ID A0A8C3ILV8_CHRPI Unreviewed; 1086 AA.
AC A0A8C3ILV8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
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:ENSCPBP00000036001.1};
OS Chrysemys picta bellii (Western painted turtle) (Emys bellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Emydidae; Chrysemys.
OX NCBI_TaxID=8478 {ECO:0000313|Ensembl:ENSCPBP00000036001.1, ECO:0000313|Proteomes:UP000694380};
RN [1] {ECO:0000313|Ensembl:ENSCPBP00000036001.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26108489; DOI=10.1093/gbe/evv119;
RA Badenhorst D., Hillier L.W., Literman R., Montiel E.E., Radhakrishnan S.,
RA Shen Y., Minx P., Janes D.E., Warren W.C., Edwards S.V., Valenzuela N.;
RT "Physical Mapping and Refinement of the Painted Turtle Genome (Chrysemys
RT picta) Inform Amniote Genome Evolution and Challenge Turtle-Bird
RT Chromosomal Conservation.";
RL Genome Biol. Evol. 7:2038-2050(2015).
RN [2] {ECO:0000313|Ensembl:ENSCPBP00000036001.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCPBP00000036001.1}
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 -!- 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}. Cell
CC projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. 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|PIRNR:PIRNR500950, ECO:0000256|RuleBase:RU000311}.
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DR RefSeq; XP_005299163.1; XM_005299106.5.
DR AlphaFoldDB; A0A8C3ILV8; -.
DR Ensembl; ENSCPBT00000042218.1; ENSCPBP00000036001.1; ENSCPBG00000025039.1.
DR GeneID; 101935558; -.
DR CTD; 5156; -.
DR GeneTree; ENSGT00940000156021; -.
DR OrthoDB; 9936425at2759; -.
DR Proteomes; UP000694380; Chromosome 4.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; 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: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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:TreeGrafter.
DR CDD; cd05859; Ig4_PDGFR; 1.
DR FunFam; 2.60.40.10:FF:000720; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 2.60.40.10:FF:000725; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 2.60.40.10:FF:000776; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 2.60.40.10:FF:000832; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 2.60.40.10:FF:000223; Platelet-derived growth factor receptor beta; 1.
DR FunFam; 1.10.510.10:FF:001735; T0011027 isoform 1; 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; 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; 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; 4.
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; 2.
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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR500950};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR500950};
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:UP000694380};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1086
FT /note="Platelet-derived growth factor receptor alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5043758846"
FT TRANSMEM 524..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1016..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1086 AA; 122538 MW; 8E3FA8D97DFF8A10 CRC64;
MGTSPRTFLL LGCLLTGPWL TFCQLPLPTV LPNRDEMVVQ LNASFTLKCS GDSEVTWQYP
MAEGSHRIDI RNEENNSGLF VTLLEVGNAS AAHTGLYTCY YNHTQEEDGE VEGKDIYIYV
PDPDIPFVPL LPEDQFILVE DGDSTIIPCR TSDPNAQVAL VNSEAKVVYA YYDSKQGFLG
NFPAGSYTCQ TTVKEVEFKS DQFFIYILKA TSELPVEIEA LKTVYKTGET IVVTCVVFDN
EVVNLQWNYP GKVKEKGVIK VDDIKVPSQK LVYTLTIPEA SVKDTGDYEC TARHATKEVK
ENKRVVITVH DKGFIHLDPQ FSPLEAVNLH EVKNFVVDVQ AYPAPKMFWL KDNVTLTENL
TEIVTSANKI NETRVQSILK LIRAKEEDSG DYTLVAENGE ETKSYTFSLL IQVSASILKL
VDHHGSGGGQ TVQCLAKGTP FPDVEWLICK DIKKCSNDTS WILLTNNISN IHMEAYRVDK
DQVKSQVTFQ KVEETLVVRC MARNTLGAVT RELKLVAPTL RSELTVAAAV LVLIVIVIIS
LIVLVIIWKQ KPKYEIRWRV IESISPDGHE YIYVDPMQLP YDSRWEFPRD GLVLGRILGS
GAFGKVVEGT AYGLSRSQPV MKVAVKMLKP TARSSEKQAL MSELKIMTHL GPHLNIVNLL
GACTKSGPIY IITEYCFYGD LVNYLHKNRD NFLSQHPEKP KKDLDIFGMN PADESTRSYV
ILSFENNGEY MDMKQADTTQ YVPMLERKEG SKYSDIQRSM YDRPASYKKK SVSEPEVKNL
LSDDNSDSLS LLDLLSFMYQ VARGMEFLAS KNCVHRDLAA RNVLLAQGKI VKICDFGLAR
DIMHDSNYVS KGSTFLPVKW MAPESIFDNL YTTLSDVWSY GILLWEIFSL GGTPYPGMMV
DSSFYNKIKS GYRMAKPDHA TSEVYEIMVK CWNSEPEKRP SFYHLSEIVE NLLPGEYKKS
YERIHLDFLK SDHPAVTRMR VDCDNTYIGV TYKNEDKLKD RESGFDEQRL SADSGYIIPL
PDIDPVSEDE LGKRNRHSSQ TSEESAIETG SSSSTFIKRE DETIEDIDMM DDIGIDSSDL
VEDSFL
//
