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Q9V521

- PPO2_DROME

UniProt

Q9V521 - PPO2_DROME

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Protein

Phenoloxidase 2

Gene

PPO2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.
L-tyrosine + O2 = dopaquinone + H2O.

Cofactori

Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi208 – 2081Copper ABy similarity
Metal bindingi212 – 2121Copper ABy similarity
Metal bindingi238 – 2381Copper ABy similarity
Metal bindingi365 – 3651Copper BBy similarity
Metal bindingi369 – 3691Copper BBy similarity
Metal bindingi405 – 4051Copper BBy similarity

GO - Molecular functioni

  1. dopamine monooxygenase activity Source: FlyBase
  2. L-DOPA monooxygenase activity Source: FlyBase
  3. metal ion binding Source: UniProtKB-KW
  4. monophenol monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. defense response to fungus Source: FlyBase
  2. defense response to Gram-positive bacterium Source: FlyBase
  3. dopamine metabolic process Source: FlyBase
  4. melanin biosynthetic process Source: UniProtKB-KW
  5. melanization defense response Source: FlyBase
  6. melanotic encapsulation of foreign target Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phenoloxidase 2 (EC:1.14.18.1)
Short name:
PO A3
Alternative name(s):
Phenoloxidase subunit A3
Processed phenoloxidase A3
Short name:
Pro-phenoloxidase A3
Gene namesi
Name:PPO2
Synonyms:proPo-A3, proPO45
ORF Names:CG8193
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033367. PPO2.

Subcellular locationi

Secreted 2 Publications
Note: Expressed in larval hemolymph.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5050PRO_0000035907Add
BLAST
Chaini51 – 684634Phenoloxidase 2PRO_0000035908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi581 ↔ 623By similarity
Disulfide bondi583 ↔ 630By similarity
Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Upon activation, a trypsin type protease cleaves prophenol oxidase to yield the active enzyme.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9V521.
PRIDEiQ9V521.

Expressioni

Developmental stagei

Expression is high during the larval stage, predominantly in the feeding and wandering larvae.1 Publication

Gene expression databases

BgeeiQ9V521.

Interactioni

Protein-protein interaction databases

BioGridi61748. 8 interactions.
MINTiMINT-982292.
STRINGi7227.FBpp0087744.

Structurei

3D structure databases

ProteinModelPortaliQ9V521.
SMRiQ9V521. Positions 4-681.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Phylogenomic databases

eggNOGiNOG131652.
GeneTreeiENSGT00730000111961.
InParanoidiQ9V521.
OMAiLPAYTEN.
OrthoDBiEOG7XPZ54.
PhylomeDBiQ9V521.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. 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]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSiPR00187. HAEMOCYANIN.
SUPFAMiSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9V521-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADKKNLLLL FDHPTEPVFM DKGKRVTVFD VPDSFLTDRY RPISNEVQSR
60 70 80 90 100
VGDKVEQRVP VREISIPDLR IPMSLGRDEQ FSLFLPKHRR IAGRLIDIFM
110 120 130 140 150
NMRSVDDLQS VAVYARDRVN PVLFNYALSV ALLHRPDTQG LDLPSFSQTF
160 170 180 190 200
PDRFIDSQVI RKMREESFVV QPGSRMPITI PRDYTASDLD PEHRLWYFRE
210 220 230 240 250
DLGINLHHWH WHLVYPFEAS DRSIVAKDRR GELFYYMHQQ VIARYNAERF
260 270 280 290 300
SNNLARVLPF NNLRDPIAEG YFPKMDSLVA SRAWPPRFES TRLSDLNRES
310 320 330 340 350
DQLNVEIGDL ERWRDRIYEA IHQGFVMDER GNRVPLDEAT GIDTLGNMIE
360 370 380 390 400
SSILSPNRVL YGDLHNNGHT FISYAHDPTS KHLESFGVMG DVSTAMRDPV
410 420 430 440 450
FYKWHSYIDR IFQEHKSRLP AYTENQLNYP GVSIAGIQVD TNGGRPNNLT
460 470 480 490 500
TFWQQSDVDM SRGFDFLPRG NVFARFTHLQ HLPFTYTISL NNDSGAQRFG
510 520 530 540 550
YVRIFMAPKN DERGQPMLMR DQRSMMIELD KFVTSLNPGP NTIRRRSTES
560 570 580 590 600
SVTIPFERTF RNLDANRPAA GTPEELEFNF CGCGWPNHML VPKGLPEGLQ
610 620 630 640 650
CVLFIMVSNY ENDRIDQQLV GRCSDAASYC GVRDRLYPDR QSMGFPFDRL
660 670 680
PRSGVDRLVN FLTPNMSIVD VNIRHENRTV QRPN
Length:684
Mass (Da):79,285
Last modified:May 1, 2000 - v1
Checksum:i16F946FFEEDB72EA
GO

Sequence cautioni

The sequence BAB43866.1 differs from that shown. Reason: Chimeric cDNA. It is a chimera between Dox-A3 and PPO2.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF59001.1.
AY060652 mRNA. Translation: AAL28200.1.
AB055857 Genomic DNA. Translation: BAB43866.1. Sequence problems.
RefSeqiNP_610443.1. NM_136599.4.
UniGeneiDm.538.

Genome annotation databases

EnsemblMetazoaiFBtr0088663; FBpp0087744; FBgn0033367.
GeneIDi35910.
KEGGidme:Dmel_CG8193.
UCSCiCG8193-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF59001.1 .
AY060652 mRNA. Translation: AAL28200.1 .
AB055857 Genomic DNA. Translation: BAB43866.1 . Sequence problems.
RefSeqi NP_610443.1. NM_136599.4.
UniGenei Dm.538.

3D structure databases

ProteinModelPortali Q9V521.
SMRi Q9V521. Positions 4-681.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 61748. 8 interactions.
MINTi MINT-982292.
STRINGi 7227.FBpp0087744.

Proteomic databases

PaxDbi Q9V521.
PRIDEi Q9V521.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0088663 ; FBpp0087744 ; FBgn0033367 .
GeneIDi 35910.
KEGGi dme:Dmel_CG8193.
UCSCi CG8193-RA. d. melanogaster.

Organism-specific databases

CTDi 35910.
FlyBasei FBgn0033367. PPO2.

Phylogenomic databases

eggNOGi NOG131652.
GeneTreei ENSGT00730000111961.
InParanoidi Q9V521.
OMAi LPAYTEN.
OrthoDBi EOG7XPZ54.
PhylomeDBi Q9V521.

Miscellaneous databases

GenomeRNAii 35910.
NextBioi 795776.

Gene expression databases

Bgeei Q9V521.

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProi IPR013788. 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 ]
PANTHERi PTHR11511. PTHR11511. 1 hit.
Pfami PF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view ]
PRINTSi PR00187. HAEMOCYANIN.
SUPFAMi SSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiPPO2_DROME
AccessioniPrimary (citable) accession number: Q9V521
Secondary accession number(s): Q9BLD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3