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Q27324

- RYK1_DROME

UniProt

Q27324 - RYK1_DROME

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Protein

Tyrosine-protein kinase Drl

Gene
drl, lio, CG17348
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei371 – 3711ATP By similarity
Active sitei468 – 4681Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi349 – 3579ATP By similarity

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 242222Extracellular Reviewed predictionAdd
BLAST
Transmembranei243 – 26321Helical; Reviewed predictionAdd
BLAST
Topological domaini264 – 610347Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...) Reviewed prediction
Glycosylationi99 – 991N-linked (GlcNAc...) Reviewed prediction
Glycosylationi143 – 1431N-linked (GlcNAc...) Reviewed prediction
Modified residuei498 – 4981Phosphotyrosine; by autocatalysis By 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 155132WIFAdd
BLAST
Domaini343 – 606264Protein kinaseAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 WIF domain.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 131 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

Similar proteinsi