ID RYK1_DROME Reviewed; 610 AA. AC Q27324; Q9U9Y3; Q9VIY6; DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 194. DE RecName: Full=Tyrosine-protein kinase Drl; DE EC=2.7.10.1; DE AltName: Full=Protein derailed; DE Flags: Precursor; GN Name=drl; Synonyms=lio; ORFNames=CG17348; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Head; RX PubMed=7656987; DOI=10.1016/0014-5793(95)00847-3; RA Dura J.-M., Taillebourg E., Preat T.; RT "The Drosophila learning and memory gene linotte encodes a putative RT receptor tyrosine kinase homologous to the human RYK gene product."; RL FEBS Lett. 370:250-254(1995). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=7603568; DOI=10.1038/376171a0; RA Callahan C.A., Muralidhar M.G., Lundgren S.E., Scully A.L., Thomas J.B.; RT "Control of neuronal pathway selection by a Drosophila receptor protein- RT tyrosine kinase family member."; RL Nature 376:171-174(1995). RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36. RX PubMed=10359803; DOI=10.1073/pnas.96.12.6856; RA Taillebourg E., Dura J.-M.; RT "A novel mechanism for P element homing in Drosophila."; RL Proc. Natl. Acad. Sci. U.S.A. 96:6856-6861(1999). RN [7] {ECO:0000305} RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=8787750; DOI=10.1242/dev.122.9.2761; RA Callahan C.A., Bonkovsky J.L., Scully A.L., Thomas J.B.; RT "derailed is required for muscle attachment site selection in Drosophila."; RL Development 122:2761-2767(1996). CC -!- FUNCTION: Probable coreceptor of Wnt proteins. Involved in neuronal CC pathway recognition and ventral muscle attachment site selection. Non- CC vital for development. May be part of a signal transduction cascade CC involved in learning and possibly memory. {ECO:0000269|PubMed:7603568, CC ECO:0000269|PubMed:7656987, ECO:0000269|PubMed:8787750}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: In the embryonic abdominal hemisegment, expression CC is restricted to cell body, axon and growth cone of a cluster of 20 CC ventral nerve cord interneurons. During muscle growth and attachment CC events in the embryonic abdominal hemisegment, expression is in somatic CC muscle fibers 21-23 at 10-13 hours and 2 patches of approximately 15 CC neighboring epidermal cells (dorsal and ventral attachment sites) at 6- CC 13 hours. {ECO:0000269|PubMed:7603568, ECO:0000269|PubMed:8787750}. CC -!- DOMAIN: The extracellular WIF domain is responsible for Wnt binding. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U36584; AAA79949.1; -; mRNA. DR EMBL; L47260; AAA75347.1; -; mRNA. DR EMBL; AE014134; AAF53776.1; -; Genomic_DNA. DR EMBL; AY051852; AAK93276.1; -; mRNA. DR EMBL; AF147883; AAD41343.1; -; Genomic_DNA. DR PIR; S58885; S58885. DR RefSeq; NP_477139.1; NM_057791.4. DR AlphaFoldDB; Q27324; -. DR SMR; Q27324; -. DR BioGRID; 69001; 17. DR DIP; DIP-22284N; -. DR IntAct; Q27324; 1. DR STRING; 7227.FBpp0303242; -. DR GlyCosmos; Q27324; 3 sites, No reported glycans. DR GlyGen; Q27324; 3 sites. DR PaxDb; 7227-FBpp0080736; -. DR DNASU; 44355; -. DR EnsemblMetazoa; FBtr0081195; FBpp0080736; FBgn0015380. DR GeneID; 44355; -. DR KEGG; dme:Dmel_CG17348; -. DR UCSC; CG17348-RA; d. melanogaster. DR AGR; FB:FBgn0015380; -. DR CTD; 30167; -. DR FlyBase; FBgn0015380; drl. DR VEuPathDB; VectorBase:FBgn0015380; -. DR eggNOG; KOG1024; Eukaryota. DR GeneTree; ENSGT00940000172861; -. DR HOGENOM; CLU_000288_7_36_1; -. DR InParanoid; Q27324; -. DR OMA; PQEPQTW; -. DR PhylomeDB; Q27324; -. DR BRENDA; 2.7.10.1; 1994. DR SignaLink; Q27324; -. DR BioGRID-ORCS; 44355; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 44355; -. DR PRO; PR:Q27324; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0015380; Expressed in eye disc (Drosophila) and 72 other cell types or tissues. DR ExpressionAtlas; Q27324; baseline and differential. DR GO; GO:0030424; C:axon; IDA:FlyBase. DR GO; GO:0030425; C:dendrite; IDA:FlyBase. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0043235; C:receptor complex; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase. DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase. DR GO; GO:0019901; F:protein kinase binding; IPI:FlyBase. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0042813; F:Wnt receptor activity; IDA:FlyBase. DR GO; GO:0017147; F:Wnt-protein binding; IPI:FlyBase. DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB. DR GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase. DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central. DR GO; GO:0198738; P:cell-cell signaling by wnt; TAS:ParkinsonsUK-UCL. DR GO; GO:0061643; P:chemorepulsion of axon; IMP:FlyBase. DR GO; GO:0070983; P:dendrite guidance; IMP:FlyBase. DR GO; GO:0016204; P:determination of muscle attachment site; IMP:FlyBase. DR GO; GO:0007482; P:haltere development; IGI:FlyBase. DR GO; GO:0007611; P:learning or memory; IMP:UniProtKB. DR GO; GO:0007613; P:memory; IMP:FlyBase. DR GO; GO:0016203; P:muscle attachment; IMP:UniProtKB. DR GO; GO:0016319; P:mushroom body development; TAS:ParkinsonsUK-UCL. DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase. DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB. DR GO; GO:0007416; P:synapse assembly; TAS:ParkinsonsUK-UCL. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR CDD; cd05043; PTK_Ryk; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR Gene3D; 2.60.40.2170; Wnt, WIF domain; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR003306; WIF. DR InterPro; IPR038677; WIF_sf. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR PANTHER; PTHR24416:SF349; TYROSINE-PROTEIN KINASE RYK; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF02019; WIF; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00469; WIF; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50814; WIF; 1. DR Genevisible; Q27324; DM. PE 2: Evidence at transcript level; KW ATP-binding; Cell membrane; Developmental protein; Glycoprotein; Kinase; KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; KW Signal; Transferase; Transmembrane; Transmembrane helix; KW Tyrosine-protein kinase; Wnt signaling pathway. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..610 FT /note="Tyrosine-protein kinase Drl" FT /id="PRO_0000024466" FT TOPO_DOM 21..242 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 243..263 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 264..610 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 24..155 FT /note="WIF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00222, FT ECO:0000305" FT DOMAIN 343..606 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 202..230 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 468 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 349..357 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 371 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 498 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT CARBOHYD 63 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 99 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 143 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 610 AA; 68312 MW; 728A3F272DAED4BE CRC64; MAPNLLTIGL LLTLIASGQA HLNIFLNLHE VLRLIGVSAE LYYVREGAIN DYALNFAVPV PANISDVTFT WQSLVDHPLP YSINIATSDT EVLPRPILNI SRIGDVPVEP QTWGIALKCS GTRNAEVTVT INVEVILDRA TNNNTNLIFK RKKICLREEQ DSAHEEYDDD DLDLLQTARK GHGGDIHYVD RNDEHVVANG HQAPEKQRPV VTESPVGRGN SGGSKRDFDP MLRENLVPPA SGLVTLIVGG ILALVLVSTL ILIAYCAKGP SKRHPSNGVH LIKTSSFQRL PTISSTAHNS IYVCPSTITP TYATLTRPFR EYEHEPEEFN RRLQELTVQK CRVRLSCLVQ EGNFGRIYRG TYNDCQEVLV KTVAQHASQL QVNLLLQESM MLYEASHPNV LSVLGISIED YATPFVLYAA TGSVRNLKSF LQDPSYARSV TTIQTVLMGS QLAMAMEHLH NHGVIHKDIA ARNCVIDDQL RVKLTDSALS RDLFPGDYNS LGDGEYRPIK WLSLEALQKS HYNEGSDVWS FGVLMWEMCT LGKLPYAEID PYEMEHYLKD GYRLAQPFNC PDELFTIMAY CWASMPAERP SFSQLQICLS EFHTQITRYV //