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P49762

- DOA_DROME

UniProt

P49762 - DOA_DROME

Protein

Serine/threonine-protein kinase Doa

Gene

Doa

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 140 (01 Oct 2014)
      Sequence version 2 (19 Sep 2003)
      Previous versions | rss
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    Functioni

    Negative regulator of the copia retrotransposon element of the white (w) gene. In the eye, it is required for normal pigmentation, photoreceptor cell development and for organization of interommatidial bristles. Also essential for embryonic segmentation and differentiation of the nervous system. Functions in the control of alternative splicing by phosphorylating the arginine/serine-rich splicing factors, SR proteins.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei508 – 5081ATP
    Active sitei605 – 6051Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi485 – 4939ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein kinase activity Source: FlyBase
    3. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
    4. protein serine/threonine kinase activity Source: FlyBase
    5. protein tyrosine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. autophagic cell death Source: FlyBase
    2. blastoderm segmentation Source: FlyBase
    3. brain morphogenesis Source: FlyBase
    4. compound eye development Source: FlyBase
    5. compound eye photoreceptor development Source: FlyBase
    6. karyosome formation Source: FlyBase
    7. locomotion involved in locomotory behavior Source: FlyBase
    8. negative regulation of male germ cell proliferation Source: FlyBase
    9. nervous system development Source: FlyBase
    10. oogenesis Source: FlyBase
    11. protein autophosphorylation Source: FlyBase
    12. protein phosphorylation Source: FlyBase
    13. protein secretion Source: FlyBase
    14. regulation of alternative mRNA splicing, via spliceosome Source: FlyBase
    15. salivary gland cell autophagic cell death Source: FlyBase
    16. sex differentiation Source: FlyBase
    17. startle response Source: FlyBase
    18. visual perception Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Sensory transduction, Vision

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 1994.
    SignaLinkiP49762.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase Doa (EC:2.7.12.1)
    Alternative name(s):
    Protein darkener of apricot
    Gene namesi
    Name:Doa
    ORF Names:CG42320
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0265998. Doa.

    Subcellular locationi

    Isoform A : Nucleus
    Note: Mainly nuclear with only low levels present in the cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. cytosol Source: UniProtKB-SubCell
    3. endoplasmic reticulum Source: FlyBase
    4. microtubule associated complex Source: FlyBase
    5. nucleus Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi508 – 5081K → R: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 832832Serine/threonine-protein kinase DoaPRO_0000085926Add
    BLAST

    Post-translational modificationi

    Autophosphorylated on serine, threonine and tyrosine residues.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP49762.
    PRIDEiP49762.

    Expressioni

    Tissue specificityi

    Ubiquitous expression in embryos. Stage 17 embryos show elevated expression in CNS and brain. Ubiquitous expression in larval imaginal disks. Increased expression posterior to the eye-antennal disk morphogenetic furrow.2 Publications

    Developmental stagei

    Expressed both maternally (isoform C) and zygotically (isoforms A and C) in all developmental stages.2 Publications

    Gene expression databases

    BgeeiP49762.

    Interactioni

    Protein-protein interaction databases

    BioGridi68286. 50 interactions.
    IntActiP49762. 48 interactions.
    MINTiMINT-805690.

    Structurei

    3D structure databases

    ProteinModelPortaliP49762.
    SMRiP49762. Positions 459-802.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini479 – 799321Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00580000081366.
    HOGENOMiHOG000141611.
    KOiK08823.
    OMAiDEDTICD.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform C (identifier: P49762-1) [UniParc]FASTAAdd to Basket

    Also known as: 105 kDa isoform

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVAANLEVPT SSSSSAATKR QKDVDNKLEK CLNDMLKLKT SSNNNSTSNS    50
    NNNAIMSHSL TGEHKDPKTA LEGPTSSSSS SSSKYIGESQ IPVPVQLYDP 100
    QKPLLQQQQQ QQRICYPIGK SNSTSQLPMG GYQRLLQHQQ QQHHQQQQQQ 150
    HQEQQQYPQH KRPFLNWNSF ACSAMNGASD PFMQQQHMPA HQQQQHLPHK 200
    LQQSYSSSHV PKQAPKSGLA MFLQKNTNKE NKFGQPMQQQ PPGMMPQMYG 250
    YQAPQQQSKI GYPRTGAPLT HSASFSSAQR PTALQFHQQH QQQQHLQQQQ 300
    QHPQQQQHQH SSFGVGMMSR NYYNMPKQPE RKPLQTFDPY AYPKPNQMQP 350
    VKYQQQQQHP HTQFQNASAG GGGGGAAGLQ YDPNTNTQLF YASPASSSSN 400
    KQPQQPQQQQ QQQQSQLQQS NSVIFNHSGQ QHQPHQQQQN EMSKSALGLH 450
    FIETAKPVIQ DDADGHLIYH TGDILHHRYK IMATLGEGTF GRVVKVKDME 500
    RDYCMALKII KNVEKYREAA KLEINALEKI AQKDPHCDHL CVKMIDWFDY 550
    HGHMCIVFEM LGLSVFDFLR ENNYEPYPLD QVRHMAYQLC YSVKFLHDNR 600
    LTHTDLKPEN ILFVDSDYTS HYNHKINREV RRVKNTDVRL IDFGSATFDH 650
    EHHSTIVSTR HYRAPEVILE LGWSQPCDVW SIGCILFELY LGITLFQTHD 700
    NREHLAMMER ILGQIPYRMA RNHTLYSKTK TKYFYHGKLD WDEKSSAGRY 750
    VRDHCKPLFL CQLSDSEDHC ELFSLIKKML EYEPSSRITL GEALHHPFFD 800
    RLPPHHRVGE VSNKQPLSSG SSSRERSHSL SR 832

    Note: No experimental confirmation available. May correspond to the described 105 kDa isoform although there is no translation sequence evidence for this.

    Length:832
    Mass (Da):95,723
    Last modified:September 19, 2003 - v2
    Checksum:i6EC90CB1A031DD68
    GO
    Isoform A (identifier: P49762-2) [UniParc]FASTAAdd to Basket

    Also known as: 55 kDa isoform

    The sequence of this isoform differs from the canonical sequence as follows:
         1-252: Missing.
         253-453: APQQQSKIGY...KSALGLHFIE → MQLPSLKDKL...GRNNRQSQAK
         722-727: Missing.

    Show »
    Length:580
    Mass (Da):67,894
    Checksum:iF73AC5B47733AF3A
    GO
    Isoform B (identifier: P49762-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-315: Missing.
         316-453: GMMSRNYYNM...KSALGLHFIE → MPRTRRLHHS...GRNNRQSQAK
         722-727: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:511
    Mass (Da):60,210
    Checksum:i8D6366BFDBD8A948
    GO

    Sequence cautioni

    The sequence CAA55367.1 differs from that shown. Reason: Chimera. Chimera of genomic DNA and cDNA.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 315315Missing in isoform B. CuratedVSP_008269Add
    BLAST
    Alternative sequencei1 – 252252Missing in isoform A. 1 PublicationVSP_008268Add
    BLAST
    Alternative sequencei253 – 453201APQQQ…LHFIE → MQLPSLKDKLMPSGSVQQAK ANFSWQSLTQLLSGLWQRLY LPRSPFLALPAPPLATPPAN TTQRRAKKEMPRTRRLHHSR DRSSAGTRDKRRRHDTADHS PPLAEAPSPPRITNTHHTRS AAKRRRHELDAKKAQISKEP TFDDSISTRRRKERSKRSHR KSPAASRRQHKYRYRDETSH SSSRRRHRDRAKDERDSGRN NRQSQAK in isoform A. 1 PublicationVSP_008270Add
    BLAST
    Alternative sequencei316 – 453138GMMSR…LHFIE → MPRTRRLHHSRDRSSAGTRD KRRRHDTADHSPPLAEAPSP PRITNTHHTRSAAKRRRHEL DAKKAQISKEPTFDDSISTR RRKERSKRSHRKSPAASRRQ HKYRYRDETSHSSSRRRHRD RAKDERDSGRNNRQSQAK in isoform B. CuratedVSP_008271Add
    BLAST
    Alternative sequencei722 – 7276Missing in isoform A and isoform B. 1 PublicationVSP_008272

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78715 Genomic DNA. Translation: CAA55367.1. Sequence problems.
    AE014297 Genomic DNA. Translation: AAF56832.3.
    AE014297 Genomic DNA. Translation: AAF56833.2.
    AE014297 Genomic DNA. Translation: AAN14305.1.
    AY061474 mRNA. Translation: AAL29022.1.
    AY069573 mRNA. Translation: AAL39718.1.
    PIRiA54099.
    RefSeqiNP_001014679.1. NM_001014679.2. [P49762-1]
    NP_001014680.1. NM_001014680.4. [P49762-2]
    NP_001014682.1. NM_001014682.3. [P49762-3]
    NP_001036765.1. NM_001043300.3. [P49762-2]
    NP_001138120.1. NM_001144648.3. [P49762-2]
    NP_001138121.1. NM_001144649.2. [P49762-2]
    NP_001138122.1. NM_001144650.1. [P49762-3]
    UniGeneiDm.6767.

    Genome annotation databases

    EnsemblMetazoaiFBtr0299743; FBpp0289021; FBgn0259220. [P49762-1]
    GeneIDi43415.
    KEGGidme:Dmel_CG42320.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78715 Genomic DNA. Translation: CAA55367.1 . Sequence problems.
    AE014297 Genomic DNA. Translation: AAF56832.3 .
    AE014297 Genomic DNA. Translation: AAF56833.2 .
    AE014297 Genomic DNA. Translation: AAN14305.1 .
    AY061474 mRNA. Translation: AAL29022.1 .
    AY069573 mRNA. Translation: AAL39718.1 .
    PIRi A54099.
    RefSeqi NP_001014679.1. NM_001014679.2. [P49762-1 ]
    NP_001014680.1. NM_001014680.4. [P49762-2 ]
    NP_001014682.1. NM_001014682.3. [P49762-3 ]
    NP_001036765.1. NM_001043300.3. [P49762-2 ]
    NP_001138120.1. NM_001144648.3. [P49762-2 ]
    NP_001138121.1. NM_001144649.2. [P49762-2 ]
    NP_001138122.1. NM_001144650.1. [P49762-3 ]
    UniGenei Dm.6767.

    3D structure databases

    ProteinModelPortali P49762.
    SMRi P49762. Positions 459-802.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68286. 50 interactions.
    IntActi P49762. 48 interactions.
    MINTi MINT-805690.

    Proteomic databases

    PaxDbi P49762.
    PRIDEi P49762.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0299743 ; FBpp0289021 ; FBgn0259220 . [P49762-1 ]
    GeneIDi 43415.
    KEGGi dme:Dmel_CG42320.

    Organism-specific databases

    CTDi 43415.
    FlyBasei FBgn0265998. Doa.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00580000081366.
    HOGENOMi HOG000141611.
    KOi K08823.
    OMAi DEDTICD.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 1994.
    SignaLinki P49762.

    Miscellaneous databases

    ChiTaRSi Doa. drosophila.
    GenomeRNAii 43415.
    NextBioi 833791.
    PROi P49762.

    Gene expression databases

    Bgeei P49762.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Doa locus encodes a member of a new protein kinase family and is essential for eye and embryonic development in Drosophila melanogaster."
      Yun B., Farkas R., Lee K., Rabinow L.
      Genes Dev. 8:1160-1173(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. Rabinow L.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "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.
    4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
      Strain: Berkeley.
      Tissue: Embryo.
    6. "Activity and autophosphorylation of LAMMER protein kinases."
      Lee K., Du C., Horn M., Rabinow L.
      J. Biol. Chem. 271:27299-27303(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-508.
    7. "The LAMMER protein kinase encoded by the Doa locus of Drosophila is required in both somatic and germline cells and is expressed as both nuclear and cytoplasmic isoforms throughout development."
      Yun B., Lee K., Farkas R., Hitte C., Rabinow L.
      Genetics 156:749-761(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiDOA_DROME
    AccessioniPrimary (citable) accession number: P49762
    Secondary accession number(s): Q8IMM0
    , Q8T041, Q95RC9, Q9VAR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 19, 2003
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 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