ID A0A668A048_9TELE Unreviewed; 1213 AA.
AC A0A668A048;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=Platelet-derived growth factor receptor alpha {ECO:0000256|ARBA:ARBA00016938, ECO:0000256|PIRNR:PIRNR500950};
DE Short=PDGF-R-alpha {ECO:0000256|PIRNR:PIRNR500950};
DE Short=PDGFR-alpha {ECO:0000256|PIRNR:PIRNR500950};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR500950};
DE AltName: Full=Alpha platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00030503, ECO:0000256|PIRNR:PIRNR500950};
DE AltName: Full=Alpha-type platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00029782, ECO:0000256|PIRNR:PIRNR500950};
GN Name=PDGFRA {ECO:0000313|Ensembl:ENSMMDP00005048210.1};
GN Synonyms=pdgfra {ECO:0000313|Ensembl:ENSMMDP00005048210.1};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005048210.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005048210.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMMDP00005048210.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSMMDP00005048210.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC for PDGFA, PDGFB and PDGFC and plays an essential role in the
CC regulation of embryonic development, cell proliferation, survival and
CC chemotaxis. Depending on the context, promotes or inhibits cell
CC proliferation and cell migration. Plays an important role in the
CC differentiation of bone marrow-derived mesenchymal stem cells. Required
CC for normal skeleton development. {ECO:0000256|PIRNR:PIRNR500950}.
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 -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Binding of PDGFA and/or PDGFB leads to dimerization
CC and activation by autophosphorylation on tyrosine residues.
CC {ECO:0000256|PIRNR:PIRNR500950}.
CC -!- SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with
CC heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound
CC ligand. {ECO:0000256|PIRNR:PIRNR500950}.
CC -!- SUBUNIT: Interacts with homodimeric pdgfa, pdgfb and pdgfc, and with
CC heterodimers formed by pdgfa and pdgfb. Monomer in the absence of bound
CC ligand. Interaction with dimeric pdgfa, pdgfb and/or pdgfc leads to
CC receptor dimerization, where both pdgfra homodimers and heterodimers
CC with pdgfrb are observed. {ECO:0000256|ARBA:ARBA00064866}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|PIRNR:PIRNR500950}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|PIRNR:PIRNR500950}.
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|PIRNR:PIRNR500950, ECO:0000256|RuleBase:RU000311}.
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DR AlphaFoldDB; A0A668A048; -.
DR FunCoup; A0A668A048; 1234.
DR Ensembl; ENSMMDT00005049159.1; ENSMMDP00005048210.1; ENSMMDG00005021927.1.
DR GeneTree; ENSGT00940000156021; -.
DR InParanoid; A0A668A048; -.
DR Proteomes; UP000472263; Chromosome 4.
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:0005018; F:platelet-derived growth factor alpha-receptor activity; IEA:InterPro.
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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:TreeGrafter.
DR FunFam; 2.60.40.10:FF:000720; Platelet-derived growth factor receptor alpha; 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 Gene3D; 2.60.40.10; Immunoglobulins; 6.
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; IPR003006; Ig/MHC_CS.
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; IPR027290; PDGFRA.
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:SF52; PLATELET-DERIVED GROWTH FACTOR RECEPTOR ALPHA; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS00290; IG_MHC; 1.
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|PIRNR:PIRNR500950};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR500950};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PIRNR:PIRNR500950};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|PIRNR:PIRNR500950};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR500950-52};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR500950};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR500950};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR500950};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR500950};
KW Reference proteome {ECO:0000313|Proteomes:UP000472263};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR500950};
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 ECO:0000256|PIRNR:PIRNR500950};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 656..680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..44
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 359..438
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 449..540
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 544..648
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 724..1096
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 887..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 944
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 703
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 730..738
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT BINDING 731..738
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 758
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 806..812
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 948
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 949
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 962
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 1088
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 185..230
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 279..320
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 366..420
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 565..632
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
SQ SEQUENCE 1213 AA; 135689 MW; 904A8EB6DBF06B7D CRC64;
MKQTLPDRVI YTLSIPHATS QDTGIYECSV THDSSGEIRA NSVAITVFEE NSFVTLDHSG
IGAVEFVSLL EETEFTILID AYPAPKVTWL KDGSRISESY YFLTKTSHLE GNRYQSILTL
RQPLEKDSGN YTITALSGSH NAQFSFTLKV KAPTTVLFPP ASAPLLLPQR EEMVVTLHTP
FTLTCRGEAE LSWETPLYLP EQTQEDNSGL FVTTITVDNA TAAHTGFYTC YYSRGNSTED
TEDSSIYIYV PDVNVPFVPS MVPFGNHVLS NHEEMEIQCR VSDPSANVTL VNADTQQPVP
SVYDSKRGAV GMFTAGTYVC KAVINGEEHY SEEYIVHGWA GGSELHVELT AQRTALLVGD
TIMVNCVARG SEILEDHWKY PGKLAERGIK SVRENKRDQE ILYTLTIPQA SAKDTGIYAC
SITDIISNES QTKELAVTVY ESAFVSLWPE FSSQESAELD EVKEFRADID SFPKARVTWL
KDGLPLNDVT AEITTSLRQL NETRYQSVLT LIRAKEEDSG NYTIRVENGN QSHSHSFSLQ
VKVPAVIVDL MDLHHGSATG QSVVCIAGGQ PTPEVEWFIC KNIKHCANDS SQWVPLPANS
TEVTVDTHID QDNHLESQVM FGHLENTLAV RCLARNGMAA VSREVKLVSN GPHPELTVAA
AVLVLLVIVI ISLIVLVVIW KQKPRYEIRW RVIESVSPDG HEYIYVDPMQ LPYDSRWEFP
RDRLVLGRIL GSGAFGKVVE GTAYGLSRSQ PVMKVAVKML KPTARSSEKQ ALMSELKIMT
HLGPHLNIVN LLGACTKSGP IYIITEYCFY GDLVNYLHKN RENFLSLHPE KNKKDLDIFG
INPADESSRS YVILSFESKG DYMDMKQADN TQYVPMLEMS NTSKYSDIQR SNYDHPPSQK
DNEMDNLLSD DSNEGLSTTD LLSFTYQVAR GMEFLASKNC VHRDLAARNV LLSQGKIVKI
CDFGLARDIM HDNNYVSKGS TFLPVKWMAP ESIFDNLYTT LSDVWSYGIL LWEIFSLGGT
PYPGMVVDSS FYNKIKSGYR MAKPEHAPHD VYEMMMKCWN SEPEKRPSFL GLSETVASLL
PSSYKRCYER VNHEFLKSDH PAVTRVCMEN DDAYIGITYK NQGKLKDRES GFDEQRLSSD
SGYIIPLPDL DPISDDEYGK RNRHSSQTSE ESAIETGSSS STLAKREGET LEDITLLDEM
CLDSSDLVED SFL
//
