ID A0A0M3JY52_ANISI Unreviewed; 1570 AA.
AC A0A0M3JY52;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=ASIM_LOCUS12778 {ECO:0000313|EMBL:VDK48131.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001335001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001335001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK48131.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; UYRR01031248; VDK48131.1; -; Genomic_DNA.
DR WBParaSite; ASIM_0001335001-mRNA-1; ASIM_0001335001-mRNA-1; ASIM_0001335001.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; 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; 1.
DR CDD; cd00064; FU; 1.
DR CDD; cd05032; PTKc_InsR_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; 2.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
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; 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|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:UP000267096};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..1570
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035041450"
FT TRANSMEM 1059..1083
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1328..1349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 649..748
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1124..1463
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 651..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1570 AA; 178030 MW; 9B7A1E39D321BDC7 CRC64;
MILRQARSDR QSCRSPCIKN NFILTVLFFF TLVTQTLTGE DVYCRSLDIR NRPGMVFQDK
ETNDKLSTLT NCTVMEGDFS VSMITSANYT HESFPVFERL RVITGHLLVF QVSALRSLKR
MFPNLRVIGG QELIMNYALV IYQNTHLVEV GLPKLTTIVN GGVRIMDNTQ LCYSRYIDWG
TMLIGPANDI LIDQSKITDS DLCSDECVPE DESRCHKVDG VLSCWDAETC QIQCAYARNE
DKTPGPGCDD YGRKCHAQCL GGCSKPNDPS ACHFCKNVIH NGVCIQKCPD HLFEIHHVYL
IRRCVTLEEC RNISAPVTSE STKKQMLIVE NMCRVDCPFG QEIDPHNSSR CVKCEGYCPV
KCKGGTIDSY GRINDYHFKK CNVIEGYLEI ELRSGLDSAA IEKVGEAFGS IEIIEGYLLI
DFSVSFVSLN MFKRLRLIKG NTLWRDRYAL AVFENPNLRQ VFDIERQPLK IGNGTVLFQN
NRMLCYNRIK ALIDHIGLTD VKENDVSYYS NGDRAICNET TFEVRTEDVH SFGFMISWVA
FNTTDMDHRK FLGYQVFYKK VDGPDPNLTI DDDRSACSDS WQMHFEPEKG NAKEGLNRGT
GLFSVESNTW PVFTCFELYA YYVQTKLINH PGARNAISKI HFVKTLFSPP DPPKDVRGRS
TKHDQMDLEW DPPLRPNGDI THYIVKWQPF LSDSTSVAGH VCDDKAGAGR RHFRDPNRLP
TVAVSTATEQ QPVCSKQPGC CDCNALKKQG SVDISAEEME KNGEAAFENA VQNLVFVPQI
RKRGKCIAGR RGEILFIAQT PFVYKQRLMV PMNELFIFSD MNRNGGTVRR VRRSKRTINT
SSSQNHKQDL LSNEERLYGD QKAILITQNE VNESLSIYRA EVDTATHEIN VTTRHLTITG
LRHYTQYQIW IRACQNVSAP GGYHCSQRPG YLVVQTAPIP ENDLVDNSTI EVINTTSPTS
DQRSRKITWI EPSNPNGAIL AYKVKVIAED REQTPVTQCV KASDFRHQGG VTFHGLSDGI
YRVEVRTITL ASLALASTDE VAVSRSLFSV FTKPFFTKWV ISLIFLIIFL VLTIGSLIAY
YFLKKVFGKK VQEYARQQIS ANPEYLSQMD VYTADEWELK RSDIHLEEEI GRGTFGKVYR
GYANDVVSKG GVRFGECAVK TVAESANSAE RLHFLVEASV MKQFHTSFIV KLYGVVSDGQ
PVLVVMELMR KGNLRDYLRS RRPGGEDNVD NSPIPTNLEY IRWAAQIADG MAYLESIKFC
HRDLAARNCM VSADDTVKIG DFGMARDIYY HEYYKPTGIR LFHLDFISKQ FIRFIGDHLS
ETEMHFSLVL FHLNVFHFIL LTLISHYLAS IQFIIIRHTI LGKRLMPVRW MAPESLKDGK
FTMKSDVWSY GIVLYEMLTL AQQPYSGIGN EEVFNYIGVS RRILTRPTGC PDFWYDLMVQ
CWKYDPRDRP DFAQIVAKLL PYTDVDFVNA SFVASTAGSA VGDESVVDEV FQPKEVYPHA
NDESELVMNE DVIPSDSDER PICNWNRRTA GGGFRRGAAS EGARSVDHDL KMRVTNTLAG
TATENEEDEL
//
