ID A0A4Z2C4K9_9TELE Unreviewed; 1078 AA.
AC A0A4Z2C4K9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=fugu_013310 {ECO:0000313|EMBL:TNM98746.1};
OS Takifugu bimaculatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=433685 {ECO:0000313|EMBL:TNM98746.1, ECO:0000313|Proteomes:UP000516260};
RN [1] {ECO:0000313|EMBL:TNM98746.1, ECO:0000313|Proteomes:UP000516260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TB-2018 {ECO:0000313|EMBL:TNM98746.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TNM98746.1};
RA Xu P., Liu B., Zhou Z.;
RT "The sequence and de novo assembly of Takifugu bimaculatus genome using
RT PacBio and Hi-C technologies.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00051243};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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:TNM98746.1}.
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DR EMBL; SWLE01000006; TNM98746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z2C4K9; -.
DR Proteomes; UP000516260; Chromosome 14.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; IEA:TreeGrafter.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:TreeGrafter.
DR GO; GO:0001667; P:ameboidal-type cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0001525; P:angiogenesis; IEA:TreeGrafter.
DR GO; GO:0060326; P:cell chemotaxis; IEA:TreeGrafter.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:TreeGrafter.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 1.10.510.10:FF:001927; Receptor protein-tyrosine kinase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR050122; RTK.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF53; PLATELET-DERIVED GROWTH FACTOR RECEPTOR BETA; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000615-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000516260};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 541..565
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..136
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 239..332
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 609..929
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1014..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1034
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 616..623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 691..697
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT SITE 937
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 1078 AA; 120818 MW; 2F3F8389B71ED001 CRC64;
MFRRLGREVH RLLPPVDLCL SFLAGSSMLR ASAMRAAVLH LTVALAALLS SCTTVSCLKI
VPEETQLILA EGSSLSLTCA GSSETTWDLK SDDVPFFQMK AESSGLNYKI VQSNSTASVL
TLWHVDWKNT GVYQCREQLT GEIKEVAVFV PDPEVWFIES SHGMVTKTSG ESTVPCVVTN
PNITVTLYDK DTDLPVNGVY VPSEGFKAYL DYRTYVCRGE LNGEVKESQA FNVYSIHVPE
DIDAYVNASQ TVLKQGEPLT VNCTVQGVEL VLFSWDIPNR DIVKHKPETV VLSATTMRSC
LVFPHATVAH SGTYVCHAHE STQDQKAFAS VNITVLERGF VAVKSTQKQN ITAELQENVE
LRVEIEAYPP PQIRWKKDGA PVRGDKTIII RQEHEIRYVT ILTLVRALIT NEDDVKEVTF
ALEVQVLARI KDLTDHHLPG KKQLVTCVAE GVPTPTIQWY SCDSMLKCNN QTSLWQQLKA
DPELLSIHTS VTEARRTNQV QSQVTFFKPQ HTTVRCETTN QEGLIDFRDV KLVSSSLFSQ
VVLLAVVLTL VPIIIMSIII LIAVWKKKPR YEIRWKVIES VSQDGHEYIY VDPIHLPYDL
AWEMPRDNLV LGRTLGSGAF GRVVEATAHG LSHSQSSIKV AVKMLKATAR RSETQALMSE
LKIMSHLGPH LNIVNLLAAC TKHGPLYLVT EYCRYGDLVD YLHRNKHTFL QYYLDKNQDD
GSLISGGSTP LSQRKGYVSF GSESDGGYMD MSKDEPAVYV PMQEQTDTIK YADIQPSPYE
SPYQQDLYQE QGGGRVDLVI SDSPALTYDD LLGFSYQVAK GMEFLASKNT FLPLKWMAPE
SIFHNLYTTL SDVWSYGILL WEIFTLGGTP YPDLPMNELF YSALKRGYRM AKPAHASDEV
YEIMKRCWDE TFEKRPDFSF LVHCVGDMLT DSYKKKYSQV NETFLKSDHP AVARTKPRLS
SPFPIANPAF GSPSLVGLSD FPDPYNQNTR HFRNEAEVQE GVTSFNEYII PIPDPKPEEA
FTDVPSESPE SSLALEEETD SVHDSTDTLP EEDRLEETSE RDALLGSSGT PEVEDSFL
//
