RYK1_DROME
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 03-AUG-2022, entry version 189.
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}.
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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.FBpp0080736; -.
DR GlyGen; Q27324; 3 sites.
DR PaxDb; Q27324; -.
DR PRIDE; Q27324; -.
DR DNASU; 44355; -.
DR EnsemblMetazoa; FBtr0081195; FBpp0080736; FBgn0015380.
DR GeneID; 44355; -.
DR KEGG; dme:Dmel_CG17348; -.
DR UCSC; CG17348-RA; d. melanogaster.
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 OrthoDB; 833475at2759; -.
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 tissues.
DR ExpressionAtlas; Q27324; baseline and differential.
DR Genevisible; Q27324; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of 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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 Gene3D; 2.60.40.2170; -; 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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02019; WIF; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00469; WIF; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50814; WIF; 1.
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
