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Database: UniProt
Entry: H2TYZ8_TAKRU
LinkDB: H2TYZ8_TAKRU
Original site: H2TYZ8_TAKRU 
ID   H2TYZ8_TAKRU            Unreviewed;      1180 AA.
AC   H2TYZ8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 71.
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};
GN   Name=egfr {ECO:0000313|Ensembl:ENSTRUP00000029907.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000029907.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000029907.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000029907.3}
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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane 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   AlphaFoldDB; H2TYZ8; -.
DR   STRING; 31033.ENSTRUP00000067832; -.
DR   Ensembl; ENSTRUT00000030024.3; ENSTRUP00000029907.3; ENSTRUG00000011834.3.
DR   GeneTree; ENSGT00940000155450; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000005226; Chromosome 22.
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:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR   CDD; cd00064; FU; 3.
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; 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; IPR049328; TM_ErbB1.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   PANTHER; PTHR24416:SF91; EPIDERMAL GROWTH FACTOR RECEPTOR; 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   Pfam; PF21314; TM_ErbB1; 1.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 2.
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; 2.
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   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, ECO:0000256|SAM:Phobius};
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:UP000005226};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000619};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR000619}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1180
FT                   /note="Receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030172380"
FT   TRANSMEM        642..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          709..976
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        834
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT   BINDING         715..723
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT   BINDING         742
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1180 AA;  130660 MW;  1ABC6478A568877C CRC64;
     MAARFVTGFG LTSLLCLCCC VLAERKVCQG ITNRLNLLGS REDHYANMLK TYSNCTVVLE
     NLEITYMEED RDLSFLRSIE EVGGYVLIAL NTVSKIRLDN LRIIRGHSLY EKKFALSVIA
     NFNKSTGQGT SELLLNSLTE ILKGGIKISG KVLCNVETIQ WYDIVNVETK PVMELPVASN
     NPQCQKCDSS CFNGSCWAPG PQNCQTLTKL NCAQQCSKRC KGTSPIDCCN EHCAAGCTGP
     RPTDCLACRD FQDDGVCKDS CPGLMRYDPN LHQLVPNPHG KYNFGATCVK TCPHNYVVTD
     HGACVRTCSG NTYEVDEGGM RKCAKCEGLC PKVCNGLGTG ELTNAMSINA TNIESFRNCT
     KINGNIAIIR TSIHGDAYTK TPKMHPSQLD VFKTVKEITG YLLIQTWPDN ISSLSPFENL
     EIIRGRTKRG SRSLMVANLG ITSLGLRSLK EISDGDVIIM KNKNLCYTSK SHWKKLFKSD
     SQHPTIDENA DAATCAQRNN SCDRKCTAEG CWGSGPDMCF ACSNYSRGGS CVDSCNILEG
     ELREAVVDKT CVECHPECER MNGTATCIAP GSGNCTRCAN SQDGLFCVSR CPQGVPGEDE
     TLVWKYADNN KVCQLCHKNC TQGCTGPGLA GCQNKSTSGF SMIAAGVVGG LLAALIAGLS
     VFVLLRRRHI KRKRTMRRLL QERELVEPLT PSGEAPNQAL LRILKEPEFK KIKVLGSGAF
     GTVYKGLWVP EGEDVKIPVA IKVLREATSP KANKEILDEA YVMASVEHPH VCRLLGICLT
     STVQLITQLM PYGCLLDYVK ENRDNIGSQY LLNWCVQIAK GMNYLEERHL VHRDLAARNV
     LVKTPQHVKI TDFGLAKLLN ADEKEYHADG GKVPIKWMAL ESILNRTYTH QSDVWSYGVT
     VWELMTFGTK PYDGIPASEI AGILEKGERL PQPPICTIDV YMIMVKCWMI DADSRPRFRE
     LIAEFTKMAR DPSRYLVIQG DERMPLPSPT ENKLFRTLIS EEYMEDAIDA DEYLVPQHGF
     FSSPSTSHTP LLQSTNGFPS RDGSFVHRYI PDPTDKLLDD AFQPAPDYMN QNGVSDVMNP
     NYKYPGPPRS VLPTISSDDT ESEYLNCFKN GTIEPEYLNE VPSSSGFPFT PNNVVQNMQK
     YAPQNSIDNP DYQQDFTPTF KTHTNGHIPA AENTEYLGPD
//
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