RYK2_DROME
ID RYK2_DROME Reviewed; 584 AA.
AC Q9V422; B9EQS2; O62533; Q5BII5; Q95TI0;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Tyrosine-protein kinase Dnt;
DE EC=2.7.10.1;
DE AltName: Full=Protein doughnut;
DE Flags: Precursor;
GN Name=dnt; ORFNames=CG17559;
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo;
RX PubMed=9858720; DOI=10.1016/s0925-4773(98)00167-1;
RA Oates A.C., Bonkovsky J.L., Irvine D.V., Kelly L.E., Thomas J.B.,
RA Wilks A.F.;
RT "Embryonic expression and activity of doughnut, a second RYK homolog in
RT Drosophila.";
RL Mech. Dev. 78:165-169(1998).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10231580; DOI=10.1016/s0378-1119(99)00061-x;
RA Savant-Bhonsale S., Friese M., McCoon P., Montell D.J.;
RT "A Drosophila derailed homolog, doughnut, expressed in invaginating cells
RT during embryogenesis.";
RL Gene 231:155-161(1999).
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;
RA Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 244-584.
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).
CC -!- FUNCTION: May play an essential role in neuronal pathway recognition
CC and ventral muscle attachment site selection.
CC {ECO:0000269|PubMed:9858720}.
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: Expressed in dynamic domains in the embryonic
CC epidermis, many of which border on sites of epithelial invagination
CC into the embryo interior, including ventral furrow, cephalic furrow,
CC fore- and hindgut, optic lobe and tracheal pits. Later in
CC embryogenesis, expression is seen in imaginal tissues.
CC {ECO:0000269|PubMed:10231580, ECO:0000269|PubMed:9858720}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically from
CC embryos to adults. High expression is seen in embryos, pupae and adults
CC (highest in early pupae) and low expression in larvae.
CC {ECO:0000269|PubMed:10231580, ECO:0000269|PubMed:9858720}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31179.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA11918.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ224361; CAA11918.1; ALT_INIT; mRNA.
DR EMBL; AF123572; AAD31179.1; ALT_INIT; mRNA.
DR EMBL; AE014134; AAF53783.2; -; Genomic_DNA.
DR EMBL; BT021239; AAX33387.1; -; mRNA.
DR EMBL; BT057997; ACM16707.1; -; mRNA.
DR EMBL; AY058760; AAL13989.1; -; mRNA.
DR RefSeq; NP_001260567.1; NM_001273638.1.
DR RefSeq; NP_477341.2; NM_057993.4.
DR AlphaFoldDB; Q9V422; -.
DR SMR; Q9V422; -.
DR BioGRID; 61188; 6.
DR DIP; DIP-20351N; -.
DR STRING; 7227.FBpp0080765; -.
DR GlyGen; Q9V422; 4 sites.
DR PaxDb; Q9V422; -.
DR PRIDE; Q9V422; -.
DR DNASU; 35207; -.
DR EnsemblMetazoa; FBtr0081224; FBpp0080765; FBgn0024245.
DR EnsemblMetazoa; FBtr0336820; FBpp0307787; FBgn0024245.
DR GeneID; 35207; -.
DR KEGG; dme:Dmel_CG17559; -.
DR CTD; 35207; -.
DR FlyBase; FBgn0024245; dnt.
DR VEuPathDB; VectorBase:FBgn0024245; -.
DR eggNOG; KOG1024; Eukaryota.
DR GeneTree; ENSGT00940000172861; -.
DR HOGENOM; CLU_000288_7_36_1; -.
DR InParanoid; Q9V422; -.
DR OMA; NTRNLKQ; -.
DR OrthoDB; 833475at2759; -.
DR PhylomeDB; Q9V422; -.
DR Reactome; R-DME-201681; TCF dependent signaling in response to WNT.
DR BioGRID-ORCS; 35207; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35207; -.
DR PRO; PR:Q9V422; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0024245; Expressed in wing disc and 20 other tissues.
DR ExpressionAtlas; Q9V422; baseline and differential.
DR Genevisible; Q9V422; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0016204; P:determination of muscle attachment site; IMP:FlyBase.
DR GO; GO:0016203; P:muscle attachment; IMP:UniProtKB.
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: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.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..584
FT /note="Tyrosine-protein kinase Dnt"
FT /id="PRO_0000024467"
FT TOPO_DOM 41..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..180
FT /note="WIF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00222"
FT DOMAIN 317..577
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 241..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 323..331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 472
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 448
FT /note="C -> Y (in Ref. 5; AAX33387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 584 AA; 64938 MW; F46FCD024BD8447E CRC64;
MESVNKCGKS ASTRNCTVKM SRKMWVLSLL ALAALQLHSG SEVAAHLNVF LNPVEVMRLL
GVSAEVYYVR EGHINNYALN FIVPVPANVK DISFTWQSLA GRGLPYSINV VSSDQEVLPR
PAINVSHSGE IPTTIQTWSI ALKCSGLKAA EVDVTVSLEV VLNRSLNNVT HLVFRRKKIC
LMNDSAEDLS EDVDDPQLLE TVMLPPTGLI TLVVGVSVAM GSVCLLLMIA YCVKGAANKR
QHHQHGGQPM RTSSFQRLNT HPPCQSSMGS AAYMTPSIIA PIHGSSLPRK VPVSVEQQHP
EELHRRISEL TVERCRVRLS SLLQEGTFGR VYRGTYNDTQ DVLVKTVAQH ASQMQVLLLL
QEGMLLYGAS HPGILSVLGV SIEDHTTPFV LYPALNNTRN LKQFLLDPAC ARTVTTIQIV
MMASQLSMAL DHLHSHGVVH KDIATRNCVI DDQLRVKLSD SSLSRDLFPS DYNCLGDSEN
RPVKWMSLEA LQHKQFSEAS DSWAFGVLMW ELCTSAKQPY AEVDPFEMEH YLKDGYRLAQ
PFNCPDELFT IMAYCWALLP AERPTFAQLQ SCLSEFYSQI TRYV
