ID A0A4W6C9G9_LATCA Unreviewed; 1105 AA.
AC A0A4W6C9G9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 08-OCT-2025, entry version 32.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=PDGFRB {ECO:0000313|Ensembl:ENSLCAP00010007109.1};
GN Synonyms=pdgfrb {ECO:0000313|RefSeq:XP_018554995.1};
OS Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010007109.1, ECO:0000313|Proteomes:UP000314980};
RN [1] {ECO:0000313|Proteomes:UP000314980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sai Rama Sridatta P.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:XP_018554995.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_018554995.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSLCAP00010007109.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2025) to UniProtKB.
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 Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
CC protein {ECO:0000256|RuleBase:RU000311}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily.
CC {ECO:0000256|RuleBase:RU000311}.
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DR RefSeq; XP_018554995.1; XM_018699479.2.
DR AlphaFoldDB; A0A4W6C9G9; -.
DR STRING; 8187.ENSLCAP00010007109; -.
DR Ensembl; ENSLCAT00010007292.1; ENSLCAP00010007109.1; ENSLCAG00010003495.1.
DR GeneID; 108899186; -.
DR KEGG; lcf:108899186; -.
DR CTD; 5159; -.
DR GeneTree; ENSGT00940000157138; -.
DR InParanoid; A0A4W6C9G9; -.
DR OrthoDB; 9936425at2759; -.
DR Proteomes; UP000314980; Unassembled WGS sequence.
DR Proteomes; UP000694890; Linkage group LG8.
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:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; IEA:TreeGrafter.
DR GO; GO:0061300; P:cerebellum vasculature development; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0072109; P:glomerular mesangium development; IEA:Ensembl.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR GO; GO:1904238; P:pericyte cell differentiation; IEA:Ensembl.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:TreeGrafter.
DR GO; GO:0097084; P:vascular associated smooth muscle cell development; IEA:Ensembl.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 1.10.510.10:FF:000140; Platelet-derived growth factor receptor beta; 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; IPR003598; Ig_sub2.
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 InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
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 PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 3: Inferred from homology;
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 ECO:0000256|RuleBase:RU000311}; 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, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000314980};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000311};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1105
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044612589"
FT TRANSMEM 524..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..118
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 210..303
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 316..400
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 592..953
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1043..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 817
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 571
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 599..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 674..680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 822
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 835
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 961
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 1105 AA; 124257 MW; A5289E7BF6A48C8E CRC64;
MRRVTVSTLH LTVTVTALLY LCTELRCLEI TPKDKEIILP RGSSLTLTCS GAGETTWEFK
REDVPFFQLE QGQNSGQSYQ IVQNGTGSSI LTLWNMSWKQ TGVYQCVDQQ TGETKEVVVF
VPDPDVWFIE SSHGMVTKTS EESTIPCVVT NPDINVTLYE KDTDMPIKGQ YIPSEGYKAQ
LEDRTYMCRG ELNGTVKESQ AFYVFSIVVP EALDAYINAS KTVLKQGEPL TVNCTVHGVE
LVFFSWDIPN REAIDVEPLT DVISSMNMRS CLMFPRATVA HSGNYICHVH EGVQDQTASA
SVNITVLERG FVDVKPAQQQ NISAKLQENV ELRVEIEAYP PPQVRWSKDG ATIKGDKTIT
SRQEHEIRYV TILTLVRVRT EQKGRYTVTV TNGDDTKEVT FDLEVQVPSQ IKDLADHHLP
GKRHLVTCIA EGVPTPTIQW YSCDSMLKCS NQTVVWQPLV PEPEELSIQT NVSYNETRKT
SQVRSQVIFY KPQQVTVRCE TSNQAGLVDR RDVKLVSSTL FSQVAVLAAV LALVVIVILS
FIILIAVWRK KPRYEIRWKV IESVSQDGHE YIYVDPIHLP YDLAWEMPRD NLVLGRTLGS
GAFGRVVEAT AYGLTHSQSS TKVAVKMLKS TARRSETQAL MSELKIMSHL GPHLNIVNLL
GACTKHGPLY LVTEYCRYGD LVDYLHRNKH TFLQYYAEKN QDDGCLISGG STPLSQRKGY
VSFGSESDGG YMDMSKDEPS VYVPMQEQID TIKYADIQPS PYESPYQQDI YQEQGGGRLD
LVISDSPILT YDDLLGFSYQ VAKGMEFLAS KNCVHRDLAA RNVLICEGKL VKICDFGLAR
DIMHDSNYIS KGSTFLPLKW MAPESIFHNL YTTLSDVWSY GILLWEIFTL GGTPYPDLPM
NELFYSALKR GYRMAKPAHA SDEVYDIMKK CWDEKFEKRP EFSFLVHSVG NMLTDSYKKR
YNQVNDNFMK SDHPAVARTK PRLSSPFPIA NPSFGSPSPI NLPFPPDPYN QSLSPGDFRQ
EAGTQEVITS YNEYIIPIPD PKPEEVFTDV PSESPASSVA LEEETDSMSQ DTADTLPEED
RLEETSERDA LLGSSGTPEV EDSFL
//
