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Q9V521

- PPO2_DROME

UniProt

Q9V521 - PPO2_DROME

Protein

Phenoloxidase 2

Gene

PPO2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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. dopamine metabolic process Source: FlyBase
    2. melanin biosynthetic process Source: UniProtKB-KW

    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

    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

    MADKKNLLLL FDHPTEPVFM DKGKRVTVFD VPDSFLTDRY RPISNEVQSR    50
    VGDKVEQRVP VREISIPDLR IPMSLGRDEQ FSLFLPKHRR IAGRLIDIFM 100
    NMRSVDDLQS VAVYARDRVN PVLFNYALSV ALLHRPDTQG LDLPSFSQTF 150
    PDRFIDSQVI RKMREESFVV QPGSRMPITI PRDYTASDLD PEHRLWYFRE 200
    DLGINLHHWH WHLVYPFEAS DRSIVAKDRR GELFYYMHQQ VIARYNAERF 250
    SNNLARVLPF NNLRDPIAEG YFPKMDSLVA SRAWPPRFES TRLSDLNRES 300
    DQLNVEIGDL ERWRDRIYEA IHQGFVMDER GNRVPLDEAT GIDTLGNMIE 350
    SSILSPNRVL YGDLHNNGHT FISYAHDPTS KHLESFGVMG DVSTAMRDPV 400
    FYKWHSYIDR IFQEHKSRLP AYTENQLNYP GVSIAGIQVD TNGGRPNNLT 450
    TFWQQSDVDM SRGFDFLPRG NVFARFTHLQ HLPFTYTISL NNDSGAQRFG 500
    YVRIFMAPKN DERGQPMLMR DQRSMMIELD KFVTSLNPGP NTIRRRSTES 550
    SVTIPFERTF RNLDANRPAA GTPEELEFNF CGCGWPNHML VPKGLPEGLQ 600
    CVLFIMVSNY ENDRIDQQLV GRCSDAASYC GVRDRLYPDR QSMGFPFDRL 650
    PRSGVDRLVN FLTPNMSIVD VNIRHENRTV QRPN 684
    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_136599.3.
    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_136599.3.
    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

    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 1, 2014
    This is version 97 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