ID A0A484D064_PERFV Unreviewed; 1467 AA.
AC A0A484D064;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 31.
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 ORFNames=EPR50_G00094600 {ECO:0000313|EMBL:TDH08167.1};
OS Perca flavescens (American yellow perch) (Morone flavescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8167 {ECO:0000313|EMBL:TDH08167.1, ECO:0000313|Proteomes:UP000295070};
RN [1] {ECO:0000313|EMBL:TDH08167.1, ECO:0000313|Proteomes:UP000295070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YP-PL-M2 {ECO:0000313|EMBL:TDH08167.1};
RC TISSUE=Blood {ECO:0000313|EMBL:TDH08167.1};
RA Feron R., Morvezen R., Bestin A., Haffray P., Klopp C., Zahm M., Cabau C.,
RA Roques C., Donnadieu C., Bouchez O., Christie M., Larson W., Guiguen Y.;
RT "A chromosome-scale genome assembly of the yellow perch, Perca
RT flavescens.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDH08167.1}.
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DR EMBL; SCKG01000009; TDH08167.1; -; Genomic_DNA.
DR STRING; 8167.A0A484D064; -.
DR Proteomes; UP000295070; Chromosome 9.
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; 9.
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; 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; 7.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 3.
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 ECO:0000256|PIRSR:PIRSR500950-52};
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:UP000295070};
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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..935
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..302
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 614..691
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 704..795
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 979..1350
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1380..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1198
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 958
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 985..993
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT BINDING 986..993
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1013
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1061..1067
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 1342
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 441..486
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 534..575
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 621..675
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 820..887
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
SQ SEQUENCE 1467 AA; 163491 MW; 1EB96EE0778EEBAF CRC64;
MDGVKTYVVF GGILVVLVSV TFGLSPPTIV SNEEEFILQP NSVFNISCTG KRNVVWVEPL
PENTFVYPGY YTATLFIYNA TVENTGYYMC TYETPEGDLE DELDEDNEAG IYVFVPDPQA
PFVPETPDNL VVPMDTLGVP ISCRVSDPYS QVTLRSVPSG EDMPAYYDNK IGFFGSLLPG
QYQCETIVNG QTMRSAIYTV ETEAPADTED FDVEVKASGE TVRAGQPFNV TCVAPPGLGF
QQQWLHPKKQ AVDAVQMKQT FPDRVIYILS IQQATSQDSG TYECSVTQHI SGEVRVSSVA
VTVFEENSFV ALDHSGIQAT EFVSLLEETE FTILIDAYPA PKVTWLKDGT AMPQNYYILT
KTSHLEGNRY QSILTLRQPL GKDNGNYTIT ALSGSSTAQF SFTLKVKAPT AMMFPPSSAP
VLLPQVEEMV VPLHTPFTLT CRGEAKLDWE TPLDVHEQTQ EDNSGLFVTT VTVDSATAMH
TGYYTCSYSR NTTEDTEESS IYVYVPDPDV PFVPSPVPFG NHVLSDHEEM EIQCRVSDPS
ANVTLINVDT QQPVPSVYDS KRGALGVFTA GTYICKALIN GEEHSSGEYI VHGWTGGAAL
HVELTAKRTA LLVGETITVT CLARGSEILE DHWKYPGKLA NRAIKTVHEN KRAQEILYTL
TIPQASTKDS GIYSCSITDV ISNEDQTKEL AVQVFATAFM SVWPEFGEYE SAELDEVREF
RAKISSMPSA HVTWLKDGIL LSDVTAEISS SLRQLSETSY MSVLTLIRAK EEDSGNYTMR
VENGDQVHDV KLNLEVKVPA VIMDLMDIHH GSATGQSVVC ITRGQPTPVV EWFICKDIKH
CANDSSAWVP LPANSTEITM DSHINEESNL ESQVMFGHLE STLAVRCLAR NEMAVVSREV
KLVSNGPHPE LTVAAAVLVL LVIVIISLIV LVIIWKQKPR YEIRWRVIES VSPDGHEYIY
VDPMQLPYDS RWEFPRDRLV LGRILGSGAF GKVVEGTAYG LSRSQPVMKV AVKMLKPTAR
SSEKQALMSE LKIMTHLGPH LNIVNLLGAC TKSGPIYIIT EYCFYGDLVN YLHKNRENFL
SLTPEKSKKE LDIFGINPTD ESSRSYVILS FESKGDYMDM KQADTQYVPM LEMSNPHKYS
DIQRSNYDHP PSQKEDEMDV LLSDNMNEGL TTTDLLSFTY QVAKGMEFLA SKNCVHRDLA
ARNVLLSQGK IVKICDFGLA RDIMHDNNYV SKGSTFLPVK WMAPESIFDN MYTSLSDVWS
YGILLWEIFS LGGTPYPGMV VDSSFYNKIK SGYRMSKPEH APQDLYEMMM KCWNSEPEKR
PTFLGLSETV SSLLPSSYKR HYERVNHEFL KSDHPAVTRV CVENDDAYIG ITYKNQGKLK
DRESGFDEQR LSSDSGYIIP LPDLDPVSDD EYGKRNRHGS QTSEESAIET GSSSSTFAKR
EGETLEDITM LDEMCLDCSD LGEDSFL
//
