TORSO_DROME
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 03-AUG-2022, entry version 203.
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}.
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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.FBpp0111751; -.
DR GlyGen; P18475; 12 sites.
DR iPTMnet; P18475; -.
DR PaxDb; P18475; -.
DR PRIDE; P18475; -.
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 CTD; 21977; -.
DR FlyBase; FBgn0003733; tor.
DR VEuPathDB; VectorBase:FBgn0003733; -.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; P18475; -.
DR OMA; APSCLDW; -.
DR PhylomeDB; P18475; -.
DR BRENDA; 2.7.10.1; 1994.
DR Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DME-186763; Downstream signal transduction.
DR Reactome; R-DME-186797; Signaling by PDGF.
DR Reactome; R-DME-210993; Tie2 Signaling.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DME-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
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 tissues.
DR ExpressionAtlas; P18475; baseline and differential.
DR Genevisible; P18475; DM.
DR GO; GO:0005887; C:integral component of 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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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 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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
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
