ID H2SCZ8_TAKRU Unreviewed; 1300 AA.
AC H2SCZ8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|PIRNR:PIRNR000619};
DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000619};
GN Name=LOC101074842 {ECO:0000313|Ensembl:ENSTRUP00000010278.2};
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:ENSTRUP00000010278.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000010278.2, 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:ENSTRUP00000010278.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: In the nucleus is involved in transcriptional regulation.
CC Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter
CC and activates its transcription. Implicated in transcriptional
CC activation of CDKN1A; the function involves STAT3 and SRC. Involved in
CC the transcription of rRNA genes by RNA Pol I and enhances protein
CC synthesis and cell growth. {ECO:0000256|ARBA:ARBA00037619}.
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 projection, ruffle membrane
CC {ECO:0000256|ARBA:ARBA00004199}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004199}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {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 RefSeq; XP_003961433.1; XM_003961384.2.
DR STRING; 31033.ENSTRUP00000010278; -.
DR Ensembl; ENSTRUT00000010336.3; ENSTRUP00000010278.2; ENSTRUG00000004330.3.
DR GeneID; 101074842; -.
DR KEGG; tru:101074842; -.
DR GeneTree; ENSGT00940000158232; -.
DR InParanoid; H2SCZ8; -.
DR OMA; YVSDRHC; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000005226; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
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 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:SF137; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2; 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; 3.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1300
FT /note="Receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017332552"
FT TRANSMEM 649..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 715..974
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1025..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 840
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT BINDING 721..729
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT BINDING 748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1300 AA; 143722 MW; C58EFEE5B94254F9 CRC64;
MEAARSLVFV GAVLLGAAGA LDREACMGTD MKLSLPSSLE NHYEMLRLLY TGCQVVHGNL
EITHLHGNPD LSFLQGIVEV QGYVLVARVS VSLVPLDNLR IIRGSQLYNS SYALAALDNT
LDGQGLRTLA LRSLTEILFG GVYIWGNPQL CFPDPQSINW RDILDELNTD TRYRLQPRAL
NCPNCSSQCL TSCWGETVQD CQTLTHSNCA LGCQRCKGSL TNDCCHKQCS AGCTGPKDSD
CLACRHFNDS GVCKENCPPP TIYDPTMFQS KPNPDRKFSF GATCVKTCPY NYLAMDVACT
LNYPKPNQEV IITQPCGNDT QKCEKCEGDC PKACYGPGMD NSGVMDSHGN TMVNSSNVEQ
FNKCTKIFGS LAFYPQSFTR DPVTNASGLS PQQLSVFRNL EEITGYLYIE AWPQEWMNLS
VFDNLKVIRG RMLYKGVFSL AIQHLQITSL GLRSLRSISG GLVLLHNNSQ LCYTSSLPWE
NIVHPTQGPH RIVSKNQDPQ ICEKQGRVCH PLCEGGCWGP GPSQCASCRT FQRGSECVEQ
CDIYQGSVRE YANESVCVAC HPECQPLNSS ASCHGPGAEH CAECRNFQDG DVCVAHCPSG
AKEDHQTVWK YSNATGHCLP CNTNCTLSCT VMDERGCPVD TRTGLGTTIA AAVGGVVLFF
ILLGLLFFYL RRQKKLKRKE TMRRILQEHE LVEPLAPSGA SPNQAQMRIL KETELKKLKV
LGAGAFGTVY KGVWAPDGEN VKIPVAIKVL RENTSPKANK EILDEAYVMA GVASPYVCRL
LGICLTSTVQ LVTQLMSYGC LLEYVRKNKD RIGSQLLLNW CVQIAKGMSY LEEVRLVHRD
LAARNVLVKN PNHVKITDFG LARLLDIDET EYHADGGKVP IKWMALESIL HRRFTHQSDV
WSYGVTVWEL MTFGAKPYDM IPAREIPEVL EGGERLPQPL ICTIDVYMIM VKCWMIDPEY
RPRFKDLVKE FTAMARDPPR YVVIQNEEQM SMSSPVDNQF FRMFLAEEGN NLRELLDAEE
YLVPQPNHFP RTHNNGIQSN GPSRHQSYRS RDQGLDVEPS GAGGPRSLYS SLSTLGPSQY
PTLPLGASTA SGMWSPPYPT LARSPSAGDQ SDSVFLESPE DPSLPPGSPD RYCRDPTYSN
DSQGDLETDG PSGFQPTHHL HHSLPRQSHG CNQNRILPEY VNQEIQDRRP GILERPTTLP
RNGSRVDRRI ANGLSSGHSV ENTGYLVPAG TRTPTSPAFD NPYYLDHLVK AKTGDGASGV
NDPEGLETDG VMPRHMNGFV TPTAENPEYL GLADTLSGHT
//
