UniProt: A0A851CKM9

Database: UniProt
Entry: A0A851CKM9_CALVR

LinkDB:  A0A851CKM9_CALVR 
Original site:  A0A851CKM9_CALVR

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Ontology (13)   
   GO (13)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (29)   
   InterPro (15)   
   Pfam (6)   
   PROSITE (5)   
   SMART (3)   
All databases (44)   

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ID   A0A851CKM9_CALVR        Unreviewed;      1046 AA.
AC   A0A851CKM9;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   28-JAN-2026, entry version 20.
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   Name=Pdgfrb {ECO:0000313|EMBL:NWI57069.1};
GN   ORFNames=CALVIR_R03148 {ECO:0000313|EMBL:NWI57069.1};
OS   Calyptomena viridis (Lesser green broadbill).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Eurylaimidae; Calyptomena.
OX   NCBI_TaxID=135972 {ECO:0000313|EMBL:NWI57069.1, ECO:0000313|Proteomes:UP000642973};
RN   [1] {ECO:0000313|EMBL:NWI57069.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B10K-DU-002-55 {ECO:0000313|EMBL:NWI57069.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NWI57069.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (OCT-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   -!- 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}.
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:NWI57069.1}.
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DR   EMBL; WEIV01020620; NWI57069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A851CKM9; -.
DR   Proteomes; UP000642973; 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   CDD; cd00096; Ig; 1.
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; 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; 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:UP000642973};
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        531..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..114
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          201..305
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          321..406
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          414..521
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          599..962
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        825
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         578
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         606..613
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         681..687
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         829
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         830
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         843
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            969
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:NWI57069.1"
FT   NON_TER         1046
FT                   /evidence="ECO:0000313|EMBL:NWI57069.1"
SQ   SEQUENCE   1046 AA;  117946 MW;  DE2ABB02D1019584 CRC64;
     MFLPGFQRNP IRSRLPPLSG LLEVTSGGSR LHIEPTDTEI ELGLHSTFSL SCYGDRALVW
     ERDGQPLAAS LEHRDGVFVS NLTLRNVTGH HTGEYTCTYS PDQAPEPVQR KALYIYVPDP
     SLVFLPTVTS EEAFIFITGY TEAVIPCRVT NPRMQVTLYE KKVEIPIPAA YDPQQGFKGF
     FEDKTYFCRT FMDDQEVDSD PFYVYRIQVS SVNVSISAVQ TIVRQGENVT VLCTVSGNEL
     VNFNWDYPRK QAGKAVEPVT DFLPGSSHEI RSILIIQNAE LEDSGTYVCN VSEGYHEKTD
     RKDIVVQVIE HGFVHFHTHL PNTVYAEVHK SHTIQVEVEA YPQPSIVWLK NNKTLTMESS
     SEFTITSRNL SETRYQTALV LVRVKQEEGG FYTIRASNED DEQEISFHLQ INVPAKVVDL
     KENSSASSGE QTVTCSAEGM PQPEISWSTC SDIKWCSTKG HPTQLLRNES AEFGLQTNAT
     YHVERQVYRV NSTLQLHRVD EPLLLRCTVQ NFLGTSSQDI TLVPHALPFK VVIISVILAL
     LVLTVISLII LIVLWQKKPR YEIRWKVIES VSSDGHEYIY VDPMQLPYDS TWEVPRDKLV
     LGRTLGSGAF GRVVEATAHG LSHSQSTMKV AVKMLKSTAR SSEKQALMSE LKIMSHLGPH
     LNIVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL QSCGEKARRE AEVYGNTPKE
     DHVQSHLSMS VESDGGYMDM SKDDSLDYVP MSDMKGEVKY ADIESSNYGT PYELDSYSPS
     APERTDRVTL INESPLLSYM DLVGFSFQVA NGMEFLASKN CVHRDLAARN VLICEGKLVK
     ICDFGLARDI MRDSNYISKG STFLPLKWMA PESIFNNLYT TLSDVWSFGI LLWEIFTLGG
     TPYPELPMNE QFYNAIKRGY RMSKPTHASD EIYDIMQKCW EEKFEIRPSF SQLVVLMGNL
     LVDCYRKRYQ QVDEEFMKSD HPAVVRTRPT IPGLNNARLA ASSPSSSILY TAVHQNGSEN
     DYIIPLPDPK PEAICELPQE ASISRA
//

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