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P26618

- PGFRA_MOUSE

UniProt

P26618 - PGFRA_MOUSE

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Protein

Platelet-derived growth factor receptor alpha

Gene

Pdgfra

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca2+ and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor.4 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

Present in an inactive conformation in the absence of bound ligand. Binding of PDGFA and/or PDGFB leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by imatinib, nilotinib and sorafenib (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei627 – 6271ATPPROSITE-ProRule annotation
Active sitei818 – 8181Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi599 – 6079ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. platelet-derived growth factor alpha-receptor activity Source: UniProtKB
  3. platelet-derived growth factor binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. vascular endothelial growth factor-activated receptor activity Source: UniProtKB

GO - Biological processi

  1. adrenal gland development Source: MGI
  2. anatomical structure morphogenesis Source: MGI
  3. cardiac myofibril assembly Source: UniProtKB
  4. cell chemotaxis Source: UniProtKB
  5. cell migration Source: UniProtKB
  6. cellular response to amino acid stimulus Source: MGI
  7. embryonic cranial skeleton morphogenesis Source: UniProtKB
  8. embryonic digestive tract morphogenesis Source: UniProtKB
  9. estrogen metabolic process Source: MGI
  10. extracellular matrix organization Source: MGI
  11. face morphogenesis Source: MGI
  12. female gonad development Source: MGI
  13. hematopoietic progenitor cell differentiation Source: MGI
  14. in utero embryonic development Source: MGI
  15. Leydig cell differentiation Source: MGI
  16. lung development Source: MGI
  17. luteinization Source: MGI
  18. male genitalia development Source: MGI
  19. metanephric glomerular capillary formation Source: UniProtKB
  20. negative regulation of platelet activation Source: UniProtKB
  21. odontogenesis of dentin-containing tooth Source: MGI
  22. organ morphogenesis Source: MGI
  23. palate development Source: MGI
  24. peptidyl-tyrosine phosphorylation Source: UniProtKB
  25. phosphatidylinositol-mediated signaling Source: UniProtKB
  26. platelet aggregation Source: UniProtKB
  27. platelet-derived growth factor receptor-alpha signaling pathway Source: UniProtKB
  28. platelet-derived growth factor receptor signaling pathway Source: MGI
  29. positive regulation of cell migration Source: UniProtKB
  30. positive regulation of cell proliferation Source: UniProtKB
  31. positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
  32. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  33. positive regulation of DNA replication Source: UniProtKB
  34. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  35. positive regulation of fibroblast proliferation Source: UniProtKB
  36. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  37. positive regulation of phospholipase C activity Source: Ensembl
  38. protein autophosphorylation Source: UniProtKB
  39. regulation of chemotaxis Source: Ensembl
  40. regulation of mesenchymal stem cell differentiation Source: UniProtKB
  41. retina vasculature development in camera-type eye Source: UniProtKB
  42. signal transduction involved in regulation of gene expression Source: MGI
  43. skeletal system morphogenesis Source: MGI
  44. wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Chemotaxis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_226341. PIP3 activates AKT signaling.
REACT_230639. Downstream signal transduction.
REACT_263353. Signaling by PDGF.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-derived growth factor receptor alpha (EC:2.7.10.1)
Short name:
PDGF-R-alpha
Short name:
PDGFR-alpha
Alternative name(s):
Alpha platelet-derived growth factor receptor
Alpha-type platelet-derived growth factor receptor
CD140 antigen-like family member A
Platelet-derived growth factor alpha receptor
CD_antigen: CD140a
Gene namesi
Name:Pdgfra
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:97530. Pdgfra.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein
Note: The activated receptor is rapidly internalized and degraded.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 528504ExtracellularSequence AnalysisAdd
BLAST
Transmembranei529 – 54921HelicalSequence AnalysisAdd
BLAST
Topological domaini550 – 1089540CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. cytoplasm Source: UniProtKB
  3. external side of plasma membrane Source: MGI
  4. integral component of plasma membrane Source: UniProtKB
  5. microvillus Source: MGI
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryonically lethal. Most embryos survive up to 13 dpc, but display important defects in skeleton development, including spina bifida, fusions of cervical vertebrae and ribs, and incomplete fusion of the skull parietal bone. Embryos display also abnormal mucosa lining the gastrointestinal tract, including fewer and misshapen villi and loss of pericryptal mesenchyme. At about 16 dpc, embryos display extensive hemorrhaging.3 Publications

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 10891065Platelet-derived growth factor receptor alphaPRO_0000016761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi49 ↔ 100PROSITE-ProRule annotation
Glycosylationi76 – 761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi150 ↔ 189PROSITE-ProRule annotation
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi235 ↔ 290PROSITE-ProRule annotation
Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi435 ↔ 501PROSITE-ProRule annotation
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi506 – 5061N-linked (GlcNAc...)Sequence Analysis
Modified residuei555 – 5551PhosphotyrosineBy similarity
Modified residuei572 – 5721Phosphotyrosine; by autocatalysisBy similarity
Modified residuei574 – 5741Phosphotyrosine; by autocatalysisBy similarity
Modified residuei582 – 5821PhosphotyrosineBy similarity
Modified residuei720 – 7201Phosphotyrosine; by autocatalysisCurated
Modified residuei731 – 7311Phosphotyrosine; by autocatalysisBy similarity
Modified residuei742 – 7421Phosphotyrosine; by autocatalysisBy similarity
Modified residuei754 – 7541Phosphotyrosine; by autocatalysisBy similarity
Modified residuei762 – 7621Phosphotyrosine; by autocatalysisBy similarity
Modified residuei768 – 7681Phosphotyrosine; by autocatalysisBy similarity
Modified residuei849 – 8491Phosphotyrosine; by autocatalysisBy similarity
Modified residuei944 – 9441PhosphotyrosineBy similarity
Modified residuei958 – 9581PhosphotyrosineBy similarity
Modified residuei962 – 9621PhosphotyrosineBy similarity
Modified residuei988 – 9881Phosphotyrosine; by autocatalysisBy similarity
Modified residuei993 – 9931PhosphotyrosineBy similarity
Modified residuei1018 – 10181Phosphotyrosine; by autocatalysis

Post-translational modificationi

Ubiquitinated, leading to its degradation.By similarity
Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-731 and Tyr-742 is important for interaction with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is important for interaction with PTPN11. Phosphorylation at Tyr-762 is important for interaction with CRK. Phosphorylation at Tyr-572 and Tyr-574 is important for interaction with SRC and SRC family members. Phosphorylation at Tyr-988 and Tyr-1018 is important for interaction with PLCG1 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP26618.
PRIDEiP26618.

PTM databases

PhosphoSiteiP26618.

Expressioni

Tissue specificityi

Focally expressed in cortical interstitial cells and highly expressed in the interstitium of the papillary region. Also expressed by adventitial cells in arterial vessels. Up-regulated in areas of renal fibrosis. In mice with unilateral ureteral obstruction, expression in cortical interstitial cells becomes prominent at day 4 which increases progressively until day 14.1 Publication

Gene expression databases

BgeeiP26618.
ExpressionAtlasiP26618. baseline and differential.
GenevestigatoriP26618.

Interactioni

Subunit structurei

Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB (via SH2 domain). Interacts (tyrosine phosphorylated) with SHF (via SH2 domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine phosphorylated) with CRK, GRB2 and GRB7 (By similarity).By similarity

Protein-protein interaction databases

BioGridi202088. 1 interaction.
IntActiP26618. 3 interactions.
MINTiMINT-4107325.

Structurei

3D structure databases

ProteinModelPortaliP26618.
SMRiP26618. Positions 28-507, 553-997.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 11389Ig-like C2-type 1Add
BLAST
Domaini117 – 20185Ig-like C2-type 2Add
BLAST
Domaini202 – 306105Ig-like C2-type 3Add
BLAST
Domaini319 – 41092Ig-like C2-type 4Add
BLAST
Domaini414 – 517104Ig-like C2-type 5Add
BLAST
Domaini593 – 954362Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112009.
HOVERGENiHBG004335.
InParanoidiP26618.
KOiK04363.
OMAiDYECAAR.
OrthoDBiEOG71G9T1.
PhylomeDBiP26618.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR027290. PDGFRA.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PANTHERiPTHR24416:SF52. PTHR24416:SF52. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500950. Alpha-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P26618-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGTSHQVFLV LSCLLTGPGL ISCQLLLPSI LPNENEKIVQ LNSSFSLRCV
60 70 80 90 100
GESEVSWQHP MSEEDDPNVE IRSEENNSGL FVTVLEVVNA SAAHTGWYTC
110 120 130 140 150
YYNHTQTDES EIEGRHIYIY VPDPDMAFVP LGMTDSLVIV EEDDSAIIPC
160 170 180 190 200
RTTDPETQVT LHNNGRLVPA SYDSRQGFNG TFSVGPYICE ATVKGRTFKT
210 220 230 240 250
SEFNVYALKA TSELNLEMDA RQTVYKAGET IVVTCAVFNN EVVDLQWTYP
260 270 280 290 300
GEVRNKGITM LEEIKLPSIK LVYTLTVPKA TVKDSGEYEC AARQATKEVK
310 320 330 340 350
EMKRVTISVH EKGFVEIEPT FGQLEAVNLH EVREFVVEVQ AYPTPRISWL
360 370 380 390 400
KDNLTLIENL TEITTDVQKS QETRYQSKLK LIRAKEEDSG HYTIIVQNED
410 420 430 440 450
DVKSYTFELS TLVPASILDL VDDHHGSGGG QTVRCTAEGT PLPEIDWMIC
460 470 480 490 500
KHIKKCNNDT SWTVLASNVS NIITELPRRG RSTVEGRVSF AKVEETIAVR
510 520 530 540 550
CLAKNNLSVV ARELKLVAPT LRSELTVAAA VLVLLVIVIV SLIVLVVIWK
560 570 580 590 600
QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG
610 620 630 640 650
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH
660 670 680 690 700
LGPHLNIVNL LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFMSQHPEK
710 720 730 740 750
PKKDLDIFGL NPADESTRSY VILSFENNGD YMDMKQADTT QYVPMLERKE
760 770 780 790 800
VSKYSDIQRS LYDRPASYKK KSMLDSEVKN LLSDDDSEGL TLLDLLSFTY
810 820 830 840 850
QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA RDIMHDSNYV
860 870 880 890 900
SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM
910 920 930 940 950
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV QCWNSEPEKR PSFYHLSEIV
960 970 980 990 1000
ENLLPGQYKK SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL
1010 1020 1030 1040 1050
KDWEGGLDEQ RLSADSGYII PLPDIDPVPE EEDLGKRNRH SSQTSEESAI
1060 1070 1080
ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL
Length:1,089
Mass (Da):122,683
Last modified:February 26, 2008 - v3
Checksum:i07AAFD2BAA12533A
GO
Isoform 2 (identifier: P26618-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     775-790: DSEVKNLLSDDDSEGL → GKSAHAHSGKYDLSVV
     791-1089: Missing.

Note: No experimental confirmation available.

Show »
Length:790
Mass (Da):88,629
Checksum:iFE13756876B68B95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651D → E in AAA39733. (PubMed:2174116)Curated
Sequence conflicti65 – 651D → E in AAA39904. (PubMed:1321404)Curated
Sequence conflicti192 – 1921T → A in AAA39733. (PubMed:2174116)Curated
Sequence conflicti202 – 2021E → A in AAA39733. (PubMed:2174116)Curated
Sequence conflicti252 – 2521E → G in AAA39733. (PubMed:2174116)Curated
Sequence conflicti271 – 2711L → V in AAA39733. (PubMed:2174116)Curated
Sequence conflicti322 – 3221G → S in AAA39733. (PubMed:2174116)Curated
Sequence conflicti326 – 3261A → P in AAA39733. (PubMed:2174116)Curated
Sequence conflicti439 – 4402GT → EG in AAA39733. (PubMed:2174116)Curated
Sequence conflicti472 – 4721I → V in BAE37548. (PubMed:16141072)Curated
Sequence conflicti529 – 5291A → E in AAA39733. (PubMed:2174116)Curated
Sequence conflicti737 – 7371A → D in AAA39733. (PubMed:2174116)Curated
Sequence conflicti849 – 8491Y → D in AAA39733. (PubMed:2174116)Curated
Sequence conflicti936 – 9361E → D in AAA39733. (PubMed:2174116)Curated
Sequence conflicti950 – 9501V → L in AAA39733. (PubMed:2174116)Curated
Sequence conflicti1005 – 10051G → S in AAA39904. (PubMed:1321404)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei775 – 79016DSEVK…DSEGL → GKSAHAHSGKYDLSVV in isoform 2. 1 PublicationVSP_031877Add
BLAST
Alternative sequencei791 – 1089299Missing in isoform 2. 1 PublicationVSP_031878Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57683 mRNA. Translation: AAA39733.1.
M84607 mRNA. Translation: AAA39904.1.
AK081664 mRNA. Translation: BAC38283.1.
AK136490 mRNA. Translation: BAE23004.1.
AK147267 mRNA. Translation: BAE27808.1.
AK163952 mRNA. Translation: BAE37548.1.
BC053036 mRNA. Translation: AAH53036.1.
CCDSiCCDS19351.1. [P26618-1]
PIRiI57511. S33727.
RefSeqiNP_001076785.1. NM_001083316.1. [P26618-1]
NP_035188.2. NM_011058.2. [P26618-1]
XP_006504324.1. XM_006504261.1. [P26618-1]
XP_006504325.1. XM_006504262.1. [P26618-1]
XP_006504326.1. XM_006504263.1. [P26618-1]
UniGeneiMm.221403.

Genome annotation databases

EnsembliENSMUST00000000476; ENSMUSP00000000476; ENSMUSG00000029231. [P26618-1]
ENSMUST00000168162; ENSMUSP00000127173; ENSMUSG00000029231. [P26618-1]
GeneIDi18595.
KEGGimmu:18595.
UCSCiuc008xub.1. mouse. [P26618-2]
uc008xuc.1. mouse. [P26618-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57683 mRNA. Translation: AAA39733.1 .
M84607 mRNA. Translation: AAA39904.1 .
AK081664 mRNA. Translation: BAC38283.1 .
AK136490 mRNA. Translation: BAE23004.1 .
AK147267 mRNA. Translation: BAE27808.1 .
AK163952 mRNA. Translation: BAE37548.1 .
BC053036 mRNA. Translation: AAH53036.1 .
CCDSi CCDS19351.1. [P26618-1 ]
PIRi I57511. S33727.
RefSeqi NP_001076785.1. NM_001083316.1. [P26618-1 ]
NP_035188.2. NM_011058.2. [P26618-1 ]
XP_006504324.1. XM_006504261.1. [P26618-1 ]
XP_006504325.1. XM_006504262.1. [P26618-1 ]
XP_006504326.1. XM_006504263.1. [P26618-1 ]
UniGenei Mm.221403.

3D structure databases

ProteinModelPortali P26618.
SMRi P26618. Positions 28-507, 553-997.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202088. 1 interaction.
IntActi P26618. 3 interactions.
MINTi MINT-4107325.

Chemistry

BindingDBi P26618.
ChEMBLi CHEMBL2096980.

PTM databases

PhosphoSitei P26618.

Proteomic databases

PaxDbi P26618.
PRIDEi P26618.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000476 ; ENSMUSP00000000476 ; ENSMUSG00000029231 . [P26618-1 ]
ENSMUST00000168162 ; ENSMUSP00000127173 ; ENSMUSG00000029231 . [P26618-1 ]
GeneIDi 18595.
KEGGi mmu:18595.
UCSCi uc008xub.1. mouse. [P26618-2 ]
uc008xuc.1. mouse. [P26618-1 ]

Organism-specific databases

CTDi 5156.
MGIi MGI:97530. Pdgfra.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118923.
HOGENOMi HOG000112009.
HOVERGENi HBG004335.
InParanoidi P26618.
KOi K04363.
OMAi DYECAAR.
OrthoDBi EOG71G9T1.
PhylomeDBi P26618.
TreeFami TF325768.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.
Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_226341. PIP3 activates AKT signaling.
REACT_230639. Downstream signal transduction.
REACT_263353. Signaling by PDGF.

Miscellaneous databases

ChiTaRSi Pdgfra. mouse.
NextBioi 294480.
PROi P26618.
SOURCEi Search...

Gene expression databases

Bgeei P26618.
ExpressionAtlasi P26618. baseline and differential.
Genevestigatori P26618.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR027290. PDGFRA.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view ]
PANTHERi PTHR24416:SF52. PTHR24416:SF52. 1 hit.
Pfami PF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF500950. Alpha-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTi SM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
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Publicationsi

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  1. "Retinoic acid promotes transcription of the platelet-derived growth factor alpha-receptor gene."
    Stiles C.D., Wang C.
    Mol. Cell. Biol. 10:6781-6784(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Mouse platelet-derived growth factor alpha receptor: sequence, tissue-specific expression and correlation with metastatic phenotype."
    Do M.S., Fitzer-Attas C., Gubbay J., Greenfeld L., Feldman M., Eisenbach L.
    Oncogene 7:1567-1575(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Colon, Embryonic head and Placenta.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  5. "The PDGF alpha receptor is required for neural crest cell development and for normal patterning of the somites."
    Soriano P.
    Development 124:2691-2700(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  6. "Abnormal gastrointestinal development in PDGF-A and PDGFR-(alpha) deficient mice implicates a novel mesenchymal structure with putative instructive properties in villus morphogenesis."
    Karlsson L., Lindahl P., Heath J.K., Betsholtz C.
    Development 127:3457-3466(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. "Platelet-derived growth factor-mediated signaling through the Shb adaptor protein: effects on cytoskeletal organization."
    Hooshmand-Rad R., Lu L., Heldin C.-H., Claesson-Welsh L., Welsh M.
    Exp. Cell Res. 257:245-254(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHB.
  8. "Obstructive uropathy in mice and humans: potential role for PDGF-D in the progression of tubulointerstitial injury."
    Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G., Ophascharoensuk V., Truong L., Johnson R.J., Alpers C.E.
    J. Am. Soc. Nephrol. 14:2544-2555(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Insight into the physiological functions of PDGF through genetic studies in mice."
    Betsholtz C.
    Cytokine Growth Factor Rev. 15:215-228(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION, DISRUPTION PHENOTYPE.
  10. "Comprehensive dissection of PDGF-PDGFR signaling pathways in PDGFR genetically defined cells."
    Wu E., Palmer N., Tian Z., Moseman A.P., Galdzicki M., Wang X., Berger B., Zhang H., Kohane I.S.
    PLoS ONE 3:E3794-E3794(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Directional cell migration and chemotaxis in wound healing response to PDGF-AA are coordinated by the primary cilium in fibroblasts."
    Schneider L., Cammer M., Lehman J., Nielsen S.K., Guerra C.F., Veland I.R., Stock C., Hoffmann E.K., Yoder B.K., Schwab A., Satir P., Christensen S.T.
    Cell. Physiol. Biochem. 25:279-292(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPGFRA_MOUSE
AccessioniPrimary (citable) accession number: P26618
Secondary accession number(s): Q3TQ37
, Q62046, Q7TSJ3, Q8C4N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 26, 2008
Last modified: November 26, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3