ID TORSO_DROME Reviewed; 923 AA. AC P18475; A8DY54; A8DY56; Q9V4R2; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 2. DT 27-MAR-2024, entry version 210. DE RecName: Full=Tyrosine-protein kinase receptor torso; DE EC=2.7.10.1; DE Flags: Precursor; GN Name=tor; ORFNames=CG1389; 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] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=2927509; DOI=10.1038/338478a0; RA Sprenger F., Stevens L.M., Nuesslein-Volhard C.; RT "The Drosophila gene torso encodes a putative receptor tyrosine kinase."; RL Nature 338:478-483(1989). RN [2] 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 [3] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). 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 [5] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=8423783; DOI=10.1128/mcb.13.2.1163-1172.1993; RA Sprenger F., Torsoclair M.M., Morrison D.K.; RT "Biochemical analysis of torso and D-raf during Drosophila embryogenesis: RT implications for terminal signal transduction."; RL Mol. Cell. Biol. 13:1163-1172(1993). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). RN [7] RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=19965758; DOI=10.1126/science.1176450; RA Rewitz K.F., Yamanaka N., Gilbert L.I., O'Connor M.B.; RT "The insect neuropeptide PTTH activates receptor tyrosine kinase torso to RT initiate metamorphosis."; RL Science 326:1403-1405(2009). CC -!- FUNCTION: Probable receptor tyrosine kinase which is required for CC determination of anterior and posterior terminal structures in the CC embryo (PubMed:2927509, PubMed:8423783). During postembryonic CC development, involved in the initiation of metamorphosis probably by CC inducing the production of ecdysone in response to prothoracicotropic CC hormone Ptth (PubMed:19965758). Binding to Ptth stimulates activation CC of canonical MAPK signaling leading to ERK phosphorylation (By CC similarity). {ECO:0000250|UniProtKB:D2IYS2, CC ECO:0000269|PubMed:19965758, ECO:0000269|PubMed:2927509, CC ECO:0000269|PubMed:8423783}. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A {ECO:0000312|FlyBase:FBgn0003733}; CC IsoId=P18475-1; Sequence=Displayed; CC Name=D {ECO:0000312|FlyBase:FBgn0003733}; CC IsoId=P18475-3; Sequence=VSP_058212; CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. CC Expressed throughout the embryo but is activated specifically at the CC poles (PubMed:2927509, PubMed:8423783, PubMed:19965758). Expressed in CC the prothoracic gland in wandering L3 larvae (PubMed:19965758). CC {ECO:0000269|PubMed:19965758, ECO:0000269|PubMed:2927509, CC ECO:0000269|PubMed:8423783}. CC -!- PTM: May be auto-phosphorylated on tyrosine residues. CC {ECO:0000250|UniProtKB:D2IYS2}. CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the prothoracic gland CC (PG) delays the onset of pupariation by prolonging the L3 larval stage. CC In addition, pupal size and, to a lesser extent, PG cell size are CC increased. {ECO:0000269|PubMed:19965758}. 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; X15150; CAA33247.1; -; Genomic_DNA. DR EMBL; AE013599; AAF59203.1; -; Genomic_DNA. DR EMBL; AE013599; ABV53713.1; -; Genomic_DNA. DR EMBL; AE013599; ABV53714.2; -; Genomic_DNA. DR EMBL; AY071403; AAL49025.1; -; mRNA. DR PIR; S03900; S03900. DR RefSeq; NP_001097212.2; NM_001103742.2. [P18475-3] DR RefSeq; NP_476762.1; NM_057414.4. [P18475-1] DR AlphaFoldDB; P18475; -. DR SMR; P18475; -. DR BioGRID; 61589; 35. DR IntAct; P18475; 2. DR STRING; 7227.FBpp0088012; -. DR GlyCosmos; P18475; 12 sites, No reported glycans. DR GlyGen; P18475; 12 sites. DR iPTMnet; P18475; -. DR PaxDb; 7227-FBpp0111751; -. DR EnsemblMetazoa; FBtr0088938; FBpp0088012; FBgn0003733. [P18475-1] DR EnsemblMetazoa; FBtr0339117; FBpp0308262; FBgn0003733. [P18475-3] DR GeneID; 35717; -. DR KEGG; dme:Dmel_CG1389; -. DR UCSC; CG1389-RA; d. melanogaster. [P18475-1] DR AGR; FB:FBgn0003733; -. DR CTD; 21977; -. DR FlyBase; FBgn0003733; tor. DR VEuPathDB; VectorBase:FBgn0003733; -. DR eggNOG; KOG0200; Eukaryota. DR InParanoid; P18475; -. DR OMA; AEIEWQP; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P18475; -. DR BRENDA; 2.7.10.1; 1994. DR SignaLink; P18475; -. DR BioGRID-ORCS; 35717; 0 hits in 1 CRISPR screen. DR ChiTaRS; Egfr; fly. DR GenomeRNAi; 35717; -. DR PRO; PR:P18475; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0003733; Expressed in egg cell and 14 other cell types or tissues. DR ExpressionAtlas; P18475; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:FlyBase. DR GO; GO:0030381; P:chorion-containing eggshell pattern formation; HMP:FlyBase. DR GO; GO:0007369; P:gastrulation; IMP:FlyBase. DR GO; GO:0007552; P:metamorphosis; IMP:FlyBase. DR GO; GO:0046957; P:negative phototaxis; IMP:FlyBase. DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase. DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:FlyBase. DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:FlyBase. DR GO; GO:0007278; P:pole cell fate determination; IGI:FlyBase. DR GO; GO:0007280; P:pole cell migration; IMP:FlyBase. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:FlyBase. DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:FlyBase. DR GO; GO:0007362; P:terminal region determination; IMP:FlyBase. DR GO; GO:0008293; P:torso signaling pathway; IDA:FlyBase. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR CDD; cd00192; PTKc; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR PANTHER; PTHR24416:SF583; TYROSINE-PROTEIN KINASE RECEPTOR TORSO; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR Genevisible; P18475; DM. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Developmental protein; Glycoprotein; KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Receptor; Reference proteome; Signal; Transferase; KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..923 FT /note="Tyrosine-protein kinase receptor torso" FT /id="PRO_0000024477" FT TOPO_DOM 21..399 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 400..420 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 421..923 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 475..874 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 656..687 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 741 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 481..489 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 502 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 608 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT CARBOHYD 37 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 63 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 107 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 142 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 146 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 287 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 298 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 314 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 326 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 342 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 348 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 377 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 389..393 FT /note="Missing (in isoform D)" FT /evidence="ECO:0000305" FT /id="VSP_058212" FT CONFLICT 125 FT /note="A -> T (in Ref. 1; CAA33247)" FT /evidence="ECO:0000305" FT CONFLICT 387 FT /note="H -> P (in Ref. 1; CAA33247)" FT /evidence="ECO:0000305" FT CONFLICT 667 FT /note="R -> Q (in Ref. 1; CAA33247)" FT /evidence="ECO:0000305" SQ SEQUENCE 923 AA; 105201 MW; 746F46E1A4277ACF CRC64; MLIFYAKYAF IFWFFVGSNQ GEMLLMDKIS HDKTLLNVTA CTQNCLEKGQ MDFRSCLKDC RINGTFPGAL RKVQENYQMN MICRTESEIV FQIDWVQHSR GTEPAPNATY IIRVDAVKDD NKETALYLSD DNFLILPGLE SNSTHNITAL AMHGDGSYSL IAKDQTFATL IRGYQPSKMG AVNLLRFVPQ PDDLHHIAAE IEWKPSAESN CYFDMVSYST NSVNMDEPLE VQFRDRKKLY RHTVDNLEFD KQYHVGVRTV NIMNRLESDL QWLPIAVPSC LDWYPYNYTL CPPHKPENLT VTQKQYLPNI LALNITWARP RYLPDNYTLH IFDLFKGGTE LNYTLDQNRS HFYVPKITVL GSHFEVHLVA QSAGGKNVSG LTLDKVHRGV LLSEGNMVKL VLFIIVPICC ILMLCSLTFC RRNRSEVQAL QMDAKDAKAS EFHLSLMDSS GLLVTLSANE SLEVMDELEV EPHSVLLQDV LGEGAFGLVR RGVYKKRQVA VKLLKDEPND EDVYAFKCEI QMLKAVGKHP NIVGIVGYST RFSNQMMLLI EYCSLGSLQN FLREEWKFRQ EQNAIGLKKN LEQNVDNRRF NRLPRNSIHD RIEDINNSML STVEEESESD QTHSSRCETY TLTRITNAAD NKGYGLEDIE NIGGSYIPKT AEAPKDRPKR KLKPQPKKDS KQDFKSDNKK RIFENKEYFD CLDSSDTKPR IPLKYADLLD IAQQVAVGME FLAQNKVVHR DLAARNVLIS VDRSIKIADF GLSRDVYHEN VYRKSGGSGK LPIKWLALES LTHQVYTSQS DVWSFGVLLY EITTLGGMPY PSVSPSDLLQ LLRQGHRMKR PEGCTQEMFS LMESCWSSVP SHRPTFSALK HRLGGMILAT NDVPERLKQL QAATESKLKS CDGLNSKVEQ VPCEEELYLE PLN //