Reviewed, UniProtKB/Swiss-Prot Q8I1F6 (PRPA3_DROER)

Names and origin

Protein names

Recommended name:
    Probable phenoloxidase subunit A3
    EC=1.14.18.1
Alternative name(s):
    Tyrosinase A3
    PO A3

Gene names

Name:

Dox-A3

Organism

Drosophila erecta (Fruit fly)

Taxonomic identifier

7220 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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 quinon.
Catalytic activity	L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O.
Cofactor	Binds 2 copper ions per subunit By similarity. UniProtKB Q27451
Subcellular location	Secreted By similarity. UniProtKB Q27451
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 Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	melanin biosynthetic process from tyrosine Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Inferred from electronic annotation. Source: EC oxygen transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 50	50	By similarity UniProtKB Q27451		PRO_0000035903
	Chain	51 – 683	633	Probable phenoloxidase 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

Sequences

	Sequence		Length	Mass (Da)
	Q8I1F6-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 9FF9A0E2A970662A	FASTA	683	79,054
	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 AIHQGYVMDA 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 SVTIPFERTF RNMDNPGQLQ NFLCGCGWPQ HMLIPKGRAE GLSFELFVMV 610 620 630 640 650 660 SNYEDDKVDQ KPEDCECSIA ASYCGLRDRL YPDRKSMGFP FDRQPRSGSE LLEKFLTPNM 670 680 CSIEVIISHE ARTEKIPELP DHS

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: 12537575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY190941 Genomic DNA. Translation: AAO01013.1.
3D structure databases
HSSP	HSSP built from PDB template 1OXY based on UniProtKB P04253.
ModBase	Search...
Organism-specific databases
FlyBase	FBgn0064624. Dere\Dox-A3.
Enzyme and pathway databases
BRENDA	1.14.18.1. 278534.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR013788. Hemocyanin. IPR005203. Hemocyanin_C. IPR000896. Hemocyanin_Cu. IPR005204. Hemocyanin_N. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit. G3DSA:2.60.40.1520. hemocyanin_C. 1 hit. G3DSA:1.20.1370.10. hemocyanin_N. 1 hit.
PANTHER	PTHR11511. Hemocyanin. 1 hit.
Pfam	PF03723. Hemocyanin_C. 1 hit. PF00372. Hemocyanin_M. 1 hit. PF03722. Hemocyanin_N. 1 hit. [Graphical view]
PRINTS	PR00187. HAEMOCYANIN.
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

PRPA3_DROER

Accession

Primary (citable) accession number: Q8I1F6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project