Q9W1V6 (PRPD3_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Diphenoloxidase subunit A3
EC=1.14.18.1

Alternative name(s):
Diphenol oxidase A3
Tyrosinase A3

Gene names

Name:	Dox-A3
Synonyms:	Dox-3
ORF Names:	CG42640

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	683 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 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.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Cellular component	Secreted
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dopamine metabolic process Inferred by curator PubMed 22120533. Source: FlyBase melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	L-DOPA monooxygenase activity Inferred from direct assay PubMed 22120533. Source: FlyBase dopamine monooxygenase activity Inferred from direct assay PubMed 22120533. Source: FlyBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 48	48	By similarity		PRO_0000035905
	Chain	51 – 683	633	Diphenoloxidase subunit A3 Ref.1		PRO_0000035906
Sites
	Metal binding	209	1	Copper A By similarity UniProtKB Q27451
	Metal binding	213	1	Copper A By similarity UniProtKB Q27451
	Metal binding	239	1	Copper A By similarity UniProtKB Q27451
	Metal binding	366	1	Copper B By similarity UniProtKB Q27451
	Metal binding	370	1	Copper B By similarity UniProtKB Q27451
	Metal binding	406	1	Copper B By similarity UniProtKB Q27451
Amino acid modifications
	Glycosylation	358	1	N-linked (GlcNAc...) Potential
	Glycosylation	492	1	N-linked (GlcNAc...) Potential
	Glycosylation	546	1	N-linked (GlcNAc...) Potential
	Disulfide bond	574 ↔ 617		By similarity
	Disulfide bond	576 ↔ 624		By similarity
Experimental info
	Sequence conflict	246	1	Y → N in AAL29172. Ref.3
	Sequence conflict	491	1	E → D in AAL29172. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9W1V6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 437CBDD9E8A278BF	FASTA	683	79,314
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
RefSeq	NP_524760.1. NM_080021.3.
UniGene	Dm.1829.
3D structure databases
ProteinModelPortal	Q9W1V6.
SMR	Q9W1V6. Positions 4-673.
ModBase	Search...
Proteomic databases
PaxDb	Q9W1V6.
PRIDE	Q9W1V6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0302290; FBpp0291496; FBgn0261363.
GeneID	44513.
KEGG	dme:Dmel_CG42640.
Organism-specific databases
CTD	44513.
FlyBase	FBgn0261375. Dox-A3.
Phylogenomic databases
eggNOG	NOG297156.
GeneTree	ENSGT00530000063973.
InParanoid	Q9W1V6.
KO	K00505.
OMA	ITHEDRT.
OrthoDB	EOG4DJHBF.
PhylomeDB	Q9W1V6.
Gene expression databases
GermOnline	CG2952. Drosophila melanogaster.
Family and domain databases
Gene3D	1.10.1280.10. 1 hit. 1.20.1370.10. 1 hit. 2.60.40.1520. 1 hit.
InterPro	IPR013788. Hemocyanin/hexamerin. IPR000896. Hemocyanin/hexamerin_mid_dom. IPR005203. Hemocyanin_C. IPR005204. Hemocyanin_N. IPR014756. Ig_E-set. IPR002227. Tyrosinase. IPR008922. Unchr_di-copper_centre. [Graphical view]
PANTHER	PTHR11511. PTHR11511. 1 hit.
Pfam	PF03723. Hemocyanin_C. 1 hit. PF00372. Hemocyanin_M. 1 hit. PF03722. Hemocyanin_N. 1 hit. [Graphical view]
PRINTS	PR00187. HAEMOCYANIN.
SUPFAM	SSF48056. Di-copper_centre. 1 hit. SSF48050. Hemocyanin_N. 1 hit. SSF81296. Ig_E-set. 1 hit.
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...
Other
GenomeRNAi	44513.
NextBio	795776.

Entry information

Entry name

PRPD3_DROME

Accession

Primary (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:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project