ID A0A3P6T266_LITSI Unreviewed; 1463 AA.
AC A0A3P6T266;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN ORFNames=NLS_LOCUS2298 {ECO:0000313|EMBL:VDK73980.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK73980.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK73980.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; UYRX01000103; VDK73980.1; -; Genomic_DNA.
DR STRING; 42156.A0A3P6T266; -.
DR Proteomes; UP000277928; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_dom.
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 InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF604; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF12810; Gly_rich; 1.
DR Pfam; PF00629; MAM; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50060; MAM_2; 1.
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|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|RuleBase:RU000312};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|RuleBase:RU000312};
KW Reference proteome {ECO:0000313|Proteomes:UP000277928};
KW Transmembrane {ECO:0000256|RuleBase:RU000312}.
FT DOMAIN 325..534
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 973..1246
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1260..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1004
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1463 AA; 161906 MW; 8B40D1F70D802CA4 CRC64;
MFEAMQKFPI SNALDDAFAS AVKPFASVGK CCSAELTSFS STILAELKIK EENAISTSHP
QETTSLQQLL LATTTTCYDQ SLELFGILCD FESKCDWIFE SPARKYPRDP RHNFKVVVGN
RGSTPTHYAY FNFTKTREEP AMIISPYYQH LSVQCELRFT FRLFGDSDTT LMVTTQHRAL
NEATNYADQY DYDDQTEWTR PTLHSTFNAQ NNYVNLWKEV GVHIGRATDP TRIRIECHSK
GNSAISTSKR SAECYIDNIE MVKCDEEVWY ENMCQSNKTK KYLCHKYDRP KCIDYDQLCD
MTVDCAEAED EQTDLHNCTS VPIGARCTFE DENEVKTGCI GWRLETYYVH NSRRADDNKH
LFIRANSIDA AKQSSLKHVP SSDHTFQNTN NSGHFLYFTS EDDEGQNSFT DTKSTYLISP
YFPPTAANSA SPHSSASLQL NSCRIRFYYC SYGSAISTLQ LTVHPVNGQP PKIIWTPPSL
SFTDHSYYCE WMKVSIDLPE QKSGYYLKMG VSRIFDASIS FAIDDFSMTP DCFINGMLKA
WNTQYIPHVY NITSCGQRGS HQPTFENCQD FYNQSATKAL LRKNTSNGFQ RWIVPKTGEY
RIEAYGASGG HLAQQTVNNY GGQVISIVNL TVVTELNILV GQMGESPCDH FKTLADGISS
HQYEVLKYLC KKGDSIWNDE TALANAIMFP GTGGGGATVV KYQSMIALVA GGGGGVFPEQ
IIQLEKPSVS ARGGHSFDID KNLQPIDLHS AKRGILWMSG DGAHLLNDNK TKKCEQCAIM
SGQLNNVSSS GGVCPSVSVW KISGGFGGGG ASCGPGGGGG AGYYGGEGGQ KYHGRGGKSF
AQYKGAIIRP GLLLNLIVEE KGVNSGNGYV LIHPCRLHCS SNATCRFRLD KIDEIASYCA
CPNGQAVDEL QDCTFGVYFR RRLKKAKMEK EELNREIGMC ALTPSTPMSI SGNPIYEPFG
PCAELQSIPR ANVTLIRPLG QGAFGEVYEG TLNCSNQLIQ VAVKTLPKSA SKQAVNDFEM
EALIMSKFRH ENICELMGVC FDVTPKLIIL ELLAGGDLKS FLRECRPKST KDQRIQMVDL
LDMAQDVAKG CKFLADNRFI HRDIAARNCL LTKKEVGRIV KIADFGMARD IYRQDYYRKG
GKAMLPVKWM PPEAFLDGVF TVKTDVWSFG VLLWEIFSLG YMPYPGKSNQ EVMSLIVSGG
RLEPPNGVPD QIYTLMLACW STADTDRPHF DDIIENLDSL LQNPLMQNMP LPVIIHRLSQ
PQSAPSHSDS PSSVAEAVSQ NTYSQRTINT VLNSYTETVP SNDCDPLPTK GDGVNFNVCT
PYQPQSLESF CLLDGTEPKS AALSLCANDR LGSGSTETCT SDGAEPVPST TLRDAAAGSR
RPLVDTDLCS NRSVGGNYAN AIRGETVSLL ERRYPPPKKL RVRPPTISND FSSPSMIGAL
RSSNPSNDQQ SLLQNYMNQS QIL
//
