ID Q153D7_XENLA Unreviewed; 789 AA.
AC Q153D7;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE Flags: Fragment;
GN Name=egfr {ECO:0000313|EMBL:ABG35749.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:ABG35749.1};
RN [1] {ECO:0000313|EMBL:ABG35749.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16258939; DOI=10.1002/dvdy.20623;
RA Nie S., Chang C.;
RT "Regulation of early Xenopus development by ErbB signaling.";
RL Dev. Dyn. 235:301-314(2006).
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; DQ646918; ABG35749.1; -; mRNA.
DR AlphaFoldDB; Q153D7; -.
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:UniProtKB-KW.
DR GO; GO:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR CDD; cd00064; FU; 2.
DR CDD; cd05108; PTKc_EGFR; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 6.10.250.2930; -; 1.
DR Gene3D; 3.80.20.20; Receptor L-domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR044912; Egfr_JX_dom.
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; IPR049328; TM_ErbB1.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF91; 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 Pfam; PF21314; TM_ErbB1; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {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, ECO:0000313|EMBL:ABG35749.1};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 297..554
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 330
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:ABG35749.1"
FT NON_TER 789
FT /evidence="ECO:0000313|EMBL:ABG35749.1"
SQ SEQUENCE 789 AA; 87982 MW; 7121C5133FED0159 CRC64;
TDLNVFENLE VIRGRTKQRG TYALAIVQRS ITALGLQSLK EVSDGDVIIK TNKNLCYVNT
INFTNMFRTP KQIKIINDNK NPEQCESEGK VCDTLCSEEG CWGPGPSQCV SCLKYIRGKE
CVENCNFLSR EPRGYTVDGR CFSCNVECLQ LNDTQTCSGP GADECFKCAH YSDGPFCVKT
CPAGIHGENN SLIWKYPDEN GACQLCHPEC KLGCAGHGID GCPPPWSYHS VAAGVVGGIL
GAVVIGLVAF FFIRRSRINR KRTLRRILQE RELVEPVTPS GEAPNQALLR ILKETEFKKI
KVLGSGAFGT VYQGLWIPEG EGIKIPVAIK ELREATSPKA NKEILDEAYV MASVENPYVC
RLLGICLTST VQLITQLMPF GCLLDYVREN KDNIGSRHLL NWCVQIAKGM NYLEERRLVH
RDLAARNVLV KGPQHVKITD FGLAKLLGAD EKAYHAEGGK VPIKWMALES ILHRTYTHQS
DVWSYGVTVW ELMTFGLKPY DGIPASEISN ILEKGERLPQ PPICTIDVYM IMVKCWMIDA
ESRPKFRELS AEFTKMARDP TRYLVIQGDD RMHLPSPVES KIHPALVEAG LGDIVDAEEY
LLPHQGFFTS PSNSRTPLLS TMSSTSNNSP VICITRNGGL PAREDSFVQR YSTDPTVILE
DSIDDEFLPA PEYVNQMVPK PVVETQTNPV YQNLSPSGNT VSPEENLYQN SHSNGLNNPE
YLNAGQTFVP KTDFDYSSIW DQKANIQINL DNPDYQQDFF PKEPKTNGHF KIPAAQNPEY
LGLAPVSDY
//
