ID A0A091RSZ8_NESNO Unreviewed; 1040 AA.
AC A0A091RSZ8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JAN-2026, entry version 60.
DE RecName: Full=Platelet-derived growth factor receptor beta {ECO:0000256|ARBA:ARBA00020507};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=Beta platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00029696};
DE AltName: Full=Beta-type platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00032009};
DE AltName: Full=CD140 antigen-like family member B {ECO:0000256|ARBA:ARBA00075975};
DE AltName: Full=Platelet-derived growth factor receptor 1 {ECO:0000256|ARBA:ARBA00075984};
DE Flags: Fragment;
GN ORFNames=N333_13057 {ECO:0000313|EMBL:KFQ45239.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ45239.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ45239.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ45239.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with
CC heterodimers formed by PDGFA and PDGFB. May also interact with
CC homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction
CC with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
CC homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA
CC homodimers and heterodimers with PDGFRB are observed. Interacts with
CC SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB.
CC Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts
CC (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated)
CC with SRC and SRC family kinases. Interacts (tyrosine phosphorylated)
CC with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated)
CC with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by
CC SHC1. Interacts (via C-terminus) with NHERF1.
CC {ECO:0000256|ARBA:ARBA00066051}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Lysosome lumen
CC {ECO:0000256|ARBA:ARBA00004227}. Membrane
CC {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC {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 EMBL; KK931411; KFQ45239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RSZ8; -.
DR Proteomes; UP000053840; Unassembled WGS sequence.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
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:TreeGrafter.
DR GO; GO:0060326; P:cell chemotaxis; IEA:TreeGrafter.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IEA:UniProtKB-ARBA.
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:000140; Platelet-derived growth factor receptor beta; 1.
DR FunFam; 2.60.40.10:FF:000223; Platelet-derived growth factor receptor beta; 1.
DR FunFam; 2.60.40.10:FF:000572; Platelet-derived growth factor receptor beta; 1.
DR FunFam; 2.60.40.10:FF:000715; Platelet-derived growth factor receptor beta; 1.
DR FunFam; 2.60.40.10:FF:000982; 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; IPR013151; Immunoglobulin_dom.
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; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 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; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 4.
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 Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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 Lysosome {ECO:0000256|ARBA:ARBA00023228};
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:UP000053840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 TRANSMEM 493..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..76
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 172..267
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 283..368
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 376..483
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 561..924
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1013..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 787
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 568..575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 643..649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 791
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 792
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 805
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 931
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ45239.1"
FT NON_TER 1040
FT /evidence="ECO:0000313|EMBL:KFQ45239.1"
SQ SEQUENCE 1040 AA; 117425 MW; D696847A23FBE251 CRC64;
ELVLSLHSTF SLLCYGDGAL VWEREGQPLT ASLEHRDSVF ISNLTLRNVT GRHTGEYTCT
YSPEQAPEPA ERKAIYIYVP DPSLVFLPTM TSEELFIFIT GYTEAIIPCR VTNPQMQVIL
YEKKVENPIP AVYDPQQGFR GFFEDKTYFC RTIVDDQEVD SDTFYVYRIQ VSSVNVSISA
VQTIVRQGEN ITLMCTVSGN ELVNFNWDYP RKQAGKTVEP VTDFLPGSTH EIRSILIIQN
AELEDSGTYV CNVSEGYHEK TDRKDISVHV IERGFVRFHT RLPSTMYAEV HKSHTIQVEV
EAYPPPSIMW LKNNKTLTME SSSEFTITSR NLSETRYQTG LVLVRVKQEE GGFYTIRASN
EDDEQELSFH LQINVPAKVV DLKENSSASS GEQTVTCSAE GMPQPEISWS TCSDIKRCST
KGQPTRLLGN ESAEIGLWTN ATYHAELQVY RVNSTLQLHR VDEPLLLRCT VHNFLGTSSQ
DITLVPHALP FKVVIISVIL ALLVLTVISL IILIVLWQKK PRYEIRWKVI ESVSSDGHEY
IYVDPMQLPY DSSWEVPRDK LVLGRTLGSG AFGRVVEATA HGLSHSQSTM KVAVKMLKST
ARSSEKQALM SELKIMSHLG PHLNIVNLLG ACTKGGPIYI ITEYCRYGDL VDYLHRNKHT
FLQCYGEKAR REAELYGNTP KEDHVQSHLS LSVESDGGYM DMSKDDSLDY VPMSDMKAEV
KYADIESSNY GTPYELDSYS PSAPERTDRV TLINESPLLS YMDLVGFSFQ VANGMEFLAS
KNCVHRDLAA RNVLICEGKL VKICDFGLAR DIMRDSNYIS KGSTFLPLKW MAPESIFNNL
YTTLSDVWSF GILLWEIFTL GGTPYPELPM NEQFYNAIKR GYRMSKPTHA SDEIYDIMQK
CWEEKFEIRP SFSQLVVLMG NLLVDCYRKR YQQVDEEFMK SDHPAVVRTR PTIPRLNNAR
ITASSPPGSI LYTSVHQNGG ENDYIIPLPD PKPEAICDLP QEASISRASS MLNEANTSST
ISCDSPLGLQ QNEEQESDPQ
//
