Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q27324 (RYK1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Drl

EC=2.7.10.1
Alternative name(s):
Protein derailed
Gene names
Name:drl
Synonyms:lio
ORF Names:CG17348
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length610 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.7

Catalytic activity

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

Subcellular location

Cell membrane; Single-pass membrane protein Potential.

Tissue specificity

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. Ref.2 Ref.7

Domain

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

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family.

Contains 1 protein kinase domain.

Contains 1 WIF domain.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance

Inferred from mutant phenotype Ref.2. Source: UniProtKB

axon midline choice point recognition

Inferred from mutant phenotype PubMed 12660735. Source: FlyBase

determination of muscle attachment site

Inferred from mutant phenotype PubMed 22403643. Source: FlyBase

haltere development

Inferred from genetic interaction PubMed 16815386. Source: FlyBase

learning or memory

Inferred from mutant phenotype Ref.1. Source: UniProtKB

memory

Inferred from mutant phenotype PubMed 12488817. Source: FlyBase

muscle attachment

Inferred from mutant phenotype Ref.7. Source: UniProtKB

olfactory learning

Inferred from mutant phenotype PubMed 12488817. Source: FlyBase

peptidyl-tyrosine phosphorylation

Non-traceable author statement PubMed 10908587PubMed 11462211. Source: GOC

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

salivary gland morphogenesis

Inferred from mutant phenotype PubMed 17507403. Source: FlyBase

signal transduction

Inferred from mutant phenotype Ref.2. Source: UniProtKB

   Cellular_componentaxon

Inferred from direct assay PubMed 19874787. Source: FlyBase

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Wnt-protein binding

Inferred from physical interaction PubMed 12660735. Source: FlyBase

protein tyrosine kinase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

transmembrane receptor protein tyrosine kinase activity

Non-traceable author statement PubMed 11462211. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 610590Tyrosine-protein kinase Drl
PRO_0000024466

Regions

Topological domain21 – 242222Extracellular Potential
Transmembrane243 – 26321Helical; Potential
Topological domain264 – 610347Cytoplasmic Potential
Domain24 – 155132WIF
Domain343 – 606264Protein kinase
Nucleotide binding349 – 3579ATP By similarity

Sites

Active site4681Proton acceptor By similarity
Binding site3711ATP By similarity

Amino acid modifications

Modified residue4981Phosphotyrosine; by autocatalysis By similarity
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1431N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q27324 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 728A3F272DAED4BE

FASTA61068,312
        10         20         30         40         50         60 
MAPNLLTIGL LLTLIASGQA HLNIFLNLHE VLRLIGVSAE LYYVREGAIN DYALNFAVPV 

        70         80         90        100        110        120 
PANISDVTFT WQSLVDHPLP YSINIATSDT EVLPRPILNI SRIGDVPVEP QTWGIALKCS 

       130        140        150        160        170        180 
GTRNAEVTVT INVEVILDRA TNNNTNLIFK RKKICLREEQ DSAHEEYDDD DLDLLQTARK 

       190        200        210        220        230        240 
GHGGDIHYVD RNDEHVVANG HQAPEKQRPV VTESPVGRGN SGGSKRDFDP MLRENLVPPA 

       250        260        270        280        290        300 
SGLVTLIVGG ILALVLVSTL ILIAYCAKGP SKRHPSNGVH LIKTSSFQRL PTISSTAHNS 

       310        320        330        340        350        360 
IYVCPSTITP TYATLTRPFR EYEHEPEEFN RRLQELTVQK CRVRLSCLVQ EGNFGRIYRG 

       370        380        390        400        410        420 
TYNDCQEVLV KTVAQHASQL QVNLLLQESM MLYEASHPNV LSVLGISIED YATPFVLYAA 

       430        440        450        460        470        480 
TGSVRNLKSF LQDPSYARSV TTIQTVLMGS QLAMAMEHLH NHGVIHKDIA ARNCVIDDQL 

       490        500        510        520        530        540 
RVKLTDSALS RDLFPGDYNS LGDGEYRPIK WLSLEALQKS HYNEGSDVWS FGVLMWEMCT 

       550        560        570        580        590        600 
LGKLPYAEID PYEMEHYLKD GYRLAQPFNC PDELFTIMAY CWASMPAERP SFSQLQICLS 

       610 
EFHTQITRYV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS58885.
RefSeqNP_477139.1. NM_057791.4.
UniGeneDm.4108.

3D structure databases

ProteinModelPortalQ27324.
SMRQ27324. Positions 285-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid69001. 10 interactions.
DIPDIP-22284N.
IntActQ27324. 1 interaction.
MINTMINT-337834.

Proteomic databases

PaxDbQ27324.
PRIDEQ27324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0081195; FBpp0080736; FBgn0015380.
GeneID44355.
KEGGdme:Dmel_CG17348.
UCSCCG17348-RA. d. melanogaster.

Organism-specific databases

CTD30167.
FlyBaseFBgn0015380. drl.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108377.
InParanoidQ27324.
KOK05128.
OrthoDBEOG7M98KK.
PhylomeDBQ27324.

Enzyme and pathway databases

BRENDA2.7.10.1. 1994.
SignaLinkQ27324.

Gene expression databases

BgeeQ27324.

Family and domain databases

InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF02019. WIF. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
ProDomPD013948. WIF. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00219. TyrKc. 1 hit.
SM00469. WIF. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50814. WIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi44355.
NextBio837187.

Entry information

Entry nameRYK1_DROME
AccessionPrimary (citable) accession number: Q27324
Secondary accession number(s): Q9U9Y3, Q9VIY6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase