Q8I1F6 (PRPD3_DROER) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Diphenoloxidase subunit A3
EC=1.14.18.1

Alternative name(s):
Tyrosinase A3

Gene names

Name:	Dox-A3
ORF Names:	GG22822

Organism

Drosophila erecta (Fruit fly) [Complete proteome]

Taxonomic identifier

7220 [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	Inferred from homology

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 UniProtKB Q27451.
Post-translational modification	Upon activation, a trypsin type protease cleaves prophenol oxidase to yield the active enzyme By similarity.
Sequence similarities	Belongs to the tyrosinase family.

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
Gene Ontology (GO)
Biological_process	melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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_0000035903
	Chain	51 – 683	633	Diphenoloxidase subunit A3 UniProtKB Q27451		PRO_0000035904
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	25	1	N-linked (GlcNAc...) Potential
	Glycosylation	358	1	N-linked (GlcNAc...) Potential
	Glycosylation	492	1	N-linked (GlcNAc...) Potential
	Glycosylation	514	1	N-linked (GlcNAc...) Potential
	Disulfide bond	574 ↔ 617		By similarity
	Disulfide bond	576 ↔ 624		By similarity
Experimental info
	Sequence conflict	328	1	L → M in AAO01013. Ref.1
	Sequence conflict	557	1	K → E in AAO01013. Ref.1
	Sequence conflict	568 – 569	2	EP → QL in AAO01013. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8I1F6 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: E8955B2798B6C260	FASTA	683	79,020
	10 20 30 40 50 60 MADKKNLLLL FDHPTEPVFM DKGGNGTVFD VPASYVTDRY NKMCKKVQRR VSGGFEKNVL 70 80 90 100 110 120 VKEIPIPDLS CSMRLGRSEQ FSLFLESHRQ MACHLIDVFI KMPTVDELQS VAVYARDRVN 130 140 150 160 170 180 PVLFNYALSV AMLHRSDTKD LGLPAFAQIF PDRFIDSQML RTMREESFVV ERSAARLPVH 190 200 210 220 230 240 SSVKYTASDL DVEHRLWYFR EDLGVNLHHW HWHLVYPNTA PDRSIVDKDR RGELFYYMHQ 250 260 270 280 290 300 QIIARYNAER LCNHMARVQP FNNLEEPIAE GYFPKMDSLV ASRAFPPRFD NTRLSDVDRP 310 320 330 340 350 360 INQLRVGIDD MKRWRERIYE AIHQGYVLDA NHKKIVLDDV KGIDILGNII ESSQLTPNKT 370 380 390 400 410 420 LYGDLHNKGH ILIAFSHDPT NKHLEYAGVM GDASTAMRDP IFYKWHAFID NLFQEHKRQL 430 440 450 460 470 480 SPYTEEDLTF PDVRVQSIQV ESQGQVNRLT TFWQESDVDM SRGLDFVPRG HVLARFTHLQ 490 500 510 520 530 540 HHPFSYTIEV ENSSEATRYG YVRIFLAPKL DDGNATMLLE QQRRMMVELD KFVVTMPPGS 550 560 570 580 590 600 HTITRDSTES SVTIPFKRTF RNMDNPGEPQ NFLCGCGWPQ HMLIPKGRAE GLSFELFVMV 610 620 630 640 650 660 SNYEDDKVDQ KPEDCECSIA ASYCGLRDRL YPDRKSMGFP FDRQPRSGSE LLEKFLTPNM 670 680 CSIEVIISHE ARTEKIPELP DHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Assessing the impact of comparative genomic sequence data on the functional annotation of the Drosophila genome." Bergman C.M., Pfeiffer B.D., Rincon-Limas D.E., Hoskins R.A., Gnirke A., Mungall C.J., Wang A.M., Kronmiller B., Pacleb J.M., Park S., Stapleton M., Wan K.H., George R.A., de Jong P.J., Botas J., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0086.1-RESEARCH0086.20(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Evolution of genes and genomes on the Drosophila phylogeny." Drosophila 12 genomes consortium Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tucson 14021-0224.01.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY190941 Genomic DNA. Translation: AAO01013.1. CH954179 Genomic DNA. Translation: EDV56739.1.
RefSeq	XP_001976339.1. XM_001976303.1.
3D structure databases
ProteinModelPortal	Q8I1F6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0142876; FBpp0141368; FBgn0064624.
GeneID	6547312.
KEGG	der:Dere_GG22822.
Organism-specific databases
FlyBase	FBgn0064624. Dere\GG22822.
Phylogenomic databases
KO	K00505.
OrthoDB	EOG4DJHBF.
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...

Entry information

Entry name

PRPD3_DROER

Accession

Primary (citable) accession number: Q8I1F6
Secondary accession number(s): B3NP06

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	September 22, 2009
Last modified:	April 3, 2013
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project