ID A0A4U5UN75_COLLU Unreviewed; 1531 AA.
AC A0A4U5UN75;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 29.
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=D9C73_009058 {ECO:0000313|EMBL:TKS74975.1};
OS Collichthys lucidus (Big head croaker) (Sciaena lucida).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Collichthys.
OX NCBI_TaxID=240159 {ECO:0000313|EMBL:TKS74975.1, ECO:0000313|Proteomes:UP000298787};
RN [1] {ECO:0000313|EMBL:TKS74975.1, ECO:0000313|Proteomes:UP000298787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JT15FE1705JMU {ECO:0000313|EMBL:TKS74975.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TKS74975.1};
RA Cai M., Xiao S.;
RT "Genome Assembly of Collichthys lucidus.";
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}.
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DR EMBL; CM014085; TKS74975.1; -; Genomic_DNA.
DR STRING; 240159.A0A4U5UN75; -.
DR Proteomes; UP000298787; Chromosome 8.
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: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; 8.
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; 1.
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 SMART; SM00409; IG; 6.
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; 4.
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|PIRSR:PIRSR500950-
KW 51}; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR500950-51};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000298787};
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 531..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 970..994
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..355
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 673..752
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 763..850
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 858..962
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1038..1414
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1200..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1262
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-50"
FT BINDING 1044..1052
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT BINDING 1072
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 471..516
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 593..634
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 680..734
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 879..946
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
SQ SEQUENCE 1531 AA; 170780 MW; B44BA278F696D012 CRC64;
MSLLTLLDKK CSVSASQLEV SPPKTEGSIV GCRLALNGKH IFWKLYITLF SRLVVECEEL
KKWEKEKETA PGMSPCDITS IVMDELKTYV VFGVLLVALV SVTSGLSPPT IVSNEEEFIL
KPNSMFNISC TGKKNVIWAD PLPKNTLVYT GYYTATLFIS NATVENTGYY MCVYDNQEGE
LQGDPDDENE AGIYVFVPDA QAPFVPETPD NLIVPMEPSG VPISCRVSNP NSHVILRSVH
SGEEMSVLYD NKMGFFGNLS PGQYQCETTL NGQTFTSFVY TVETEDIAEF EDFDVEVRAS
EETAVGAVQL KQTFPDWVIY TLSIPHATSQ DSGMYECSVT HEFSREVRVS SVSVTVFEES
SFVALDHSGI LATESVNLLE ETEFTILINA YPPPKVMWLK DGKAIPESYF ILTKTSHLEG
NRRLLQTNIE TKLSAVPLSN KKYSVFIAAP VLLPKVEEMV VPLHTSFTLT CRGEGKLAWE
TPFEMPEKTQ EDNSGLFVTT ITVDNATAMH TGYYICFYSR NTTDDTEDSS IYIYVPGMAC
TAAFVFFYYL TSLSGLGKFF SFPNSDPDAP FVPSPVPFGN HVLSDHEEME IQCRVSDPSA
NVTLVNVDTQ QPVPSVYDSK RGALGVFTAG TYVCKALING EEHYSGEYIV HGWTGGAALH
VELTAKRTAL LVGDTITVTC LARGSEILED HWKYPGKVAN RAVKTVHENK RDQEILYTLT
IPQASTKDSG IYSCSITDII SNESQTKQLA IQVFGSEFLT IWPKFGEYES AELDEVREFK
AEISSFPSAH VTWLKDGIPL SDVTAEISTS LRQLSETSYM SVLTLIRAKE EDSGNYTMRV
ENGDQRRSVG LMLEVKVPAV IVDLMDIHHG SATGQSVVCI TRGQPTPVVE WFVCKNIKHC
ANDSSSWVPL PANSTEISMD SHFDEENNLE SQVMFGHLEN TLAVRCLARN EMAAVSREVK
LVSNGPHPEL TVAAAVLVLL VIVIISLIVL VVIWKQKPRY EIRWRVIESV SPDGHEYIYV
DPMQLPYDSR WEFPRDRLVL GRILGSGAFG KVVEGTAYGL SRSQPVMKVA VKMLKPTARS
SEKQALMSEL KIMTHLGPHL NIVNLLGACT KSGPIYIITE YCFYGDLVNY LHKNRENFLS
LNPEKNNKKE LDIFGINPAD ESSRSYVILS FESKGDYMDM KQADNTQYVP MLEMSNTSKY
SDIQGSNYDQ PPSQKGSNEG EMDDLLSDDM SEGLTTTDLL SFTYQVAKGM EFLASKNCVH
RDLAARNVLL SQGKIVKICD FGLARDIMHD NNYVSKGSTF LPVKWMAPES IFDNLYTTLS
DVWSYGILLW EIFSLGGTPY PGMVVDSSFY NKIKSGYRMS KPEHAPHDVY EMMMKCWNSE
PEKRPSFLGL SDTVASLLPS SYKRHYERVN HEFLKSDHPA VTRVCMENND AYIGITYKNQ
GKLKDRESGF DEQRLSSDSG YIIPLPDLDP ISDDEYGKRN RHGSQTSEES AIETGSSSST
FAKREGETLE DITLLDEMCL DCSDLVEDSF L
//
