase
  2. dopamine monooxygenase activity Source: FlyBase
  3. metal ion binding Source: UniProtKB-KW
  4. monophenol monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. dopamine metabolic process Source: FlyBase
  2. melanin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Diphenoloxidase subunit A3 (EC:1.14.18.1)
Alternative name(s):
Diphenol oxidase A3
Prophenoloxidase 59
Tyrosinase A3
Gene namesi
Name:proPO59
Synonyms:Dox-3, Dox-A3
ORF Names:CG42640
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0261363. proPO59.

Subcellular locationi

Secreted By similarity
Note: Expression not detected in larval hemolymph.By similarity1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4848 By similarity
PRO_0000035905Add
BLAST
Chaini51 – 683633Diphenoloxidase subunit A31 Publication
PRO_0000035906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi358 – 3581N-linked (GlcNAc...) Reviewed prediction
Glycosylationi492 – 4921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi546 – 5461N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi574 ↔ 617 By similarity
Disulfide bondi576 ↔ 624 By similarity

Post-translational modificationi

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

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

Structurei

3D structure databases

ProteinModelPortaliQ9W1V6.
SMRiQ9W1V6. Positions 4-673.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.

Phylogenomic databases

eggNOGiNOG297156.
GeneTreeiENSGT00730000111961.
InParanoidiQ9W1V6.
KOiK00505.
OMAiITHEDRT.
OrthoDBiEOG7XPZ54.
PhylomeDBiQ9W1V6.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. 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]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSiPR00187. HAEMOCYANIN.
SUPFAMiSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9W1V6-1 [UniParc]FASTAAdd to Basket

« Hide

MADKKNLLLL FDHPTEPVFM DKGGNGTVFD VPDSYVTDRY NQMCKKVQRR    50
VSSASEKNVQ VKEIAIPDLS CSMRLGRSEQ FSIFLKSHRK MASHLIEIFT 100
KMQTVDELQS VAVYARDRVN PVLFNYALSV ALLHRPDTKD LELPAFAQTF 150
PDRFIDSKML RSMREESFVV ERSAARLPVV SSVKYTASDL DVEHRLWYFR 200
EDLGVNLHHW HWHLVYPIEA PDRSIVDKDR RGELFYYMHQ QIIARYNAER 250
LSNHMARVQP FNNLDEPIAE GYFPKMDSLV ASRAYPPRFD NTRLSDVDRP 300
NNQLRVGIDD MKRWRERIYE AIHQGYVLDT NNEKIVLDDA KGIDILGNII 350
EASDLTPNST LYGDFHNMGH ILIAYSHDPT NKHLEYAGVM GDASTAMRDP 400
IFYKWHAFID NMFQEHKRLL SPYEKQELSF PDVRVESIQV ESQGQVNRLT 450
TFWQESDVDM SRGLDFVPRG HVLARFTHLQ HHEFSYTIKV ENSSEATRYG 500
YVRIFLAPKL DDRNAPMLLE QQRLMMVELD KFVVTMPPGS HTITRNSTES 550
SVTIPFERTF RNLDKLEELQ NFLCGCGWPQ HMLIPKGRPE GLRFELFVMV 600
SNYEEDKVDQ TVADCGCSIA ASYCGLRDRL YPDRKSMGFP FDRKPRRGSE 650
ILENFLTPNM CAVEVIITHE DRTEKLREVP ARS 683
Length:683
Mass (Da):79,314
Last modified:May 1, 2000 - v1
Checksum:i437CBDD9E8A278BF
GO

Sequence cautioni

The sequence BAB43866.1 differs from that shown. Reason: Chimeric cDNA. It is a chimera between Dox-A3 and CG8193.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti246 – 2461Y → N in AAL29172. 1 Publication
Sequence conflicti491 – 4911E → D in AAL29172. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_080021.3.
UniGeneiDm.1829.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF46946.1 .
AY061624 mRNA. Translation: AAL29172.1 .
AB055857 Genomic DNA. Translation: BAB43866.1 . Sequence problems.
RefSeqi NP_524760.1. NM_080021.3.
UniGenei Dm.1829.

3D structure databases

ProteinModelPortali Q9W1V6.
SMRi Q9W1V6. Positions 4-673.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q9W1V6.
PRIDEi Q9W1V6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0302290 ; FBpp0291496 ; FBgn0261363 .
GeneIDi 44513.
KEGGi dme:Dmel_CG42640.

Organism-specific databases

CTDi 44513.
FlyBasei FBgn0261363. proPO59.

Phylogenomic databases

eggNOGi NOG297156.
GeneTreei ENSGT00730000111961.
InParanoidi Q9W1V6.
KOi K00505.
OMAi ITHEDRT.
OrthoDBi EOG7XPZ54.
PhylomeDBi Q9W1V6.

Miscellaneous databases

GenomeRNAii 44513.
NextBioi 795776.

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProi IPR013788. 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 ]
PANTHERi PTHR11511. PTHR11511. 1 hit.
Pfami PF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view ]
PRINTSi PR00187. HAEMOCYANIN.
SUPFAMi SSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. "Prophenol oxidase A3 in Drosophila melanogaster: activation and the PCR-based cDNA sequence."
    Asada N., Yokoyama G., Kawamoto N., Norioka S., Hatta T.
    Biochem. Genet. 41:151-163(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-664, PROTEOLYTIC CLEAVAGE.
    Strain: Oregon-R.
    Tissue: Larva and Pupae.
  5. "Identification of the gene encoding pro-phenoloxidase A(3) in the fruitfly, Drosophila melanogaster."
    Asano T., Takebuchi K.
    Insect Mol. Biol. 18:223-232(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiPRPD3_DROME
AccessioniPrimary (citable) accession number: Q9W1V6
Secondary accession number(s): Q95R43, Q9BLD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

Similar proteinsi