ID G0N858_CAEBE Unreviewed; 1851 AA.
AC G0N858;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=CAEBREN_08229 {ECO:0000313|EMBL:EGT55050.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001171};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; GL379849; EGT55050.1; -; Genomic_DNA.
DR STRING; 135651.G0N858; -.
DR EnsemblMetazoa; CBN08229.1; CBN08229.1; WBGene00146954.
DR eggNOG; KOG4258; Eukaryota.
DR HOGENOM; CLU_000288_166_3_1; -.
DR InParanoid; G0N858; -.
DR OMA; HRCWHHR; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000003; P:reproduction; IEA:UniProt.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00064; FU; 1.
DR CDD; cd05032; PTKc_InsR_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
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:SF525; INSULIN-LIKE RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00261; FU; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1168..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1296..1314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 749..846
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1061..1162
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1230..1514
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1777..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1807..1833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1851 AA; 207740 MW; C1F8011A612974E6 CRC64;
MVEEETTEES TEEYPPSTSY CHQDPPNPPE HQQPTEDESA TTPRTLRIMS DNRHDDLVVD
DSNTTMRHRR RCFVNFRRTR RRKPVDDAST TARTTTTLGS TLKFHRPMLI LLVLCAIFKP
TISEAELRCG PVDIRNKPWN FRQQWSRLGD PNAVNFMNKS VVDCTVVEGS FSISFIYQPQ
NHSAPRIRAD QFPRFPKLKE ITGTLLVFET NALKNLRDVF PNLRVIGGQT LIQHFSVIIY
RNVDLEILGL DKLTVIRNGG VRIQDNKKLC HPKTIDWKGM IQGPINDVMV DDAAAMSVSE
TGKLCPIGCD DNDKDFTKCR YLNEGNNRIQ SCWNDTTCDL KCDHEFVEGK AGPSGPGCDP
FGNRCHEQCL GGCDRANDAG ACSACQHFHY NGKCVEECAK HLYVLMDRRC VSKEECLSYN
PHHKNVKVPI KATAGLCSDR CPNGYEIDKT NPHACKKCDG KCVITCTIDH VIDSFPKALA
LKRCNIIEGN LSIEMRGKQD SGMAAQLKDV FGNIQVITGY LRIQRSTPFL SFAMFKSLKR
IEARSLYNNK YAVVVVENQN LRRLFESYTK FTIGRGTVFI HNNRMLCFIH VENLMKDLGI
FEKHTVDDQS PESNGDKAIC QDMVIEVNVT ETFATTIFFE WPGFNTTNMD HRKFLGYELY
YKEVPAIDPN MSIDDDRSAC VDTWSSIFIE HRERDDMAIA ERITAKLDAA NRIRPNTLYA
YYVATQMVHH AGARNGISKI GFAKTKFSVP DAPVFVNIIS GKESISVSWD PPHITNGEIG
FYHVTWRAVE ASTDEMVKGC CLNDRERNTD DKSYQNKYDM KLAVKEDAVS SFVSKIKGEE
QPTCSAIENC CECSAVPAAA PAGKSGPPDH ATTVEQANFE NTVMDTVLVQ RDTLRSRRSI
ENANRVSKEL EREEAKEKKQ QKKAPPRKLV YKDKKTTPTT TTTTTTTTTT TVPTTTIPRK
LKYDLLPPLV NENSEIFRKM NTIYDISSPN DTHRDSSPLF GINVTDGNSY TITGLKHYTL
YGISIAACQV RLNTSEYYCS PTHKAGVTKL TLPIYEMDRI DNNTIRVSPG NNSRQLLVKW
DPPQYPNGGI RGYMIQLDGI NHKDEKVRCK GASSGWSPAV NGVTIDGLTH GFYKIKIKTI
SLSGIGPEAE AILDDARIIE PSWVTVPMII GFLSIVLFIA TAIGVGTYYW VQIHYGKKVK
ALADFMHLNP EYCVDNEYTP DDWELDPASV TMMDQIGEGS FGKVYIGMGK NCQSLYGCTF
GPCAIKINVS DAENAAENQM NYLMEATIMK NFKTNFIVKL YGVISTFNPA WVVMEMMEKG
NLRDYLRAKR EDEIFNEMDC NFFDVIPREK FTNWAAMICD GMAYLESLKF CHRDLAARNC
MIDANEVVKI GDFGMARDLF YHDYYKPSGK RMMPVRWMSP ESLKDGKFDS KSDVWSFGVV
LYEMVTLGAQ PYIGLSNDEV LNYIGMSRKI IRKPECCSDY WYKIMKMCWR YSSRDRPTFL
QLVHLLSAEA SPEFKEMSFV LTENQMAMED SEPLDLDQID IWEEPEPEKT QAQTPEGGAP
KGDESDGAAN GDYEIQDPSA RRNTDSIPMK QFKTTMPTSP STLSVDSGAK KQQKNPDDEY
QLMTHSRGPS DNEVRHYGTD HDGDYVERDV HNDVPTRRNT GASTSSYTGG PYCLSNRGGS
NERAGFGEGL RLTDNIGSGH LHDDNDYVEK DLSSMDTRRS TGASTASYGV PQVTNWSGTR
GATYYANKQQ QAAQAAAAAA AALAASQQQQ HALLNGRGDR LTQLPGTGNL PAPRGRDEDY
IETMPRSNGG GRNQGSPSRN GNTGPNRGSF NGRSAFGENE RLIEDIEHPL S
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