ID A0A182E0K1_ONCOC Unreviewed; 1398 AA.
AC A0A182E0K1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=NOO_LOCUS1479 {ECO:0000313|EMBL:VDK64256.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t01479-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t01479-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK64256.1, ECO:0000313|Proteomes:UP000271087}
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};
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DR EMBL; UYRW01000189; VDK64256.1; -; Genomic_DNA.
DR STRING; 42157.A0A182E0K1; -.
DR WBParaSite; nOo.2.0.1.t01479-RA; nOo.2.0.1.t01479-RA; nOo.2.0.1.g01479.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR CDD; cd00096; Ig; 1.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
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 PANTHER; PTHR24416:SF503; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS00290; IG_MHC; 1.
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|PROSITE-ProRule:PRU10141};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000271087};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 930..953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..296
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 391..494
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 751..831
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 840..919
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1012..1337
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT COILED 949..976
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 1200
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 1051
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1398 AA; 160826 MW; D429080C7BEA4514 CRC64;
MEELVDDTIQ QIFSDILRIE WFDEQDNDNL LSQALLYNRV IALPHRWKIN NPDDPGDASL
LANVNSLTHS SQKNSHDDSS AFSLIHHIPR LLAAFYGDIH KRTLATVRMK EVQCSSAKVF
RFGTDSHVCP RSLRATSPTI SSTKEHRYIS PAYSPLPSFY CRTSCRRRLM HLFHPFVAHL
FIILCFITSD ASPYAPVIIG NIDFREYKGQ QYIERKTGEA LELNCSTMEA VKWILPNNTL
SIDFDPNERT SRVTESGFDI GFRSLRIEPL KRSDTGEYVC VAEHSGFSSS IYVYVSNDKS
EKSVKTGSFL NSGPLIISKA LRGLNVVLPC RTDKFIESGV ELFINHVKQT TGIQFDPRIG
FVVDRRLLND RTEIPVRCEY LGHVSEMVIV PIKNDQEIED SPVIEMSSVW PYLRQKLEMN
CTFHTRDGFR YVLTWKCPQC EDGTGHVVSN RYVKIRDGIR KLLFIGDLHE ADSGDYECIV
TNKDDMHDVR RSVHRLQVSP TRGQLKVIDF SENVDFEEGD TVTLFHMARA FPSDEYSNGV
TSHEILPYLD FLSCRESIPF NSPEYSKTIS SRGELVEKID KDVRSKLNAD IHEDELSIIN
AAVDDSATYQ LVIRVSEDYV YRKNWTLSIR PISIQPRIII HDQFGQPLSS HVLIDSKIIV
TCIVKDTIPR KLRLLYETRD REWKQPDDYE ELSGFTYESA VKWITYAKEH MRIRCEDDET
KKIDEKDLVI SEVETINAYF IAKKPVDLLN EGSSIYEKDH LELICILPLD DEFDVSWVHD
NVQLSRPVRY ITLYSQKFKT TLDNISSDQS GDYHCIAKSK NDHISRTYTL HIKVNRVVAP
YIIEANEEYE HLAKYGERTE LACPIEGEPE PLYRWLKNGI EYNGYGSLTK KIDFPRVIVE
DKAIYTCVAK NRAGSQQLTG EPAYIRSSKY WWTLGFVTVS VLFLLLLALV FLLKQYRKSK
RQKEQLRALY NQLMSESNGE YLTGSIDLKQ PLHERVEQLP YDRRYEISKD KLSFKQLLGG
GHFGQVYLGE LKKPRVSDSL AVSDVLKVAI KAPRDGRNLH HQKALADELK IMIAIGIHPN
VLCLIGAVTK QMSSGQLYVI MEYCENDNLK DYLSKNSAGF LNEVEVNREP LSSDGYLTPT
RNAQHESQIY LAELKPQWAI EVDEVRMADK MITTGDLISF GYQVANGMEY LSSKMCIHRD
IAARNILVTK NRAIRIADFG LARKDSTVYH IRSSQNVPLP LKWMALESIL YHNFTEQSDV
WSYGILLWEI FSLGKVPYPQ VDNDDLVNYL QEGNRMEQPK FAPDDIYNLM RQCWLSDPSN
RPMFSECRVL MKTHLSRASP PLSARLDKML KEDQILMERY SEWRDAEENE LDLRAQATRN
GFIAVPTQEP QTNSNIYM
//