ID A0A1I7UFJ3_9PELO Unreviewed; 1871 AA.
AC A0A1I7UFJ3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g8812.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g8812.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 STRING; 1561998.A0A1I7UFJ3; -.
DR WBParaSite; Csp11.Scaffold629.g8812.t1; Csp11.Scaffold629.g8812.t1; Csp11.Scaffold629.g8812.
DR eggNOG; KOG4258; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
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; cd19941; TIL; 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 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 1191..1213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 777..876
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1082..1184
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1252..1538
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1636..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1815..1871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1833..1850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1857..1871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1871 AA; 209392 MW; E9FC2CCA7C630358 CRC64;
MIPKGTSNAN SEDDTAATMT MNMVRSRQRH KCQDYCTTTE DDGEAEAEEN QEEEELFLQP
STSCPHPQPQ PTLPARPKDP EDVAETPRRI MKRTATGDVV DATMMPRRRQ FGRTRRRSDS
TDDPPSRSSL DFLPSFSSTF LYLVLLFAIL QPVASITELR CGPVDIRNKP WHFRQQWSRL
GDPNAVNFYN KSVVDCTVVE GSFTISFVYD YNDKSLPPLK STDYPVFPHL REITGTLLVF
ETTALKNLND VFPNLRVIGG QSLIQHYALI IYRNMDLHTI GLEKLSVVRN GGIRIQDNKY
LCHAKSIEWK NMIMSPINDV VVDNAADLAV AETGIICTKA PCEQDKDYKK CRYLESAGHQ
RIQSCWSNST CHKVCNHEMQ NGYMGPGCDP KGNRCHEQCI GGCDRPDDNT ACSACRHVHH
RGRCIEKCDE GLYLLMDRRC VTYDECLSLN PVHANKTVPI KATAGICSDR CPLNYEIDPH
DKHKCRKCDG KCIITCQLNH IIDSFPKALA IKRCNIIEGN LKIEMRGKQE SGMAAELKEV
FANIHTITGY LSIQRSPPFL TLSMFRSLKR IEARELYNDK YALVVVENQN LRKLFEDNIN
FTIGNGTTQF HNNRMLCFSH VMTLMKRLNI TVNEFSQSPS SNGDKAICED TRIYVNVTMV
SADQIGFEWT PFDTTDMDHR KFLGYELYWK EVDAIDPKMS IDDDRSACVD SWSSVFLQHI
ERDDMQMVAK VETVLTGTNR IRPYTIYAFY VATQMVHHAG AKNGISKIGF VTTKFSVPEP
PTLTTAKADT ESITIAWEPP HQPHGQITHY LISWRELNTH VEHAAQLFCS TGSFSDTSKN
TNEPPDAYDP NYDDWALPSE SSATVSKSKA KGTCSAFANC CECSATSGAA LLTGSTTEMS
LIEKEEKDDF ENEVMDVAIM PSEAIRARRS IKNTNRNNEM LEKEEKEEAK KRKIIQVKKT
TTPKPTTPGT TPGTTPAGPS TTTEFISDMQ QYAVFGGRIP EGRWQFGVPT IISKEGEEIR
WGVNVTAKET GNYYQIRFLK HFTLYGLSVS ACQNVSHAEN YCSHDYKAGA KKRTLPLENL
DRVDNRTIKA APGNTTGAVV ITWQDIQDSN GGIRGYEVRM INTETRLTTT KCLGATSKWN
ASVHGAYFNG LPGGDYIVQI VTTSMKGAGP EVNALEHVSV FVPGFFTVQR VAFILVLIMF
ILGCVAVAVY YYVQVHYGKK VKALADFMHL NPEYCVDNKY LADDWELDPS LVTLGDQVGE
GSFGKVFLGY GKDILSLYGC RFGPCAIKIN QMEGPQPANN ENALNYLMEA NIMKNFKAHF
IVKLYGVISS CDPAWVVMEV MELGNLRDYL RSKREDEVFN EMECNFYDIV PREKFQEWAA
QVADGMAYLE SLKFCHRDLA ARNVMINNQE ICKIGDFGMA RDLFYHDYYK PSGKRMMPVR
WMSPESLKDG KFDSKSDIWS FGVVLYEMVT LGAQPYIGLS NDEVLNYIGM ARKVIKKPEC
CSEYWYKIMK MCWRYSPRDR PTFLQLVHLL SAEASPEFKE KSFVLTENQM AMEDTEPLDL
EEIDIWGDDP EAIAASTLPD MQKTPPPPTG EDQEDPKMRR NTDSIPMKEF KIAASPSTLS
VDVTTVRQRS VDDEYALMNH SRGPSDTEVR NYGGDGDYVE RDVQNDVPTR RNTGASNSSY
TGGPYCLANR GGSNERAGFG EGLRLTEGIG SGHHLHEDGD YVEKDLSMDT RRSTGASTTS
YGMGMGMQTQ PTNWSGSRGA TYYANKAQQE KAAAAAAAAA AAAAHQQALI NGRGDKLTQL
PGTGHIQRGR DEDYIETQPL NGGGAAGAAG GRNNGSPSRN GNTGPNRGSF GRNTGFGEHE
RLIEDTEHPL K
//
