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Q9V521 (PRPA3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. 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:
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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5050
PRO_0000035907
Chain51 – 684634Phenoloxidase subunit A3
PRO_0000035908

Sites

Metal binding2081Copper A By similarity
Metal binding2121Copper A By similarity
Metal binding2381Copper A By similarity
Metal binding3651Copper B By similarity
Metal binding3691Copper B By similarity
Metal binding4051Copper B By similarity

Amino acid modifications

Glycosylation4481N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation6651N-linked (GlcNAc...) Potential
Glycosylation6771N-linked (GlcNAc...) Potential
Disulfide bond581 ↔ 623 By similarity
Disulfide bond583 ↔ 630 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V521 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 16F946FFEEDB72EA

FASTA68479,285
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_610443.1. NM_136599.3.
UniGeneDm.538.

3D structure databases

ProteinModelPortalQ9V521.
SMRQ9V521. Positions 4-681.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61748. 8 interactions.
MINTMINT-982292.
STRING7227.FBpp0087744.

Proteomic databases

PaxDbQ9V521.
PRIDEQ9V521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088663; FBpp0087744; FBgn0033367.
GeneID35910.
KEGGdme:Dmel_CG8193.
UCSCCG8193-RA. d. melanogaster.

Organism-specific databases

CTD35910.
FlyBaseFBgn0033367. CG8193.

Phylogenomic databases

eggNOGNOG131652.
GeneTreeENSGT00730000111961.
InParanoidQ9V521.
OrthoDBEOG7XPZ54.
PhylomeDBQ9V521.

Gene expression databases

BgeeQ9V521.

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.
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...

Other

GenomeRNAi35910.
NextBio795776.

Entry information

Entry namePRPA3_DROME
AccessionPrimary (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: April 16, 2014
This is version 93 of the entry and version 1 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