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Q9W1V6 (PRPD3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. 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:
Diphenoloxidase subunit A3

EC=1.14.18.1
Alternative name(s):
Diphenol oxidase A3
Prophenoloxidase 59
Tyrosinase A3
Gene names
Name:proPO59
Synonyms:Dox-3, Dox-A3
ORF Names:CG42640
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length683 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 By similarity.

Catalytic activity

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

L-tyrosine + O2 = dopaquinone + H2O.

Cofactor

Binds 2 copper ions per subunit By similarity. UniProtKB Q27451

Subcellular location

Secreted By similarity. Note: Expression not detected in larval hemolymph. Ref.5 UniProtKB Q9V521

Developmental stage

Expression is very low during all stages of development. Ref.5

Post-translational modification

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

Sequence similarities

Belongs to the tyrosinase family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4848 By similarity
PRO_0000035905
Chain51 – 683633Diphenoloxidase subunit A3 Ref.1
PRO_0000035906

Sites

Metal binding2091Copper A By similarity UniProtKB Q27451
Metal binding2131Copper A By similarity UniProtKB Q27451
Metal binding2391Copper A By similarity UniProtKB Q27451
Metal binding3661Copper B By similarity UniProtKB Q27451
Metal binding3701Copper B By similarity UniProtKB Q27451
Metal binding4061Copper B By similarity UniProtKB Q27451

Amino acid modifications

Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation5461N-linked (GlcNAc...) Potential
Disulfide bond574 ↔ 617 By similarity
Disulfide bond576 ↔ 624 By similarity

Experimental info

Sequence conflict2461Y → N in AAL29172. Ref.3
Sequence conflict4911E → D in AAL29172. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9W1V6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 437CBDD9E8A278BF

FASTA68379,314
        10         20         30         40         50         60 
MADKKNLLLL FDHPTEPVFM DKGGNGTVFD VPDSYVTDRY NQMCKKVQRR VSSASEKNVQ 

        70         80         90        100        110        120 
VKEIAIPDLS CSMRLGRSEQ FSIFLKSHRK MASHLIEIFT KMQTVDELQS VAVYARDRVN 

       130        140        150        160        170        180 
PVLFNYALSV ALLHRPDTKD LELPAFAQTF PDRFIDSKML RSMREESFVV ERSAARLPVV 

       190        200        210        220        230        240 
SSVKYTASDL DVEHRLWYFR EDLGVNLHHW HWHLVYPIEA PDRSIVDKDR RGELFYYMHQ 

       250        260        270        280        290        300 
QIIARYNAER LSNHMARVQP FNNLDEPIAE GYFPKMDSLV ASRAYPPRFD NTRLSDVDRP 

       310        320        330        340        350        360 
NNQLRVGIDD MKRWRERIYE AIHQGYVLDT NNEKIVLDDA KGIDILGNII EASDLTPNST 

       370        380        390        400        410        420 
LYGDFHNMGH ILIAYSHDPT NKHLEYAGVM GDASTAMRDP IFYKWHAFID NMFQEHKRLL 

       430        440        450        460        470        480 
SPYEKQELSF PDVRVESIQV ESQGQVNRLT TFWQESDVDM SRGLDFVPRG HVLARFTHLQ 

       490        500        510        520        530        540 
HHEFSYTIKV ENSSEATRYG YVRIFLAPKL DDRNAPMLLE QQRLMMVELD KFVVTMPPGS 

       550        560        570        580        590        600 
HTITRNSTES SVTIPFERTF RNLDKLEELQ NFLCGCGWPQ HMLIPKGRPE GLRFELFVMV 

       610        620        630        640        650        660 
SNYEEDKVDQ TVADCGCSIA ASYCGLRDRL YPDRKSMGFP FDRKPRRGSE ILENFLTPNM 

       670        680 
CAVEVIITHE DRTEKLREVP ARS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013599 Genomic DNA. Translation: AAF46946.1.
AY061624 mRNA. Translation: AAL29172.1.
AB055857 Genomic DNA. Translation: BAB43866.1. Sequence problems.
RefSeqNP_524760.1. NM_080021.3.
UniGeneDm.1829.

3D structure databases

ProteinModelPortalQ9W1V6.
SMRQ9W1V6. Positions 4-673.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9W1V6.
PRIDEQ9W1V6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0302290; FBpp0291496; FBgn0261363.
GeneID44513.
KEGGdme:Dmel_CG42640.

Organism-specific databases

CTD44513.
FlyBaseFBgn0261363. proPO59.

Phylogenomic databases

eggNOGNOG297156.
GeneTreeENSGT00730000111961.
InParanoidQ9W1V6.
KOK00505.
OMAITHEDRT.
OrthoDBEOG7XPZ54.
PhylomeDBQ9W1V6.

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...

Other

GenomeRNAi44513.
NextBio795776.

Entry information

Entry namePRPD3_DROME
AccessionPrimary (citable) accession number: Q9W1V6
Secondary accession number(s): Q95R43, Q9BLD9
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase