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Database: UniProt
Entry: H2T9G3_TAKRU
LinkDB: H2T9G3_TAKRU
Original site: H2T9G3_TAKRU 
ID   H2T9G3_TAKRU            Unreviewed;      1267 AA.
AC   H2T9G3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   24-JAN-2024, entry version 69.
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=LOC101074687 {ECO:0000313|Ensembl:ENSTRUP00000021303.3};
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:ENSTRUP00000021303.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000021303.3, 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:ENSTRUP00000021303.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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; H2T9G3; -.
DR   Ensembl; ENSTRUT00000021391.3; ENSTRUP00000021303.3; ENSTRUG00000008503.3.
DR   GeneTree; ENSGT00940000154695; -.
DR   HOGENOM; CLU_003384_0_1_1; -.
DR   Proteomes; UP000005226; Chromosome 1.
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; cd12092; TM_ErbB4; 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:SF90; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-4; 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; 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; 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|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|PIRNR:PIRNR000619};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000619};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR000619}.
FT   TRANSMEM        615..638
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          681..948
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1054..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        806
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT   BINDING         687..695
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT   BINDING         714
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1267 AA;  141478 MW;  FDF48F97130ECADE CRC64;
     MMCAGTENKL STLSDLDQQY QTMRKNYENC EVVMGNLEIT SIDRSRNLTF LRSIREVTGY
     VLVALNQFDY LPLENLRIIR GTKLYEDRYA LAIFLNYRRD GNSGLRQLGL KNLTEILNGG
     VYVDRNNFLC HADTIHWQDI VKHPRIHPLV VPTNSSITCQ KCHRSCNGRC WGPKVDQCQS
     LTKTVCAEQC DGRCFGPYIS DCCHRECAGG CYGPKDTDCF ACTNFNDSGA CVTQCPQPFF
     YNSITFQLEH NVRTKYTYGA FCVKKCPHNF VVDHSSCVRA CPSNKMEVEE NGIKICIPCT
     DICPKACDGI GTASLQTAQT VDSSNIDKFV NCTKINGNLV FLITGIKGDS YHNIEALDPE
     KLNVFRTVRE ITGFLNIQSW PDNMTDLSVF SNLATIGGRT LYSGISLLVL KQQGISSLQL
     QSLREISAGN VHVADNSQLC YYNTINWTRL FRTAHQKALI RNNQSPEQCS KKRMVCDPLC
     SGAGCWGPGP DQCLSCKYFS RGRTCVDGCN LYEGEIREYA NESVCVECDG QCELADDDSL
     TCHGPGPEHC EKCLHFKDGP NCVEKCPDGL QGANSFIFKY AEANNECHPC HANCTQGCIG
     PRLQDCIGLM DRTPLIAAGV IGVLFMVVIL VLSVAVSVRR KNIKKKRALR RFLETELVEP
     LTPSGTAPNQ AQLRILKETE LKRVKVLGSG AFGTVYKGIW VPEGEKVKIP VAVKILNEAT
     GPKANVEFMD EALIMASMEH PHLVRLLGVC LSPTIQLVTQ LMPHGCLLDY VHEHKDNIGS
     QLLLNWCVQI AKGMMYLEER RLVHRDLAAR NVLVKSPNHI KITDFGLARL LDVNEKEYNA
     DGGKMAIKWM ALECIHYRKF THQSDVWSYG VTIWELMTFG GKPYDGISTR DIPDLLEKGE
     RLPQPPICTI DVYMVMVKCW MIDADSRPKF KELAAEFTRM ARDPQRYLVI QGDDCMKLPG
     PNDSKFFQSL LAEEELEDLM DAEEYLVPHS FNIPPLAYTP RTRMDSNKNQ FGYQDPSFSM
     EKMLATLPRG VSGASVSGGC LPTQDLASGV QVGGGFIRSN QDDPRCNGTL KKQASPRTDD
     SSGQRYSADP TGLLSERGAK GDQDGYMAAM RDKKISVEEN PFVTRRRNGD AHAVMDGAGC
     HTLHIAAAAA APKNQHIHGD DEYINEPLYL NTFLNPGDKN GLTASNTIMK NKKANFDNPE
     YWQHSLPPKS SLHNPEYLQD CSTRFFYRQN GRIRPAVAEN QEYLSEAAMK AGNVLPPPPY
     RQRNTVV
//
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