Diphenoloxidase subunit A3 precursor - Drosophila erecta (Fruit fly)

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Reviewed, UniProtKB/Swiss-Prot Q8I1F6 (PRPD3_DROER)

Last modified February 9, 2010. Version 41. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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)

Taxonomic identifier

7220 [NCBI]

Taxonomic lineage

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

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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.

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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	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.
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.

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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 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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 48

By similarity

PRO_0000035903

Chain

51 – 683

633

Diphenoloxidase subunit A3 UniProtKB Q27451

PRO_0000035904

Sites

Metal binding

209

Copper A By similarity UniProtKB Q27451

Metal binding

213

Copper A By similarity UniProtKB Q27451

Metal binding

239

Copper A By similarity UniProtKB Q27451

Metal binding

366

Copper B By similarity UniProtKB Q27451

Metal binding

370

Copper B By similarity UniProtKB Q27451

Metal binding

406

Copper B By similarity UniProtKB Q27451

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

358

N-linked (GlcNAc...) Potential

Glycosylation

492

N-linked (GlcNAc...) Potential

Glycosylation

514

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

328

L → M in AAO01013. Ref.1

Sequence conflict

557

K → E in AAO01013. Ref.1

Sequence conflict

568 – 569

EP → QL in AAO01013. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8I1F6-1 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: E8955B2798B6C260
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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

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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: 12537575] [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: 17994087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tucson 14021-0224.01.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AY190941 Genomic DNA. Translation: AAO01013.1. CH954179 Genomic DNA. Translation: EDV56739.1.
RefSeq	XP_001976339.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6547312.
KEGG	der:Dere_GG22822.
Organism-specific databases
FlyBase	FBgn0064624. Dere\GG22822.
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. IPR014756. Ig_E-set. 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...

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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:	February 9, 2010
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project

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Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents