ID A0A9Q1DTM3_CONCO Unreviewed; 1439 AA.
AC A0A9Q1DTM3;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
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=COCON_G00071400 {ECO:0000313|EMBL:KAJ8280074.1};
OS Conger conger (Conger eel) (Muraena conger).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Congridae; Conger.
OX NCBI_TaxID=82655 {ECO:0000313|EMBL:KAJ8280074.1, ECO:0000313|Proteomes:UP001152803};
RN [1] {ECO:0000313|EMBL:KAJ8280074.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Concon-B {ECO:0000313|EMBL:KAJ8280074.1};
RX PubMed=36758078;
RA Parey E., Louis A., Montfort J., Bouchez O., Roques C., Iampietro C.,
RA Lluch J., Castinel A., Donnadieu C., Desvignes T., Floi Bucao C.,
RA Jouanno E., Wen M., Mejri S., Dirks R., Jansen H., Henkel C., Chen W.J.,
RA Zahm M., Cabau C., Klopp C., Thompson A.W., Robinson-Rechavi M.,
RA Braasch I., Lecointre G., Bobe J., Postlethwait J.H., Berthelot C.,
RA Roest Crollius H., Guiguen Y.;
RT "Genome structures resolve the early diversification of teleost fishes.";
RL Science 379:572-575(2023).
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:KAJ8280074.1}.
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DR EMBL; JAFJMO010000004; KAJ8280074.1; -; Genomic_DNA.
DR OrthoDB; 9936425at2759; -.
DR Proteomes; UP001152803; Unassembled WGS sequence.
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; 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; PF13927; Ig_3; 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; PIRSF500950; Alpha-PDGF_receptor; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 4.
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:UP001152803};
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 890..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..294
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 300..394
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 414..498
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 613..692
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 958..1311
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1373..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1439
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 937
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 964..972
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT BINDING 965..972
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 992
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1040..1046
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 1319
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 435..483
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 533..574
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 620..674
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 799..866
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
SQ SEQUENCE 1439 AA; 159846 MW; 8F5D51FB74774DB3 CRC64;
MDALRTYLAV QIVLIGMLSG FQTVVSIPPT IVTNQDEFVL PLRSQFNISC TGKRAVAWSG
PRPHRVLSEP GFYTATLFIQ NATAENTGYF TCNYTTPGGH AWEEESDIYI FVPDPQVPFI
PEAPRDSHVL SDETGTVIPC RVTDPASHVV LRSAGSGAEV PGLYDSKLGF IGDFPPGAYV
CETSASGVRT YSITYTVGQS PESADLHVEL RASRVSLRVG EPFHLTCAAP AGSSYHQQWL
HPGTQVELLQ QQTQEQVVYV LRVERASLQD AGEYQCSVTN TLTAQSHSQT ATITIHPERP
TLTLEHRLAG VEFAELQEEK ELSVFIDAYP APRVLWLRDG VVIDNSDPMV FSKTRHIGGI
RYQSTLTLSR PTEDDSGNYS LMASSDSSPS AQTSFLLRVK TPSQPLQPLA LFPPAIEPQG
EETVVPLHSP FRLRCRGEAE LAWDTPTLLG PDWEGPGEDN SGLFISSVTV ENATAAHSGF
YTCYYTYANN TDHELEASSI YVYVPDPDVP FVPSMVPFGN HVLTNHEEME IPCRVTDPST
NVTLMNVDTQ KAVPSQYDSK RGAVGFFTSG TYVCHALVNG HEHLSEDYIV HGWTGGSGLQ
VDLQAPRAAL LVGESLVVTC VARGSEMLED NWKYPGKRAQ RGVKTVRENK KEQEIRYMLT
IPQASVKDSG LYACSITDIL SNDSQTRELS ITVYDRPFVS LDPLFRQAQF AELDEDGAVL
NDISAEITNS LQPITETRFR SVLRLIRAKE EDSGNYTIRV ENGNQSQTFN FTLQVKIPVA
IVDLMDLHHG SASGQSVVCI SRGLPIPEVE WFTCSNIKQC ANDSSQWTPL PVNSSEVTVE
THINEDNNLE SQVIFAKLDS TLSVRCLARN ELSAVSREVK LVSNALQSEL TVAAAVLVLL
VIVIISLIIL VIIWKQKPRY EIRWRVIESI SPDGHEYIYV DPMQLPYDSR WEFPRDGLVL
GRVLGSGAFG KVVEGTAYGL TRSQPVMKVA VKMLKPTARS SEKQALMSEL KIMTHLGPHL
NIVNLLGACT KSGPIYIITE YCLHGDLVNY LHKNRETFLS RHPEKAKKDL DIFGLDPADQ
SSRSYVILSF ESKADYMDMK PADATQYVPM LEMSDSPVNY DRPPSHKDKA LSEGEGRGLL
DDVTEGLSTM DLLSFTFQVA RGMDFLASKN CVHRDLAARN VLLSHGKIVK ICDFGLARDI
MHDNNYVSKG STFLPVKWMA PESIFDNLYT TLSDVWSYGI LLWEIFSLGG TPYPGMVVDS
SFYNKIKSGY RMSKPEHATS DVYEVMMRCW NSEPEKRPSF HSLSETVATL LPSEYKKSYE
RVNQDFLKSD HPAVTRVCVE GDAYVGMAYK NQGKAKQRES GLEEQRLSSD SGYIIPLPDL
EPLSDHPHSK RNRHSSQTSE ESAIETGSSS STLLRREAET LEDIQDLELE EELEEDSFL
//
