ID A0A671DYR7_RHIFE Unreviewed; 1019 AA.
AC A0A671DYR7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=Platelet-derived growth factor receptor alpha {ECO:0000256|ARBA:ARBA00016938};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=Alpha platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00030503};
DE AltName: Full=Alpha-type platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00029782};
DE AltName: Full=CD140 antigen-like family member A {ECO:0000256|ARBA:ARBA00075973};
DE AltName: Full=Platelet-derived growth factor alpha receptor {ECO:0000256|ARBA:ARBA00080714};
GN Name=PDGFRA {ECO:0000313|Ensembl:ENSRFEP00010006010.1};
OS Rhinolophus ferrumequinum (Greater horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Rhinolophoidea;
OC Rhinolophidae; Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479 {ECO:0000313|Ensembl:ENSRFEP00010006010.1, ECO:0000313|Proteomes:UP000472240};
RN [1] {ECO:0000313|Ensembl:ENSRFEP00010006010.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25689317; DOI=10.1146/annurev-animal-090414-014900;
RA Koepfli K.P., Paten B., O'Brien S.J., Koepfli K.P., Paten B., Antunes A.,
RA Belov K., Bustamante C., Castoe T.A., Clawson H., Crawford A.J.,
RA Diekhans M., Distel D., Durbin R., Earl D., Fujita M.K., Gamble T.,
RA Georges A., Gemmell N., Gilbert M.T., Graves J.M., Green R.E., Hickey G.,
RA Jarvis E.D., Johnson W., Komissarov A., Korf I., Kuhn R., Larkin D.M.,
RA Lewin H., Lopez J.V., Ma J., Marques-Bonet T., Miller W., Murphy R.,
RA Pevzner P., Shapiro B., Steiner C., Tamazian G., Venkatesh B., Wang J.,
RA Wayne R., Wiley E., Yang H., Zhang G., Haussler D., Ryder O., O'Brien S.J.;
RT "The Genome 10K Project: a way forward.";
RL Annu Rev Anim Biosci 3:57-111(2015).
RN [2] {ECO:0000313|Ensembl:ENSRFEP00010006010.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=29166127; DOI=10.1146/annurev-animal-022516-022811;
RA Teeling E.C., Vernes S.C., Davalos L.M., Ray D.A., Gilbert M.T.P.,
RA Myers E.;
RT "Bat Biology, Genomes, and the Bat1K Project: To Generate Chromosome-Level
RT Genomes for All Living Bat Species.";
RL Annu Rev Anim Biosci 6:23-46(2018).
RN [3] {ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Teeling E., Myers G., Vernes S., Pippel M., Winkler S., Fedrigo O.,
RA Rhie A., Koren S., Phillippy A., Lewin H., Damas J., Howe K.,
RA Mountcastle J., Jarvis E.D.;
RT "G10K-VGP greater horseshoe bat female genome, primary haplotype.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSRFEP00010006010.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [5] {ECO:0000313|Ensembl:ENSRFEP00010006010.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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 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. Interacts (tyrosine phosphorylated) with SHB
CC (via SH2 domain). Interacts (tyrosine phosphorylated) with SHF (via SH2
CC domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain).
CC Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine
CC phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine
CC phosphorylated) with CRK, GRB2 and GRB7. Interacts with CD248; this
CC interaction promotes PDGF receptor signaling pathway.
CC {ECO:0000256|ARBA:ARBA00062037}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Golgi
CC apparatus {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|RuleBase:RU000311}.
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DR AlphaFoldDB; A0A671DYR7; -.
DR Ensembl; ENSRFET00010006590.1; ENSRFEP00010006010.1; ENSRFEG00010004089.1.
DR GeneTree; ENSGT00940000156021; -.
DR Proteomes; UP000472240; Chromosome 5.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IEA:TreeGrafter.
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 CDD; cd05861; IgI_PDGFR-alphabeta; 1.
DR CDD; cd05105; PTKc_PDGFR_alpha; 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; 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; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
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|PIRSR:PIRSR000615-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000472240};
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 538..562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..126
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 215..319
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 606..967
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 831
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 585
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 613..620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 640
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 688..694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 835
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 836
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1019 AA; 115189 MW; 1E7F92C2FAE1CEA3 CRC64;
MTRNGETWFQ FSRAMGTSRL ALLVLGCLLA GPSLILCQLS LPSILPNENE KVVQLNSSFS
LRCFGESEVS WQYPMPDENL NVEIRNEENN SGFFVTVLEV VNASAAHTGL YTCYYNHTQT
EENEIEGRRI YIYVPDPDVA FVPLGMTDYL VIVEDDDSAI IPCRTTDPDT PVTLLSSDGV
VFASYDSRQG FNGTFTVGPY ICEATVRGKK FQTIPFNVYA LKATSELDLE MEAPQTVYKS
GETIAVTCAV FNNEVVDLQW TYPGEVKGKG ITMLEEIKVP SIKLVYTLMV PEATVKDSGD
YECAARQATK EVKEMKKVTI SVHEKGFIEI KPNFNQLEAV NLHEVKHFVV DVQAYPPPRI
SWLKDNLTLI ENLTEITTDI EKIQEIRYRS KLKLIRAKEE DSGHYTIVVQ NEDDVKSYTF
ELLTQVPSSI LDLVDDHHGS TGGQTVRCTA EGTPLPDIEW MICKDIKKCN NETSWTVLAN
NISNIITEVH PRDRSTVEGR VTFAKVEETI AVRCLAKNLL GAENRELKLV APTLRSELTV
AAAVLVLLVI VIISLIVLVV IWKQKPRYEI RWRVIESISP DGHEYIYVDP MQLPYDSRWE
FPRDGLVLGR ILGSGAFGKV VEGTAYGLSR SQPVMKVAVK MLKPTARSSE KQALMSELKI
MTHLGPHLNI VNLLGACTKS GPIYIITEYC FYGDLVNYLH KNRDSFLSRH PEKPKKELDI
FGLNPTDEST RSYVILSFEN NGDYMDMKQA DTTQYVPMLE RKEVSKYSDI QRSLYDRPAS
YKKKSMLDSE VKNLLSDDNS EGLTLLDLLS FTYQVARGME FLASKNCVHR DLAARNVLLA
QGKIVKICDF GLARDIMHDS NYVSKGSTFL PVKWMAPESI FDNLYTTLSD VWSYGILLWE
IFSLGGTPYP GMMVDSTFYN KIKSGYRMAK PDHATSEVYE IMVKCWNSEP EKRPSFYHLS
EIVENLLPGQ YKKEHFKGGK RLCDPVARLH GVLPRPWEQW WMITLPFPEG SLSSSAYDT
//
