Q9V521 (PRPA3_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenoloxidase subunit A3
Short name=PO A3
EC=1.14.18.1

Alternative name(s):
Processed phenoloxidase A3
Short name=Pro-phenoloxidase A3

Gene names

Name:	proPo-A3
ORF Names:	CG8193

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	684 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 quinonee 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. Note: Expressed in larval hemolymph. Ref.4 Ref.5
Developmental stage	Expression is high during the larval stage, predominantly in the feeding and wandering larvae. 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	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 space Inferred from direct assay Ref.5. Source: FlyBase
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 – 50	50	Ref.4		PRO_0000035907
	Chain	51 – 684	634	Phenoloxidase subunit A3 Ref.4		PRO_0000035908
Sites
	Metal binding	208	1	Copper A By similarity UniProtKB Q27451
	Metal binding	212	1	Copper A By similarity UniProtKB Q27451
	Metal binding	238	1	Copper A By similarity UniProtKB Q27451
	Metal binding	365	1	Copper B By similarity UniProtKB Q27451
	Metal binding	369	1	Copper B By similarity UniProtKB Q27451
	Metal binding	405	1	Copper B By similarity UniProtKB Q27451
Amino acid modifications
	Glycosylation	448	1	N-linked (GlcNAc...) Potential
	Glycosylation	492	1	N-linked (GlcNAc...) Potential
	Glycosylation	665	1	N-linked (GlcNAc...) Potential
	Glycosylation	677	1	N-linked (GlcNAc...) Potential
	Disulfide bond	581 ↔ 623		By similarity
	Disulfide bond	583 ↔ 630		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9V521 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 16F946FFEEDB72EA	FASTA	684	79,285
	10 20 30 40 50 60 MADKKNLLLL FDHPTEPVFM DKGKRVTVFD VPDSFLTDRY RPISNEVQSR VGDKVEQRVP 70 80 90 100 110 120 VREISIPDLR IPMSLGRDEQ FSLFLPKHRR IAGRLIDIFM NMRSVDDLQS VAVYARDRVN 130 140 150 160 170 180 PVLFNYALSV ALLHRPDTQG LDLPSFSQTF PDRFIDSQVI RKMREESFVV QPGSRMPITI 190 200 210 220 230 240 PRDYTASDLD PEHRLWYFRE DLGINLHHWH WHLVYPFEAS DRSIVAKDRR GELFYYMHQQ 250 260 270 280 290 300 VIARYNAERF SNNLARVLPF NNLRDPIAEG YFPKMDSLVA SRAWPPRFES TRLSDLNRES 310 320 330 340 350 360 DQLNVEIGDL ERWRDRIYEA IHQGFVMDER GNRVPLDEAT GIDTLGNMIE SSILSPNRVL 370 380 390 400 410 420 YGDLHNNGHT FISYAHDPTS KHLESFGVMG DVSTAMRDPV FYKWHSYIDR IFQEHKSRLP 430 440 450 460 470 480 AYTENQLNYP GVSIAGIQVD TNGGRPNNLT TFWQQSDVDM SRGFDFLPRG NVFARFTHLQ 490 500 510 520 530 540 HLPFTYTISL NNDSGAQRFG YVRIFMAPKN DERGQPMLMR DQRSMMIELD KFVTSLNPGP 550 560 570 580 590 600 NTIRRRSTES SVTIPFERTF RNLDANRPAA GTPEELEFNF CGCGWPNHML VPKGLPEGLQ 610 620 630 640 650 660 CVLFIMVSNY ENDRIDQQLV GRCSDAASYC GVRDRLYPDR QSMGFPFDRL PRSGVDRLVN 670 680 FLTPNMSIVD VNIRHENRTV QRPN

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: Head.
[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 1-670, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION. 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: AAF59001.1. AY060652 mRNA. Translation: AAL28200.1. AB055857 Genomic DNA. Translation: BAB43866.1. Sequence problems.
RefSeq	NP_610443.1. NM_136599.3.
UniGene	Dm.538.
3D structure databases
ProteinModelPortal	Q9V521.
SMR	Q9V521. Positions 4-681.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-982292.
STRING	7227.FBpp0087744.
Proteomic databases
PaxDb	Q9V521.
PRIDE	Q9V521.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0088663; FBpp0087744; FBgn0033367.
GeneID	35910.
KEGG	dme:Dmel_CG8193.
UCSC	CG8193-RA. d. melanogaster.
Organism-specific databases
CTD	35910.
FlyBase	FBgn0033367. CG8193.
Phylogenomic databases
eggNOG	NOG131652.
GeneTree	ENSGT00530000063973.
InParanoid	Q9V521.
OrthoDB	EOG408KPZ.
PhylomeDB	Q9V521.
Gene expression databases
Bgee	Q9V521.
GermOnline	CG8193. 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	35910.
NextBio	795776.

Entry information

Entry name

PRPA3_DROME

Accession

Primary (citable) accession number: Q9V521
Secondary accession number(s): 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 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project