ID A0A556U6L6_BAGYA Unreviewed; 1644 AA.
AC A0A556U6L6;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-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=Baya_9422 {ECO:0000313|EMBL:TSN30193.1};
OS Bagarius yarrelli (Goonch) (Bagrus yarrelli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Sisoridae; Sisorinae; Bagarius.
OX NCBI_TaxID=175774 {ECO:0000313|EMBL:TSN30193.1, ECO:0000313|Proteomes:UP000319801};
RN [1] {ECO:0000313|EMBL:TSN30193.1, ECO:0000313|Proteomes:UP000319801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JWS20170419001 {ECO:0000313|EMBL:TSN30193.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TSN30193.1};
RX PubMed=31274158;
RA Jiang W., Lv Y., Cheng L., Yang K., Chao B., Wang X., Li Y., Pan X.,
RA You X., Zhang Y., Yang J., Li J., Zhang X., Liu S., Sun C., Yang J.,
RA Shi Q.;
RT "Whole-Genome Sequencing of the Giant Devil Catfish, Bagarius yarrelli.";
RL Genome Biol. Evol. 11:2071-2077(2019).
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}. Nucleus {ECO:0000256|PROSITE-
CC ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
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:TSN30193.1}.
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DR EMBL; VCAZ01000055; TSN30193.1; -; Genomic_DNA.
DR OrthoDB; 9936425at2759; -.
DR Proteomes; UP000319801; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; 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:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
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 GO; GO:0003309; P:type B pancreatic cell differentiation; IEA:UniProtKB-ARBA.
DR CDD; cd00086; homeodomain; 1.
DR FunFam; 1.10.10.60:FF:000176; pancreas/duodenum homeobox protein 1; 1.
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; 1.10.10.60; Homeodomain-like; 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; IPR001356; HD.
DR InterPro; IPR020479; HD_metazoa.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR009057; Homeodomain-like_sf.
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; PF00046; Homeodomain; 1.
DR Pfam; PF07679; I-set; 3.
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; PR00024; HOMEOBOX.
DR PRINTS; PR00109; TYRKINASE.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
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 Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000319801};
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 1143..1167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..173
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 434..536
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 846..925
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 936..1027
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1211..1509
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DNA_BIND 115..174
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 1561..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1374
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 1190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1217..1225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT BINDING 1218..1225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 1379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 1518
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT DISULFID 675..720
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 766..807
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 853..907
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 1052..1119
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
SQ SEQUENCE 1644 AA; 185525 MW; D0DF0B46AE0EEE81 CRC64;
MDSFDGYFNG SFEPQIHDSV EREPSACLYS QCADQAPYVE LQSNTAPGNQ ERDLAPYELP
SCQLLQAESP QADVFHPRTD DTTAHLAYPW MRASRSQISQ TPMTGEFLCE DPDDQKRSRT
AYSRAQLLEL EKEFLFNRYI SRPRRYELAT TLNLTERHIK IWFQNRRMKW KKEEARRCRS
TRKQERLEHD ADSTLATRLP STFFALRNFP GSEFDVHPNF CTQPRADLRA IRSFAYGLQS
ERREGKAAWL QRAAGDGTCD PSAPIIVSDR EEFVLELHSV FNISCTGKES VVWKEPLPAN
THVLPGFYTS TLLIEDAAAH HTGEYMCVYE SQYEDQETLD NIASIYIFVP GKNPQVPFAP
DDSTEASMYT IPCRITDPQT AVILRSLPSE DEVPSQYEQK YGFIGSYPPG QYVCETIVNG
EAVRSVVYNV PHIPSATEML NEMENYFSVK LTASPEEIKE GEAFSLICEV PPGSLYVQQW
LHLSKQAVSA VPRKEIYPDR VLYILSIPHA STNDTGFYEC FVTDQSNGKT RSSQVTIVVH
EGSFVTLDHS GIGAVETISL LEEAEFTIYI HSDAVPKVTW FKDDLVMNSN FITVKTTLLA
DKRYESVLVL RHPVEEDSGT YKIVAAAGSQ TEEFSFKLHV KAAEPQIMQS MLAPVIWPRK
ETMVMQLHST FRLTCRGQAE LAWDSPVPLD NQKLDDKRGL FVSTVTVDDA MATHTGEYTC
YYKNENQTDE SSIYIYVPDP NMLFVPALLP YGHHVLKSPD EMEIPCRVSD PSARVALLHV
ETQQEVPADY DSKKGFVGNF SPGTYVCQTL VNGEQHESEE YIVHGWIGGM GVQVELKADK
TALLVGETIV VNCVARGSDL LEQQWKYPGK MADRAIMNLK ENKKEQEIYY TLTVPDARTK
DSGNYACSIT DIMSNESQTK EVTITVYETE FVSLAPMFAP VETAKLNDVR EFQVEIEALP
APKVTWLKDG MVLGDIAAEF ITSLRMISKT RYQSTLVLIR AKAEDSGNYT VLAEIGNQSA
SHSFHLQVKV PAVILDLTDL HHGSETGQAV VCVAQGSPVP EVEWYICKNI KQCSNDSSEW
LPLQTNMTGI TVDTHIDQDN QLESQVIFGH LEDTLAVRCL VRNEMVAVSR EIKLVANGPH
SELTVAAAVL VLLVIVIISL IVLVIIWKQK PRYEIRWRVI ESVSPDGHEY IYVDPMQLPY
DTRWEFPRDG LVLGRILGSG AFGKVVEGTA YGLSRSQPVM KVAVKMLKPT ARSSEKQALM
SELKIMTHLG PHLNIVNLLG ACTKSEKGDY MDMKQADTMQ YVPMLERSNA YKYFDLQRDD
YDHPPSYKHI NESEVEKLLS DDSERLTTMD LLSFTYQVAR GMEFLASKNC VHRDLAARNV
LLSQGKIVKI CDFGLARDIM HDNNYVSKGS TFLPVKWMAP ESIFDNLYTT LSDVWSYGIL
LWEIFSLGGT PYPGMVVDSS FYNKIKSGYR MAKPEHASSD VYELMVKCWN NEPEKRPSFH
SLSESMASLL PCGYKRSYER VNNDFLKSDH PAVTRVQCVQ SDETYLGVAY KNQCKMRERE
SGFEEQRLSS DSGYIIPLPD LDPLSDEEYT KRNRHSSQTS EESAIETGSS SSTLPKREGE
TLEDITLLDE MCLDSGDLVE DSFL
//
