ID A0A0V0W5C0_9BILA Unreviewed; 1585 AA.
AC A0A0V0W5C0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN Name=Igf1r {ECO:0000313|EMBL:KRX70922.1};
GN ORFNames=T06_8762 {ECO:0000313|EMBL:KRX70922.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX70922.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX70922.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX70922.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 ECO:0000256|RuleBase:RU000312};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX70922.1}.
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DR EMBL; JYDK01000261; KRX70922.1; -; Genomic_DNA.
DR Proteomes; UP000054673; 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 GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
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 InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
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; 3.
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.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 3: Inferred from homology;
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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000312};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1115..1138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 757..853
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1008..1107
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1179..1454
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1489..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1585 AA; 179338 MW; 9AABE8AAF05AD0DA CRC64;
MRKIEIFVAF YSNLTDQSSE KNRKLSKPLG FVHLYFQMNR NNVRAKRRRS LFCSVRDEQR
RPSRAAGQTV LSTTLSDLCR AGAMRAASAD RRHLIALLVY LVLFTNNITQ CLEEVVDLGR
KKNGIVECLQ SSFRTAEFGD LESVYQSVTR NNRRQRMLQN YFFLIIISLC GGFDIRNSPK
RFIENLGPRA RLQWRRCTVI EGDVRLILMT RDNMTQEDFN VAIMPNLREI TGSVLVFQVV
GLESLGALFP NLRIIRGNGL VYNYALVLFQ NPNLREINLA NLTEISKGGV RIVNNGELCY
VNTILWSQLC REEDAHIVIE GNRDPMLCSE KCTDTTNDPF CAQHTNSEGP SKACWNGENC
QLACPAECTE KNLACNTTME KPFCCHRRCV GGCIGPTDRD CYACRDVIYQ GQCLDKCPKG
LYELGHRRCI NQEECISRHP VKDEVTGDIL RYKALDAEGS CVLKCPTGYE EDPNDDRKCV
LCQGVCLKKC FGGDVRSLAE AAQFKGCNIV LGPLDIMMQR NVAGKLEEYL GDIREITHYL
KVSFSPSFVS LNMLKNLRII RGQELWNDKY ALSVFENEHL SKLWNFTAGE EKLHIENGKL
QFHNNPNLCY RTIVELVEIV GQKDSLHEFD VSPMSNGNKA VCEELEIEIE RRFVGPDTIV
LRWDTFNTSM MDHRMFLGYQ LYYRPVDSEN VSIVENRDAC HDSWKMLFYQ PSERGAFLSE
LKPYTLYAFY ITTLMVNSPG ARGGISKVVY VRTAFGHPSS IILKKVESRS PWTIYLEWEP
PLLPNGEVTH YMISYVEKVR ATSSDRNYCE EPPDYSVNLD KLPGSNSAAA LHRALTAAQM
DLSSWHHGSS SEGVCSQVKC CECSGTTISN ISGPVPNHEL LASEQKERAV FENIIHNIVF
VSNRHKRQVI GPLNVDDDTF DFTSLNNMNS GGRAAYAVAF GANGAVIKPN VVNVTDTNFT
IEHLHHFTMY EIKIWACQNQ SVAENHCSRR EVVIMKNTML IESKDAINDS SVLIYNASEA
THDRFISWTP PIDPNGVIVS YEMEYLRNMD GDVKPKRDCI TQNDFMEKLG FLIQDLPPGN
YSFRIRALSL AQRGPWTSYF AFIIPERAKV TETTVILIAF GCSFFAIIFG VLLVIAVYRR
KYKKKLPEYL LNVFSANPEY ISQLEVYKPD EWELKRGDIE LLKEIGRGTF GTVYAGRGRN
VRSVRGDTFG ECAVKTVSDK ASIYDRWHFL IEASVMKKFD TAFIVKLYGV VSEGQPALVV
MEMMSKGNLK DYLRSRRPGA EENVHNLVPP TEEEMFNYAA EIADGMAYLE AIKFCHRDLA
ARNCMVSVDG SCKIGDFGMA RDVYVKDYYR PQGRRLMPVR WMAPEALKDA KFTSKSDIWS
YGVILWEIAT LANQPYAGLA NEEVMRLVVD HRKIMEKPKD CPKRMYDLML LCWKYDPKDR
PLFSELAASL YDDLPSQFKS ISFCGKNGIK GTRISRRAAC GAGDPFLQCS SSQGHSRHLR
DGGGGRSDRR PRLTIGIGGA MSVSAVDHHK APLCKNNRVP QAKIGSAQSW MKRSSPTRRD
RRLASSVDPR EGNGALLNGH ATSVD
//
