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Database: UniProt
Entry: A0A0V0XQX5_TRIPS
LinkDB: A0A0V0XQX5_TRIPS
Original site: A0A0V0XQX5_TRIPS 
ID   A0A0V0XQX5_TRIPS        Unreviewed;       707 AA.
AC   A0A0V0XQX5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Epidermal growth factor receptor {ECO:0000313|EMBL:KRX90408.1};
DE   Flags: Fragment;
GN   Name=Egfr {ECO:0000313|EMBL:KRX90408.1};
GN   ORFNames=T4E_8900 {ECO:0000313|EMBL:KRX90408.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX90408.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX90408.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX90408.1};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:KRX90408.1}.
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DR   EMBL; JYDU01000166; KRX90408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0XQX5; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR   GO; GO:0000003; P:reproduction; IEA:UniProt.
DR   CDD; cd00064; FU; 3.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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:SF566; EPIDERMAL GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 5.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF52058; L domain-like; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000313|EMBL:KRX90408.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        440..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        685..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          501..707
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         534
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX90408.1"
SQ   SEQUENCE   707 AA;  79396 MW;  2A10EED3E531538E CRC64;
     LVVQKWMEFI PYDPMTPAQL EALSSVRQVT HYVLVQTEKL KSLNFLRNLQ KIEGRKLFDS
     KYALYITHSF SLQQLGTISL TSVLNGEIYI ASNFDLCYIH NIPWNKLIAS THSVAKVRKN
     READVCEAEG RTCDVSCDLS QGCWGPGSEM CFECLHWRLG NVCVDDCSSD GEYQASPKQC
     ALCHSECISC TGPGSRNCTK CRHVSLDGEC IRNCPQETHF ENPATHVCEP CHANCYSYGC
     TGSGNFVGIG GCNRCKYGVF DEDTQSITRC LRELSAERLC SEFPDLENYY WTVPLSTKIQ
     TEVAHAVCMK CHPACKSCYG YGVDFVHYGC DCLNYTYRET PTSSVCVLQC PKNTFIRPAP
     DAGRADECIP CDSQCDGCVG PTSTDCVECV TYKDYLSDTD RFNCTNVCPA DRPYVSADRL
     CTDINMDEVI YEKNKRMQTI VISAVVAALF LGFVVFLILI LFMKRKASLL AHLEEPDPKL
     EINSDACPNL TRLLLIRESE LKRGGILGYG AFGAVYKGVW IPQKEKVKVP VAIKVLHEAN
     AAAQQETLEE ARIMASVSHT YLVRLIGVCV GQQMMLVTPL MPLGNLLDYV QENKSKIGSA
     ALIRWSSQIA GGMSYLEEHR LVHRDLAARN VLVKTPYHVR ITDFGLAKLL EYGQEEIKIF
     EGKMPIKWLA LECIQYRRYT HKSDVWAFGN FIFEFSLFVA FYSAQKC
//
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