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Q8I1F6 (PRPD3_DROER) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diphenoloxidase subunit A3

EC=1.14.18.1
Alternative name(s):
Tyrosinase A3
Gene names
Name:proPO59
Synonyms:Dox-A3
ORF Names:GG22822
OrganismDrosophila erecta (Fruit fly) [Complete proteome]
Taxonomic identifier7220 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 processMelanin biosynthesis
   Cellular componentSecreted
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processmelanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

monophenol monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4848 By similarity
PRO_0000035903
Chain51 – 683633Diphenoloxidase subunit A3 UniProtKB Q27451
PRO_0000035904

Sites

Metal binding2091Copper A By similarity UniProtKB Q27451
Metal binding2131Copper A By similarity UniProtKB Q27451
Metal binding2391Copper A By similarity UniProtKB Q27451
Metal binding3661Copper B By similarity UniProtKB Q27451
Metal binding3701Copper B By similarity UniProtKB Q27451
Metal binding4061Copper B By similarity UniProtKB Q27451

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation5141N-linked (GlcNAc...) Potential
Disulfide bond574 ↔ 617 By similarity
Disulfide bond576 ↔ 624 By similarity

Experimental info

Sequence conflict3281L → M in AAO01013. Ref.1
Sequence conflict5571K → E in AAO01013. Ref.1
Sequence conflict568 – 5692EP → QL in AAO01013. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8I1F6 [UniParc].

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

FASTA68379,020
        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 

« Hide

References

« Hide '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.
RefSeqXP_001976339.1. XM_001976303.1.

3D structure databases

ProteinModelPortalQ8I1F6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0142876; FBpp0141368; FBgn0064624.
GeneID6547312.
KEGGder:Dere_GG22822.

Organism-specific databases

FlyBaseFBgn0064624. Dere\GG22822.

Phylogenomic databases

KOK00505.
OrthoDBEOG7XPZ54.
PhylomeDBQ8I1F6.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERPTHR11511. PTHR11511. 1 hit.
PfamPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSPR00187. HAEMOCYANIN.
SUPFAMSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRPD3_DROER
AccessionPrimary (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: July 9, 2014
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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