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Q27324

- RYK1_DROME

UniProt

Q27324 - RYK1_DROME

Protein

Tyrosine-protein kinase Drl

Gene

drl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Probable coreceptor of Wnt proteins. Involved in neuronal pathway recognition and ventral muscle attachment site selection. Non-vital for development. May be part of a signal transduction cascade involved in learning and possibly memory.3 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei371 – 3711ATPPROSITE-ProRule annotation
    Active sitei468 – 4681Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi349 – 3579ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein tyrosine kinase activity Source: FlyBase
    3. transmembrane receptor protein tyrosine kinase activity Source: FlyBase
    4. Wnt-protein binding Source: FlyBase

    GO - Biological processi

    1. axon guidance Source: UniProtKB
    2. axon midline choice point recognition Source: FlyBase
    3. determination of muscle attachment site Source: FlyBase
    4. haltere development Source: FlyBase
    5. learning or memory Source: UniProtKB
    6. memory Source: FlyBase
    7. muscle attachment Source: UniProtKB
    8. olfactory learning Source: FlyBase
    9. peptidyl-tyrosine phosphorylation Source: GOC
    10. protein phosphorylation Source: FlyBase
    11. salivary gland morphogenesis Source: FlyBase
    12. signal transduction Source: UniProtKB
    13. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 1994.
    ReactomeiREACT_184329. PCP/CE pathway.
    REACT_207070. TCF dependent signaling in response to WNT.
    SignaLinkiQ27324.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Drl (EC:2.7.10.1)
    Alternative name(s):
    Protein derailed
    Gene namesi
    Name:drl
    Synonyms:lio
    ORF Names:CG17348
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0015380. drl.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: FlyBase
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 610590Tyrosine-protein kinase DrlPRO_0000024466Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi143 – 1431N-linked (GlcNAc...)Sequence Analysis
    Modified residuei498 – 4981Phosphotyrosine; by autocatalysisBy similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ27324.
    PRIDEiQ27324.

    Expressioni

    Tissue specificityi

    In the embryonic abdominal hemisegment, expression is restricted to cell body, axon and growth cone of a cluster of 20 ventral nerve cord interneurons. During muscle growth and attachment events in the embryonic abdominal hemisegment, expression is in somatic muscle fibers 21-23 at 10-13 hours and 2 patches of approximately 15 neighboring epidermal cells (dorsal and ventral attachment sites) at 6-13 hours.2 Publications

    Gene expression databases

    BgeeiQ27324.

    Interactioni

    Protein-protein interaction databases

    BioGridi69001. 10 interactions.
    DIPiDIP-22284N.
    IntActiQ27324. 1 interaction.
    MINTiMINT-337834.

    Structurei

    3D structure databases

    ProteinModelPortaliQ27324.
    SMRiQ27324. Positions 285-596.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 242222ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini264 – 610347CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei243 – 26321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 155132WIFCuratedPROSITE-ProRule annotationAdd
    BLAST
    Domaini343 – 606264Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The extracellular WIF domain is responsible for Wnt binding.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 WIF domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108377.
    InParanoidiQ27324.
    KOiK05128.
    OrthoDBiEOG7M98KK.
    PhylomeDBiQ27324.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR003306. WIF.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF02019. WIF. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    ProDomiPD013948. WIF. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00219. TyrKc. 1 hit.
    SM00469. WIF. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50814. WIF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q27324-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPNLLTIGL LLTLIASGQA HLNIFLNLHE VLRLIGVSAE LYYVREGAIN    50
    DYALNFAVPV PANISDVTFT WQSLVDHPLP YSINIATSDT EVLPRPILNI 100
    SRIGDVPVEP QTWGIALKCS GTRNAEVTVT INVEVILDRA TNNNTNLIFK 150
    RKKICLREEQ DSAHEEYDDD DLDLLQTARK GHGGDIHYVD RNDEHVVANG 200
    HQAPEKQRPV VTESPVGRGN SGGSKRDFDP MLRENLVPPA SGLVTLIVGG 250
    ILALVLVSTL ILIAYCAKGP SKRHPSNGVH LIKTSSFQRL PTISSTAHNS 300
    IYVCPSTITP TYATLTRPFR EYEHEPEEFN RRLQELTVQK CRVRLSCLVQ 350
    EGNFGRIYRG TYNDCQEVLV KTVAQHASQL QVNLLLQESM MLYEASHPNV 400
    LSVLGISIED YATPFVLYAA TGSVRNLKSF LQDPSYARSV TTIQTVLMGS 450
    QLAMAMEHLH NHGVIHKDIA ARNCVIDDQL RVKLTDSALS RDLFPGDYNS 500
    LGDGEYRPIK WLSLEALQKS HYNEGSDVWS FGVLMWEMCT LGKLPYAEID 550
    PYEMEHYLKD GYRLAQPFNC PDELFTIMAY CWASMPAERP SFSQLQICLS 600
    EFHTQITRYV 610
    Length:610
    Mass (Da):68,312
    Last modified:November 1, 1996 - v1
    Checksum:i728A3F272DAED4BE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U36584 mRNA. Translation: AAA79949.1.
    L47260 mRNA. Translation: AAA75347.1.
    AE014134 Genomic DNA. Translation: AAF53776.1.
    AY051852 mRNA. Translation: AAK93276.1.
    AF147883 Genomic DNA. Translation: AAD41343.1.
    PIRiS58885.
    RefSeqiNP_477139.1. NM_057791.4.
    UniGeneiDm.4108.

    Genome annotation databases

    EnsemblMetazoaiFBtr0081195; FBpp0080736; FBgn0015380.
    GeneIDi44355.
    KEGGidme:Dmel_CG17348.
    UCSCiCG17348-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U36584 mRNA. Translation: AAA79949.1 .
    L47260 mRNA. Translation: AAA75347.1 .
    AE014134 Genomic DNA. Translation: AAF53776.1 .
    AY051852 mRNA. Translation: AAK93276.1 .
    AF147883 Genomic DNA. Translation: AAD41343.1 .
    PIRi S58885.
    RefSeqi NP_477139.1. NM_057791.4.
    UniGenei Dm.4108.

    3D structure databases

    ProteinModelPortali Q27324.
    SMRi Q27324. Positions 285-596.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 69001. 10 interactions.
    DIPi DIP-22284N.
    IntActi Q27324. 1 interaction.
    MINTi MINT-337834.

    Proteomic databases

    PaxDbi Q27324.
    PRIDEi Q27324.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0081195 ; FBpp0080736 ; FBgn0015380 .
    GeneIDi 44355.
    KEGGi dme:Dmel_CG17348.
    UCSCi CG17348-RA. d. melanogaster.

    Organism-specific databases

    CTDi 30167.
    FlyBasei FBgn0015380. drl.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108377.
    InParanoidi Q27324.
    KOi K05128.
    OrthoDBi EOG7M98KK.
    PhylomeDBi Q27324.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 1994.
    Reactomei REACT_184329. PCP/CE pathway.
    REACT_207070. TCF dependent signaling in response to WNT.
    SignaLinki Q27324.

    Miscellaneous databases

    GenomeRNAii 44355.
    NextBioi 837187.

    Gene expression databases

    Bgeei Q27324.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR003306. WIF.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF02019. WIF. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    ProDomi PD013948. WIF. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00219. TyrKc. 1 hit.
    SM00469. WIF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50814. WIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Drosophila learning and memory gene linotte encodes a putative receptor tyrosine kinase homologous to the human RYK gene product."
      Dura J.-M., Taillebourg E., Preat T.
      FEBS Lett. 370:250-254(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Head.
    2. "Control of neuronal pathway selection by a Drosophila receptor protein-tyrosine kinase family member."
      Callahan C.A., Muralidhar M.G., Lundgren S.E., Scully A.L., Thomas J.B.
      Nature 376:171-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Embryo.
    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.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    6. "A novel mechanism for P element homing in Drosophila."
      Taillebourg E., Dura J.-M.
      Proc. Natl. Acad. Sci. U.S.A. 96:6856-6861(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
    7. "derailed is required for muscle attachment site selection in Drosophila."
      Callahan C.A., Bonkovsky J.L., Scully A.L., Thomas J.B.
      Development 122:2761-2767(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiRYK1_DROME
    AccessioniPrimary (citable) accession number: Q27324
    Secondary accession number(s): Q9U9Y3, Q9VIY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 132 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