ID A0A1A6G0X4_NEOLE Unreviewed; 1033 AA.
AC A0A1A6G0X4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 28-JAN-2026, entry version 47.
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 ORFNames=A6R68_09414 {ECO:0000313|EMBL:OBS59460.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS59460.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS59460.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS59460.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS59460.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) 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 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:OBS59460.1}.
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DR EMBL; LZPO01108079; OBS59460.1; -; Genomic_DNA.
DR STRING; 56216.A0A1A6G0X4; -.
DR OrthoDB; 9936425at2759; -.
DR Proteomes; UP000092124; 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:TreeGrafter.
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 GO; GO:0006950; P:response to stress; IEA:UniProtKB-ARBA.
DR GO; GO:0007423; P:sensory organ development; IEA:UniProtKB-ARBA.
DR GO; GO:0035295; P:tube development; IEA:UniProtKB-ARBA.
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: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 FunFam; 1.10.510.10:FF:001346; Uncharacterized protein; 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; 2.
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; 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; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
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 Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000092124};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1033
FT /note="Platelet-derived growth factor receptor alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008345195"
FT TRANSMEM 508..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 209..329
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 576..1033
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 963..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1033
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 801
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 555
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 583..590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 658..664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 805
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 806
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 819
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 907
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT NON_TER 1033
FT /evidence="ECO:0000313|EMBL:OBS59460.1"
SQ SEQUENCE 1033 AA; 116083 MW; F502C69FBED53DB6 CRC64;
MVMIMLMWGW TGPWLVSLAG ELQDGNVIKT PAGKLALGAA LKLVKWIIGP SLIFCQLLLP
SILPNENEKV VQLNSSFSLR CFGESEVSWQ HPMSEEEDPN VEIRNEENNS GLFVTVLEVV
NASAAHTGWY TCYYNHTQTD ESEXEGRHIY IYVPGMTDSL VIVEEDDSAI IPCRTTDPET
QVTLHNNGRL VLASYDSRQG FNGTFSVGPY ICEATVKGRT FKTGEFXVYA LKATSDLNLE
MEARQTVYKS GETIVVTCAV FNNEVVDLQW TYPGEVRNKG ITMLEEIKLP SIKLVYTLTV
PKATVKDSGD YECAARQATK EVKEMKKVTI SVHEKGFVEI KPTFGQLEAV NLHQVREYQS
KLKLIRAKEE DSGHYTIIVQ NDDDIKSYTF ELSTLVPASI LELVDDHDGS GGGQTVRCTA
EGTPLPDIXW MICKDIKKCN NDTSWTTLAS NVSNIITEFH RRGRSTVEGR VSFAKVEETI
AVRCLAKNDL GIGNRELKLV APTLRSELTV AAAVLVLLVI VIVSLIVLVV IWKQKPRYEI
RWRVIESISP DGHEYIYVDP MQLPYDSRWE FPRDGLVLGR ILGSGAFGKV VEGTAYGLSR
SQPVMKVAVK MLKPTARSSE KQALMSELKI MTHLGPHLNI VNLLGACTKS GPIYIITEYC
FYGDLVNYLH KNRDSFMSRH PEKPKKELDI FGLNPADDST RSYVILSFEN NGDYMDMKQA
DTTQYVPMLE RKEVSKYSDI QRSLYDRPAS YKKKSMLDSE VKNLLSDDDS EGLTLLDLLS
FTYQVARGME FLASKNCVHR DLAARNVLLA QGKIVKICDF GLARDIMHDS NYVSKGSGTP
YPGMMVDSTF YNKIKSGYRM AKPDXATSEV YEIMVQCWNS EPEKRPSFYH LSEIVENLLP
GQYKKSYEKI HLDFLKSDHP AVARMRVDSD NAYIGVTYKN EDDKLKDWEG GLDEQRLSAD
SGYIIPLPDI DPVPEEEDLG KRNRHSSQTS EESAIETGSS SSTFIKREDE TIEDIDMMDD
IGIDSSDLVE DSF
//
