ID W5LFR0_ASTMX Unreviewed; 1398 AA.
AC W5LFR0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000018672.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000018672.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. EGF receptor subfamily. {ECO:0000256|PIRNR:PIRNR000619}.
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DR STRING; 7994.ENSAMXP00000018672; -.
DR Ensembl; ENSAMXT00000018672.2; ENSAMXP00000018672.2; ENSAMXG00000018110.2.
DR eggNOG; KOG1025; Eukaryota.
DR GeneTree; ENSGT00940000156107; -.
DR HOGENOM; CLU_003384_2_1_1; -.
DR InParanoid; W5LFR0; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000018110; Expressed in intestine and 12 other cell types or tissues.
DR GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
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:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:UniProtKB-UniRule.
DR CDD; cd00064; FU; 3.
DR CDD; cd12095; TM_ErbB3; 1.
DR Gene3D; 6.10.250.2930; -; 1.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR044912; Egfr_JX_dom.
DR InterPro; IPR006211; Furin-like_Cys-rich_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; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR PANTHER; PTHR24416:SF88; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-3; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000619};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000619};
KW Membrane {ECO:0000256|PIRNR:PIRNR000619};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000619};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000619};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000619};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000619}.
FT DOMAIN 697..964
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1151..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 703..711
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT BINDING 730
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1398 AA; 155557 MW; 20508F306CDAB916 CRC64;
LVCEESALCT LQSVFCLGTT NGLSFTDSSA LHYKNLKARY ENCEIIIGNL EITLMERDFD
FSFLGGIREV TGYVLIATNQ FSRLPLGQLR VIRGSTLYDQ NWALSVFLNF DGQTGLEEMG
LTHLTEILAG GVQIVNNKFL SYVPSINWKD IVSDSSVRVE IDRNGPELAC HPDCRGHCWG
PNKDQCQTLT KTVCAPQCHG RCFGTSPRDC CNTECAGGCT GPLETHCFAC RHVNHSGACV
PHCPQPLIYN RQTFQLEPNP DAMYQYGSVC MPNCPDHFVV DGSACVSSCP LDKMEVERNG
TKRCEPCVGL CPKVCNGTGA SDRQTVDSSN IDTFINCTKI QGSLHFLVTG IHGDDYNKIP
PLDPKKLKYF STVREITGVL DIQSWPKELS DLSYFSNLTT IRGRSLRSPF SLLLMKVDSL
TSLGLRSLRE INDGSVYISN NTNLCYHHTV DWGKIFTGNR RQRRLNYNDI KFNKPQSQCE
EAGRVCDPLC SDAGCWGPGP EQCLFCRNHS RDGTCVAHCN IYSGETREFT GPNGECLACH
PECLQQEGEP TCRGKGADEC VACSNLMDGP HCVSSCPNGV NGERGQAIFK YHNSKRQCEP
CHPNCTRGCT GPTLRDCINP DRASDSPPIA AIVSGVLAGL IVCLAVAVLS LLYHRGLAIR
HKRALRRYLE SRESIEPLDP GEKGTKVHAR ILRASELRKG KLLGSGVFGT VHKSFWIPEG
DSLKIPVAIK TIQDRSGRQT FTEITDHMLS MGSLDHPYIV RLLGICPGPS LQLVTQLSTQ
GSLLQHLRQN ANSLDPQRLL NWCVQIAKGM YYLEEHCMVH RNLAARNVLL KSDYMVQISD
FGVADLLYPD DKKYVYSEHK TPIKWMALES ILFRRYSHQS DVWSYGVTVW EMMSHGAEPY
ATMHPHDVPN LLEKGERLAQ PQICTIDVYM VMVKCWMIDE NIRPTFKELA NEFTRMARDP
QRYLVVKVRK ENSAVSDESH SREFKLTEVN LESEDEEVLD DGFATPPLHL SPSRSHSRLR
IGSYRSGSGQ SVPVGYLPMT PSPGEDSRQL WYQRKRLGSA RTTSESSEGR GTVVDIEMGE
IVSQTGSLRR GHSRADSAYM SNCVSVASDP LSPVLQVAEE DTDGYVLPRS AHNSERGNEP
PQEYELMTKQ QPTVVPHLPK DRIHTTTSTS IPGKEGAGTD PLACSTNLPP YEDAIETAKQ
QEDTIERDHQ PDEEISEGNN EDGATAEERP PQQAVVEYEY MDIQTEPKPV QSSSEEERTE
RCSDETDTNS ISPCKVKRES TEDVVYQNMC DIPALKSNST KGSSFKANEH SSIITCLPEE
YEDMGVVCGR GNASADQVEY QNMPAKDRKL QGEVPHSAKL RAFRGACSGP DEKNGKTSFD
NPDYWHSRLF HKPDAVCT
//
