TORSO_BOMMO
ID TORSO_BOMMO Reviewed; 807 AA.
AC D2IYS2;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Tyrosine-protein kinase receptor torso {ECO:0000305};
DE EC=2.7.10.1 {ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:26928300};
DE Flags: Precursor;
GN Name=tor {ECO:0000303|PubMed:19965758};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000312|EMBL:ACZ81657.1};
RN [1] {ECO:0000312|EMBL:ACZ81657.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
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).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PHOSPHORYLATION, DISULFIDE BONDS,
RP AND MUTAGENESIS OF CYS-381; CYS-393 AND CYS-394.
RX PubMed=26928300; DOI=10.1038/srep22437;
RA Konogami T., Yang Y., Ogihara M.H., Hikiba J., Kataoka H., Saito K.;
RT "Ligand-dependent responses of the silkworm prothoracicotropic hormone
RT receptor, Torso, are maintained by unusual intermolecular disulfide bridges
RT in the transmembrane region.";
RL Sci. Rep. 6:22437-22437(2016).
RN [3] {ECO:0007744|PDB:5AOQ}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 24-287 IN COMPLEX WITH PTTH,
RP SUBUNIT, DOMAIN, GLYCOSYLATION AT ASN-195, AND DISULFIDE BONDS.
RX PubMed=26698662; DOI=10.1016/j.molcel.2015.10.026;
RA Jenni S., Goyal Y., von Grotthuss M., Shvartsman S.Y., Klein D.E.;
RT "Structural basis of neurohormone perception by the receptor tyrosine
RT kinase Torso.";
RL Mol. Cell 60:941-952(2015).
CC -!- FUNCTION: Probable receptor tyrosine kinase. 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) (By similarity). Binding to PTTH stimulates activation
CC of canonical MAPK signaling leading to ERK phosphorylation
CC (PubMed:19965758, PubMed:26928300). {ECO:0000250|UniProtKB:P18475,
CC ECO:0000269|PubMed:19965758, ECO:0000269|PubMed:26928300}.
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 ECO:0000269|PubMed:26928300};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:26698662,
CC ECO:0000269|PubMed:26928300}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19965758};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the prothoracic gland in 4th and 5th
CC instar stage larvae, and P0 stage pupae. Also detected at lower level
CC in testes and ovaries of 5th instar larvae.
CC {ECO:0000269|PubMed:19965758}.
CC -!- DOMAIN: Contains 3 very unusual FN3 domains in the extracellular
CC domain. The second FN3 domain is involved in the binding to PTTH dimer.
CC {ECO:0000269|PubMed:26698662}.
CC -!- PTM: May be auto-phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:26928300}.
CC -!- PTM: At least one of the 3 cysteine residues Cys-381, Cys-393 or Cys-
CC 394 is involved in the formation of interchain disulfide bonds. The
CC disulfide bond sites in the extracellular region are not involved in
CC homodimer formation. {ECO:0000269|PubMed:26698662}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|RuleBase:RU000307, ECO:0000305}.
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DR EMBL; GQ477743; ACZ81657.1; -; mRNA.
DR RefSeq; NP_001164049.1; NM_001170578.1.
DR PDB; 5AOQ; X-ray; 2.70 A; A/B=24-287.
DR PDBsum; 5AOQ; -.
DR AlphaFoldDB; D2IYS2; -.
DR SMR; D2IYS2; -.
DR STRING; 7091.BGIBMGA003976-TA; -.
DR iPTMnet; D2IYS2; -.
DR GeneID; 100322874; -.
DR KEGG; bmor:100322874; -.
DR CTD; 652945; -.
DR eggNOG; KOG0200; Eukaryota.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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; 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 3D-structure; ATP-binding; Cell membrane; Developmental protein;
KW Disulfide bond; Glycoprotein; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..807
FT /note="Tyrosine-protein kinase receptor torso"
FT /evidence="ECO:0000255"
FT /id="PRO_5003032856"
FT TOPO_DOM 29..370
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..807
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 439..738
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 607
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 445..453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 205
FT /note="Implicated in PTTH ligand binding"
FT /evidence="ECO:0000269|PubMed:26698662"
FT SITE 219
FT /note="Implicated in PTTH ligand binding"
FT /evidence="ECO:0000269|PubMed:26698662"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:26698662"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 46..61
FT /evidence="ECO:0000269|PubMed:26698662,
FT ECO:0007744|PDB:5AOQ"
FT DISULFID 81..203
FT /evidence="ECO:0000269|PubMed:26698662,
FT ECO:0007744|PDB:5AOQ"
FT DISULFID 210..239
FT /evidence="ECO:0000269|PubMed:26698662,
FT ECO:0007744|PDB:5AOQ"
FT DISULFID 259..265
FT /evidence="ECO:0000269|PubMed:26698662,
FT ECO:0007744|PDB:5AOQ"
FT MUTAGEN 381
FT /note="C->P: Forms non-covalently attached homodimers which
FT become phosphorylated independently of ligand-binding but
FT fail to induce ERK phosphorylation in response to PTTH
FT binding; when associated with P-393 and P-394."
FT /evidence="ECO:0000269|PubMed:26928300"
FT MUTAGEN 393
FT /note="C->P: Forms non-covalently attached homodimers which
FT become phosphorylated independently of ligand-binding but
FT fail to induce ERK phosphorylation in response to PTTH
FT binding; when associated with P-381 and P-394."
FT /evidence="ECO:0000269|PubMed:26928300"
FT MUTAGEN 394
FT /note="C->P: Forms non-covalently attached homodimers which
FT become phosphorylated independently of ligand-binding but
FT fail to induce ERK phosphorylation in response to PTTH
FT binding; when associated with P-381 and P-393."
FT /evidence="ECO:0000269|PubMed:26928300"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:5AOQ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:5AOQ"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 174..194
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:5AOQ"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:5AOQ"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:5AOQ"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:5AOQ"
SQ SEQUENCE 807 AA; 91552 MW; 54B4010F9D1031A8 CRC64;
MYSEGKLLKV FLIFAGFIIF SLCGEVVSQR YPPAPGLLKY LEQDVCYSLY YYLNWTSLAD
CKTNFEETGI SDVPSTVKVR CQSKNSIRFE TEPSEHWQLF ILMEHDNFDP IPFTLIEPNN
VFGELITTAN KEYQIWSTYL DEYGTLQDWM EGPIVLKFDQ RNQQPDDIKY NVTQEFKYII
LGNDSYTING KFVWNTTGDR DLCFDIANIC QNTNMKHAKI WPTAHPSFDV ENLVLNDECE
IHVKGIHGTT KHKYKTPSCF ELPECFLNNM EPEIPQDVAI AADQDLRGWW NINVAWAKPH
FQPEIYNVTV RANMIRSIIL PGNATETTFR NIPNTFLSAG KIYNVSVYAI IGQKASHTSR
RAFTPGMLRW VWAGATAGAG CAAGGLLAAT LLCCGHRRAT SRVSQEDPDE KTPKEDDVEI
IGIESGSADD HWEVRSDRVL LHEVIGEGAF GVVRRGTLAP GGKSVAVKML KEFPSQEEVR
SFRSEMELMK SVGAHPHVVS LVGCCSGRKP LIVAEYCSRG DLLSYLRSSW DIIVSKHTAK
YYNNNMDSMD TSKLKVHKEH TKLVVNKLYE LQGPCETELT PLDLLSFCRQ IAMGMEFLAS
NRIVHRDLAA RNVLVTEDKT LKIADFGLSR DIYEENQYKQ KGNGKMPVKW MALESLTRRV
YTTQSDVWSF GVVIWEIVTV GGSPYPEVPA ARLVRSLRSG YRMPKPVNCS KPLYDIMRAC
WNASPRDRPT FPELHQKLDD LLHSACANEY ITLEVDVDEA PSTPKPQRYI KMLIRGKLPW
SRESYERPVN PTSNLYSSPP VIQTKTA
