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Database: UniProt
Entry: A0A7K9A3I7_9PASS
LinkDB: A0A7K9A3I7_9PASS
Original site: A0A7K9A3I7_9PASS 
ID   A0A7K9A3I7_9PASS        Unreviewed;      1084 AA.
AC   A0A7K9A3I7;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   28-JAN-2026, entry version 22.
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:NXG21880.1};
GN   ORFNames=GRAVAR_R06261 {ECO:0000313|EMBL:NXG21880.1};
OS   Grallaria varia (variegated antpitta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Formicariidae; Grallaria.
OX   NCBI_TaxID=117165 {ECO:0000313|EMBL:NXG21880.1, ECO:0000313|Proteomes:UP000591535};
RN   [1] {ECO:0000313|EMBL:NXG21880.1, ECO:0000313|Proteomes:UP000591535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B10K-DU-001-02 {ECO:0000313|EMBL:NXG21880.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXG21880.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-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   -!- 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:NXG21880.1}.
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DR   EMBL; VWZG01009028; NXG21880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7K9A3I7; -.
DR   Proteomes; UP000591535; 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; 1.
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; 4.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
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:UP000591535};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1084
FT                   /note="Platelet-derived growth factor receptor alpha"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5029585046"
FT   TRANSMEM        525..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        878..896
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          212..306
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          414..517
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          593..974
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1014..1056
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1054
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        818
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         572
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         599..607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-51"
FT   BINDING         600..607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         675..681
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         822
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         823
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         836
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   DISULFID        49..99
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT   DISULFID        149..189
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT   DISULFID        235..290
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT   DISULFID        435..501
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500950-52"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXG21880.1"
FT   NON_TER         1084
FT                   /evidence="ECO:0000313|EMBL:NXG21880.1"
SQ   SEQUENCE   1084 AA;  122539 MW;  A341C06278A70AE6 CRC64;
     MGTSPQTFLI LGCFLTGPLL TFCQLPLPTI VPNRNEMVVQ LNSNFTLKCS GDSEVSWQYP
     VTEGSHRIDV RHEENNSGLF MTVLEVANAS AAHTGLYVCY YNHTQVEDGE VEGKDIYIYV
     PDPDMPFVPS IPEDQFILVE EGDPTVIPCR TSDPDAQVTL INSLDKAVYA LYDTKQGFIG
     NFPAGSYTCK TMAKGVEFKS EDFLVYIIRA TPQLPVEIEA LKTVYKTGET IVVTCVVFDN
     EVVNLQWNYP GKVKEKGLIK LDDIKVPSQK LVYTLTIPEA SVKDTGDYEC TARHATKEVK
     ENKKVVITVH DKGFVHLEPQ FSPQETVNLH EVKNFVVDVQ AYPAPKMYWL KDNVTLIENL
     TEIVTSSNRV QETRFQSVLK LIRAKEEDSG YYTLVAENED EIKRYTFSLL IRVPALISAL
     VDDHHGTAGG QTVRCLAEGT PPPDVEWLVC KDIKKCNNDT SWTLLTSNIS DIHMEAHLDE
     KNMVESQVTF QKVEETLAVR CVARNDLGAV TRELKLVAPT LRSELTVAAA VLVLLVIVII
     SLIVLVIIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG
     SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL
     LGACTKSGPI YIITEYCFYG DLVNYLHKNR DNFLNRHPEK PKKDLDIFGM NPADESTRSY
     VILSFENTGE YMDMKQADTT QYVPMLERKE GSKYSDIQRS VYDRPASYKK KSMSESEVKN
     LLSDDSSEGL SLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA
     RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGMYLIKFFQ
     FKLFYKNKLY VRNPLLVVVL YISDSSVRCE VKCLYSPKVL IFAGLTFHSC PSEERQPYYE
     KIHLDFLKSD HPAVTRMRGD CDNAYIGVTY KNEDKLKDRE SGFDEQRLSA DSGYIIPLPD
     IDPVSEDELG KRNRHSSQTS EESAIETGSS SSTFIKREDE TIEDIDMMDD IGIDSSDLVE
     DSFL
//
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