ID A0A8J4MYC2_EUDMI Unreviewed; 1089 AA.
AC A0A8J4MYC2;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
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};
DE Flags: Fragment;
GN Name=PDGFRA {ECO:0000313|EMBL:KAF1499218.1};
GN ORFNames=FQV19_0013261 {ECO:0000313|EMBL:KAF1499218.1};
OS Eudyptula minor (Little blue penguin) (Aptenodytes minor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Aequornithes; Sphenisciformes;
OC Spheniscidae; Eudyptula.
OX NCBI_TaxID=37083 {ECO:0000313|EMBL:KAF1499218.1, ECO:0000313|Proteomes:UP000782854};
RN [1] {ECO:0000313|EMBL:KAF1499218.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Gonzo {ECO:0000313|EMBL:KAF1499218.1};
RX PubMed=31531675; DOI=10.1093/gigascience/giz117;
RA Pan H., Cole T.L., Bi X., Fang M., Zhou C., Yang Z., Ksepka D.T., Hart T.,
RA Bouzat J.L., Argilla L.S., Bertelsen M.F., Boersma P.D., Bost C.A.,
RA Cherel Y., Dann P., Fiddaman S.R., Howard P., Labuschagne K., Mattern T.,
RA Miller G., Parker P., Phillips R.A., Quillfeldt P., Ryan P.G., Taylor H.,
RA Thompson D.R., Young M.J., Ellegaard M.R., Gilbert M.T.P., Sinding M.S.,
RA Pacheco G., Shepherd L.D., Tennyson A.J.D., Grosser S., Kay E., Nupen L.J.,
RA Ellenberg U., Houston D.M., Reeve A.H., Johnson K., Masello J.F.,
RA Stracke T., McKinlay B., Borboroglu P.G., Zhang D.X., Zhang G.;
RT "High-coverage genomes to elucidate the evolution of penguins.";
RL Gigascience 8:0-0(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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Golgi
CC apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC {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:KAF1499218.1}.
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DR EMBL; VULC01021909; KAF1499218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J4MYC2; -.
DR OrthoDB; 9936425at2759; -.
DR Proteomes; UP000782854; Unassembled WGS sequence.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; 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: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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:TreeGrafter.
DR CDD; cd05859; Ig4_PDGFR; 1.
DR FunFam; 1.10.510.10:FF:002211; -; 1.
DR FunFam; 2.60.40.10:FF:000720; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 2.60.40.10:FF:000725; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 2.60.40.10:FF:000776; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 2.60.40.10:FF:000832; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR FunFam; 2.60.40.10:FF:000223; Platelet-derived growth factor receptor beta; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
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; 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; 4.
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; 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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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:UP000782854};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 524..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 877..895
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..305
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 592..979
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1019..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 817
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 571
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 598..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT BINDING 599..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 674..680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 822
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 835
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT DISULFID 48..98
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 148..188
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 234..289
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT DISULFID 434..500
FT /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAF1499218.1"
FT NON_TER 1089
FT /evidence="ECO:0000313|EMBL:KAF1499218.1"
SQ SEQUENCE 1089 AA; 123192 MW; C98ACF3D711270F3 CRC64;
GCSVCSCAIY SCRFAGPFLT LCQLPLPTIV PNRNEMVVQL NSNFTLKCSG DSEVSWQYPV
TEGSHRIDIR HEENNSGLFV TVLEVGNASA AHTGLYVCYY NHTQVEDGEV EGKDIYIYVP
DPDMPFVPSI PEDQFILVEE GDPTVIPCRT SDPKAQVTLI NSLDKAVYAF YDSKQGFIGN
FPAGSYTCKT MIKGMEFKSD EFLIYILRAT SQLPVEIEAL KTVYKTGETI VVTCVVFDNE
VVNLQWNYPG KVKEKGLIKL DDIKVPSQKL VYTLTIPEAS VKDTGDYECT ARHATKEVKE
NKKVVITVHD KGFVHLEPQF SPLEAVNLHE VKNFVVDVQA YPAPKMYWLK DNVTLIENLT
EIVTSSNRVQ ETRFQSILKL IRAKEEDSGY YTLVAENEDE IKRYTFSLLI QVPALILDLV
DDHHGSAGGQ TVRCLAEGTP LPDVEWLVCK DIKKCSNDTS WTLLTNNISD IHMEAHLDEK
NMVESQVTFQ KVEETLAVRC VARNDLGAVT RELKLVAPTL RSELTVAAAV LVLLVIVIIS
LIVLVIIWKQ KPRYEIRWRV IESISPDGHE YIYVDPMQLP YDSRWEFPRD GLVLGRILGS
GAFGKVVEGT AYGLSRSQPV MKVAVKMLKP TARSSEKQAL MSELKIMTHL GPHLNIVNLL
GACTKSGPIY IITEYCFYGD LVNYLHKNRD NFLSRHPEKP KKDLDIFGMN PADESTRSYV
ILSFENTGEY MDMKQADTTQ YVPMLERKEG SKYSDIQRSV YDRPASYKKK SMSESEVKNL
LSDDSSEGLS LLDLLSFTYQ VARGMEFLAS KNCVHRDLAA RNVLLAQGKI VKICDFGLAR
DIMHDSNYVS KGSTFLPVKW MAPESIFDNL YTTLSDVWSY GILLWEIFSL GMYLIKLFQF
KLFYIKYFKF CSKNICVKST VILLYGVLDP NVRCEVKRPY SPKGRIFAGL MNHSYPSEER
QPYYEKIHLD FLKSDHPAVT RMRGDCDNAY IGVTYKNEDK LKDRESGFDE QRLSADSGYI
IPLPDIDPVS EDELGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS
SDLVEDSFL
//
