ID A0A401RWL5_CHIPU Unreviewed; 1215 AA.
AC A0A401RWL5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=chiPu_0000938 {ECO:0000313|EMBL:GCC22550.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC22550.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC22550.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC22550.1}.
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DR EMBL; BEZZ01000013; GCC22550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RWL5; -.
DR STRING; 137246.A0A401RWL5; -.
DR OMA; KDRYTNC; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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 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:UP000287033};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1215
FT /note="Receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019021864"
FT TRANSMEM 642..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 708..975
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1024..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 833
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT BINDING 714..722
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT BINDING 741
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1215 AA; 136739 MW; 5CC420AA943098D6 CRC64;
MLCSLLPGAV HLLILLSLGS ESLSREVCSG IENKLNLLAT EDNHYNSLRR TYSGCEVVMG
NLEITFVQPH HDVSFLKSIQ EVSGYVLIGL NKISTIPLEN LRIIRGHQLY EDKYALVILS
NNDQEKKFGL TELPLRNLTE ILSGSVNIIS NPYLCYVQSI QWDDILDKSM VSEMAINFTA
KNCSKCHPDC QDGACWGPGL ENCQKFTKKI CAQQCSGRCR GKNPSDCCHT QCAAGCTGPR
EYDCLACQRF RDGDTCKESC PRLEIYDTRT YQLKPNPDGK YSFGATCVKK CPHNYVVTDL
GSCVRTCSPR TYEVDEGDQR KCKKCDGPCP KDCNGLGTPA FKGAISINSS NIDSFKNCTK
INGNVIFLSV AFKGDSFTNT TPMPPEKLEV FRTVKEITGY LFIQNWPDKY KNLQVFENLE
IIRGRTQHRS SISLALVNLN ITSLGLRSLK EISDGQVSIF NNSKLCYVET IQWEKLFKSN
RQSLKITPNK PKTQCIAENK ICHPLCSDDG CWGPGPSQCF SCRHYERGRE CVAKCNIYEG
ELREYEDQRR CIQCDAECKP QNGSLTCTSF GNENCVECAH VKDGPRCVSS CPSGISGENN
TLVWKYTDEN KHCQLCHPNC TQECKGPRLE DCEPVGSRIP SIAAGIVSGL LGLVVVALLI
AICMRRRHVR KKRTLRRLLQ ERELVEPLTP SGAAPNQALL RILKETEFKK IKVLGSGAFG
TVYKGLWNPE GENVKIPVAI KVLREATSPK ANKEILDEAY VMASVDHPHV CRLLGICLTS
TVQLVTQLMP FGCLLDYMRE NKEHIGSQYL LNWCVQIAKG MSYLEERRLV HRDLAARNVL
VKTPHHIKIT DFGLARLLDV DEKEYHEDGG KLPIKWMALE SILQRTFTHQ SDIWSYGVTV
WELMTFGSKP YDGIPACEIP SILEKGERLP QPPICTIDVY MIMVKCWMID AESRPRFREL
TSEFSRMARD PSRYLVIQGD DHMHLPSPTN SRFYRTIMEE EEMEDIVDAD DYLVPHPGFF
NSPSTSRTPL CPSVSQTSNN SSTLIPRNGH QGMPKREDSE ILRYSSDPTM PPDHIDINGC
FQPAPEYVNQ IRDKPLPSTV RSPASDMENP GYQELFIPLN QNGRLHNSSE PADTDTVKNP
EYVNAFQPSN KVVLEHPNHW DQNITRNISL DNPEYQQNLF PKHTKVNGHI FNTATENPEY
LGIAVPPTGQ KNSTV
//
