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Database: UniProt
Entry: A0A368FXJ0_ANCCA
LinkDB: A0A368FXJ0_ANCCA
Original site: A0A368FXJ0_ANCCA 
ID   A0A368FXJ0_ANCCA        Unreviewed;       543 AA.
AC   A0A368FXJ0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN   ORFNames=ANCCAN_18648 {ECO:0000313|EMBL:RCN35485.1};
OS   Ancylostoma caninum (Dog hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN35485.1, ECO:0000313|Proteomes:UP000252519};
RN   [1] {ECO:0000313|EMBL:RCN35485.1, ECO:0000313|Proteomes:UP000252519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Baltimore {ECO:0000313|EMBL:RCN35485.1,
RC   ECO:0000313|Proteomes:UP000252519};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Ancylostoma caninum.";
RL   Submitted (OCT-2014) 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: 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:RCN35485.1}.
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DR   EMBL; JOJR01000657; RCN35485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368FXJ0; -.
DR   STRING; 29170.A0A368FXJ0; -.
DR   Proteomes; UP000252519; 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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   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; PF07714; PK_Tyr_Ser-Thr; 2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   Kinase {ECO:0000313|EMBL:RCN35485.1}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000252519};
KW   Transferase {ECO:0000313|EMBL:RCN35485.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU000312, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..362
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          478..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   543 AA;  60679 MW;  82F235C81DAB009E CRC64;
     MLQHKLAVIV LLFCLSMCLF GIIRMLRRAY KKPPTAADQI KLVVMQSDYK DVDVGESYWD
     QIASLPCLPW DEIAIGREIG TGAFGTVHEG RTSDGKAFAV KTICMNKSTS AEAQREFAFE
     ALFMHKFNHP NIVRLHWIQW DPPRLRIILE LMEGGDLRSF LRDARPTQEN LNPFDLSILD
     IVNISLDIAR GCEELNRQKY IHRDLAARNC LLTERGPNRR AKIGDFGMAR DIYENNYYRK
     GGRAKLPVRW MPPEAFLDGL FTTQTDVWSF GEYLSSTLNL LNERILKLHY LGVVLWEISS
     FGMLPYFGVD NFDVMGLVTN GGRLDAPNTV PVELQEVMRN CWNTRPEDRP SFSEIVAALE
     LLAQREELAH QPICCLAPAS SALVSPVICS APMMPSPSIS LADTPCTVVT ALSPMTPDRT
     GVQNYLNSMN VQAVLGSNIL RVIFNKIEGF GVSMTGVPYI PINTAALREV FAEKSSMMEE
     QRNPDLEKLI RPGTADGGDP SPGAVEDNID DTIAKVKQAL FGSIVPPTPP PRRPTTLPRL
     RNT
//
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