ID A0A8C4SHZ0_ERPCA Unreviewed; 1043 AA.
AC A0A8C4SHZ0;
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};
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};
GN Name=PDGFRA {ECO:0000313|Ensembl:ENSECRP00000016741.1};
GN Synonyms=pdgfra {ECO:0000313|Ensembl:ENSECRP00000016741.1};
OS Erpetoichthys calabaricus (Rope fish) (Calamoichthys calabaricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Polypteriformes; Polypteridae; Erpetoichthys.
OX NCBI_TaxID=27687 {ECO:0000313|Ensembl:ENSECRP00000016741.1, ECO:0000313|Proteomes:UP000694620};
RN [1] {ECO:0000313|Ensembl:ENSECRP00000016741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSECRP00000016741.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSECRP00000016741.1}
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. {ECO:0000256|ARBA:ARBA00064866}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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|RuleBase:RU000311}.
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DR AlphaFoldDB; A0A8C4SHZ0; -.
DR Ensembl; ENSECRT00000017040.1; ENSECRP00000016741.1; ENSECRG00000010949.1.
DR GeneTree; ENSGT00940000156021; -.
DR Proteomes; UP000694620; Chromosome 5.
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: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; 4.
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; 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; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF21339; VEGFR-1-like_Ig-like; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 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|PIRSR:PIRSR000615-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 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:UP000694620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 481..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..367
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 549..926
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 956..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1043
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 774
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 556..563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 631..637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 778
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 779
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 792
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 918
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 1043 AA; 117839 MW; 7060333D7D071F9D CRC64;
MPSQSVLQQI YIRQMYFYCV LLGPQSPVLL QAPPMIYPPG EELVIPLHSS FKLTCSGESE
VEWDAEDKDN FTLKEEQDNS GLFVISLAVQ NASASHTGYY TCLYPSMNGS GYESIIYIYV
PDPNVTFLPH VSPFSQHVLG AYEDTEIPCR VSDPEVHVAL INAYTNMEVV DSLYDSKRGF
IGVFPEGTYF CEATVDGVQH QSVEYIVHGW RETSELKVDL QVDNIVVMEG EPITITCVAR
GSEMLEDFWK YPGKQVRNIN LAVDHNKGFA RLESTFDQQE FADLHEVKEF KVLIEAYPFP
AVTWLKDSMV LSDENTEITR QVTHSLVLFC RYQSSLLLIR AKEEDSGNYT IQVKSGNESS
SYTFSLQVKA VIVELMDLHH GSASGQSVVC IAGGLPTPDV EWFICKNIKH CANDTSQWMV
LPVNSTDVST ETHLTDESKV ESQVTFAKLE HTLAVKCSAK NELAAVAREV KLVSPSLRSE
LTVAAAVLVL LVIVIICLIV LVIIWKQKPR YEIRWRVIES ISPDGHEYIY VDPMQLPYDS
RWEFPRDGLV LGRVLGSGAF GKVVEGTAYG LSRSQPVMKV AVKMLKPTAR SSEKQALMSE
LKIMTHLGPH LNIVNLLGAC TKSGPIYIIT EYCFYGDLVN YLHKNREAFL NRHPEKVKKD
LDIFGINPAD ESTRSYVILS FENKGDYMDM KQADATQYVP MLEMKESSKY SDIQRSNYDH
PPSHKHKSLT ETEVNNLLSD DNSEGLTLMD LLSFTYQVAR GMEFLASKNC VHRDLAARNV
LLSQGKIVKI CDFGLARDIM HDNNYVSKGS TFLPVKWMAP ESIFDNLYTT LSDVWSYGIL
LWEIFSLGGT PYPGMVVDSS FYNKIKSGYR MTKPEHATTD IYEMMMKCWN SEPEKRPSFK
CLRDTLESLL PDEYRKSYEK INHDFLKSDH PAVTRTQSHS DDAYIGVTYK NENKLKDRES
GFDEQRLSSD SGYIIPLPDL DPLSDDEYGK RNRHSSQTSE ESAIETGSSS STFIKREDET
IEDIDMMDDI GIDSSDLAED SFL
//
