ID A0A668AS56_9TELE Unreviewed; 1185 AA.
AC A0A668AS56;
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:ENSMMDP00005048211.1};
GN Synonyms=pdgfra {ECO:0000313|Ensembl:ENSMMDP00005048211.1};
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:ENSMMDP00005048211.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005048211.1}
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:ENSMMDP00005048211.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSMMDP00005048211.1}
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; A0A668AS56; -.
DR Ensembl; ENSMMDT00005049160.1; ENSMMDP00005048211.1; ENSMMDG00005021927.1.
DR GeneTree; ENSGT00940000156021; -.
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; 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; 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; 2.
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; 3.
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; 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 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 625..649
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 374..513
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 517..621
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 693..1068
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 856..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 916
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 672
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 699..707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT BINDING 700..707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 727
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 775..781
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 920
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 921
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 934
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 1060
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 1185 AA; 132665 MW; FD1BEBAE0D017A3A 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 GVFACMCQYT CVSSLEKSHI
ILLLSGLELK YLMPSVRENK RDQEILYTLT IPQASAKDTG IYACSITDII SNEKSAFVSL
WPEFSSQESA ELDEVKEFRA DIDSFPKARV TWLKDGLPLN DVTAEITTSL RQLNETRYQS
VLTLIRAKEE DSGNYTIRVE NGNQSHSHSF SLQVKVPAVI VDLMDLHHGS ATGQSVVCIA
GGQPTPEVEW FICKNIKHCA NDSSQWVPLP ANSTEVTVDT HIDQDNHLES QVMFGHLENT
LAVRCLARNG MAAVSREVKL VSNELTVAAA VLVLLVIVII SLIVLVVIWK QKPRYEIRWR
VIESVSPDGH EYIYVDPMQL PYDSRWEFPR DRLVLGRILG SGAFGKVVEG TAYGLSRSQP
VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL LGACTKSGPI YIITEYCFYG
DLVNYLHKNR ENFLSLHPEK NKKDLDIFGI NPADESSRSY VILSFESKGD YMDMKQADNT
QYVPMLEMSN TSKYSDIQRS NYDHPPSQKG LSDNEMDNLL SDDSNEGLST TDLLSFTYQV
ARGMEFLASK NCVHRDLAAR NVLLSQGKIV KICDFGLARD IMHDNNYVSK GSTFLPVKWM
APESIFDNLY TTLSDVWSYG ILLWEIFSLG GTPYPGMVVD SSFYNKIKSG YRMAKPEHAP
HDVYEMMMKC WNSEPEKRPS FLGLSETVAS LLPSSYKRCY ERVNHEFLKS DHPAVTRVCM
ENDDAYIGIT YKNQGKLKDR ESGFDEQRLS SDSGYIIPLP DLDPISDDEY GKRNRHSSQT
SEESAIETGS SSSTLAKREG ETLEDITLLD EMCLDSSDLV EDSFL
//
