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P26618 (PGFRA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet-derived growth factor receptor alpha

Short name=PDGF-R-alpha
Short name=PDGFR-alpha
EC=2.7.10.1
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 names
Name:Pdgfra
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1089 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.10 Ref.11

Catalytic activity

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

Enzyme regulation

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.

Subunit structure

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. Ref.7

Subcellular location

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

Tissue specificity

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. Ref.8

Post-translational modification

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.

Disruption phenotype

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. Ref.5 Ref.6 Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processLeydig cell differentiation

Inferred from mutant phenotype PubMed 19056881. Source: MGI

adrenal gland development

Inferred from genetic interaction PubMed 19056881. Source: MGI

anatomical structure morphogenesis

Inferred from mutant phenotype PubMed 15543606. Source: MGI

cardiac myofibril assembly

Inferred from genetic interaction PubMed 11239463. Source: UniProtKB

cell chemotaxis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.11. Source: UniProtKB

cellular response to amino acid stimulus

Inferred from direct assay PubMed 20548288. Source: MGI

embryonic cranial skeleton morphogenesis

Inferred from mutant phenotype Ref.5. Source: UniProtKB

embryonic digestive tract morphogenesis

Inferred from mutant phenotype Ref.6. Source: UniProtKB

estrogen metabolic process

Inferred from genetic interaction PubMed 19056881. Source: MGI

extracellular matrix organization

Inferred from mutant phenotype PubMed 15543606. Source: MGI

face morphogenesis

Inferred from mutant phenotype PubMed 17143286. Source: MGI

female gonad development

Inferred from genetic interaction PubMed 19056881. Source: MGI

hematopoietic progenitor cell differentiation

Inferred from mutant phenotype PubMed 24029230. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 10331973PubMed 17143286. Source: MGI

lung development

Inferred from mutant phenotype PubMed 11803579. Source: MGI

luteinization

Inferred from mutant phenotype PubMed 19056881. Source: MGI

male genitalia development

Inferred from mutant phenotype PubMed 12651897. Source: MGI

metanephric glomerular capillary formation

Inferred from genetic interaction PubMed 11239463. Source: UniProtKB

negative regulation of platelet activation

Inferred from sequence or structural similarity. Source: UniProtKB

odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 15543606. Source: MGI

organ morphogenesis

Inferred from mutant phenotype PubMed 10806482. Source: MGI

palate development

Inferred from mutant phenotype PubMed 17143286. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.11. Source: UniProtKB

phosphatidylinositol-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

platelet aggregation

Inferred from sequence or structural similarity. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 17143286. Source: MGI

platelet-derived growth factor receptor-alpha signaling pathway

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of DNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phospholipase C activity

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of chemotaxis

Inferred from electronic annotation. Source: Ensembl

regulation of mesenchymal stem cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

retina vasculature development in camera-type eye

Inferred from genetic interaction PubMed 11239463. Source: UniProtKB

signal transduction involved in regulation of gene expression

Inferred from direct assay PubMed 18462699. Source: MGI

skeletal system morphogenesis

Inferred from mutant phenotype PubMed 17143286. Source: MGI

wound healing

Inferred from mutant phenotype Ref.11. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay PubMed 22265737. Source: BHF-UCL

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

external side of plasma membrane

Inferred from direct assay PubMed 17350578. Source: MGI

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

microvillus

Inferred from direct assay PubMed 23266329. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

platelet-derived growth factor alpha-receptor activity

Inferred from direct assay Ref.11. Source: UniProtKB

platelet-derived growth factor binding

Inferred from direct assay Ref.11. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

vascular endothelial growth factor-activated receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P26618-1)

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.
Isoform 2 (identifier: P26618-2)

The sequence of this isoform differs from the canonical sequence as follows:
     775-790: DSEVKNLLSDDDSEGL → GKSAHAHSGKYDLSVV
     791-1089: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 10891065Platelet-derived growth factor receptor alpha
PRO_0000016761

Regions

Topological domain25 – 528504Extracellular Potential
Transmembrane529 – 54921Helical; Potential
Topological domain550 – 1089540Cytoplasmic Potential
Domain25 – 11389Ig-like C2-type 1
Domain117 – 20185Ig-like C2-type 2
Domain202 – 306105Ig-like C2-type 3
Domain319 – 41092Ig-like C2-type 4
Domain414 – 517104Ig-like C2-type 5
Domain593 – 954362Protein kinase
Nucleotide binding599 – 6079ATP By similarity

Sites

Active site8181Proton acceptor By similarity
Binding site6271ATP By similarity

Amino acid modifications

Modified residue5551Phosphotyrosine By similarity
Modified residue5721Phosphotyrosine; by autocatalysis By similarity
Modified residue5741Phosphotyrosine; by autocatalysis By similarity
Modified residue5821Phosphotyrosine By similarity
Modified residue7201Phosphotyrosine; by autocatalysis Probable
Modified residue7311Phosphotyrosine; by autocatalysis By similarity
Modified residue7421Phosphotyrosine; by autocatalysis By similarity
Modified residue7541Phosphotyrosine; by autocatalysis By similarity
Modified residue7621Phosphotyrosine; by autocatalysis By similarity
Modified residue7681Phosphotyrosine; by autocatalysis By similarity
Modified residue8491Phosphotyrosine; by autocatalysis By similarity
Modified residue9441Phosphotyrosine By similarity
Modified residue9581Phosphotyrosine By similarity
Modified residue9621Phosphotyrosine By similarity
Modified residue9881Phosphotyrosine; by autocatalysis By similarity
Modified residue9931Phosphotyrosine By similarity
Modified residue10181Phosphotyrosine; by autocatalysis
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation761N-linked (GlcNAc...) Potential
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential
Glycosylation4681N-linked (GlcNAc...) Potential
Glycosylation5061N-linked (GlcNAc...) Potential
Disulfide bond49 ↔ 100 By similarity
Disulfide bond150 ↔ 189 By similarity
Disulfide bond235 ↔ 290 By similarity
Disulfide bond435 ↔ 501 By similarity

Natural variations

Alternative sequence775 – 79016DSEVK…DSEGL → GKSAHAHSGKYDLSVV in isoform 2.
VSP_031877
Alternative sequence791 – 1089299Missing in isoform 2.
VSP_031878

Experimental info

Sequence conflict651D → E in AAA39733. Ref.1
Sequence conflict651D → E in AAA39904. Ref.2
Sequence conflict1921T → A in AAA39733. Ref.1
Sequence conflict2021E → A in AAA39733. Ref.1
Sequence conflict2521E → G in AAA39733. Ref.1
Sequence conflict2711L → V in AAA39733. Ref.1
Sequence conflict3221G → S in AAA39733. Ref.1
Sequence conflict3261A → P in AAA39733. Ref.1
Sequence conflict439 – 4402GT → EG in AAA39733. Ref.1
Sequence conflict4721I → V in BAE37548. Ref.3
Sequence conflict5291A → E in AAA39733. Ref.1
Sequence conflict7371A → D in AAA39733. Ref.1
Sequence conflict8491Y → D in AAA39733. Ref.1
Sequence conflict9361E → D in AAA39733. Ref.1
Sequence conflict9501V → L in AAA39733. Ref.1
Sequence conflict10051G → S in AAA39904. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: 07AAFD2BAA12533A

FASTA1,089122,683
        10         20         30         40         50         60 
MGTSHQVFLV LSCLLTGPGL ISCQLLLPSI LPNENEKIVQ LNSSFSLRCV GESEVSWQHP 

        70         80         90        100        110        120 
MSEEDDPNVE IRSEENNSGL FVTVLEVVNA SAAHTGWYTC YYNHTQTDES EIEGRHIYIY 

       130        140        150        160        170        180 
VPDPDMAFVP LGMTDSLVIV EEDDSAIIPC RTTDPETQVT LHNNGRLVPA SYDSRQGFNG 

       190        200        210        220        230        240 
TFSVGPYICE ATVKGRTFKT SEFNVYALKA TSELNLEMDA RQTVYKAGET IVVTCAVFNN 

       250        260        270        280        290        300 
EVVDLQWTYP GEVRNKGITM LEEIKLPSIK LVYTLTVPKA TVKDSGEYEC AARQATKEVK 

       310        320        330        340        350        360 
EMKRVTISVH EKGFVEIEPT FGQLEAVNLH EVREFVVEVQ AYPTPRISWL KDNLTLIENL 

       370        380        390        400        410        420 
TEITTDVQKS QETRYQSKLK LIRAKEEDSG HYTIIVQNED DVKSYTFELS TLVPASILDL 

       430        440        450        460        470        480 
VDDHHGSGGG QTVRCTAEGT PLPEIDWMIC KHIKKCNNDT SWTVLASNVS NIITELPRRG 

       490        500        510        520        530        540 
RSTVEGRVSF AKVEETIAVR CLAKNNLSVV ARELKLVAPT LRSELTVAAA VLVLLVIVIV 

       550        560        570        580        590        600 
SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG 

       610        620        630        640        650        660 
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL 

       670        680        690        700        710        720 
LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFMSQHPEK PKKDLDIFGL NPADESTRSY 

       730        740        750        760        770        780 
VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN 

       790        800        810        820        830        840 
LLSDDDSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA 

       850        860        870        880        890        900 
RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM 

       910        920        930        940        950        960 
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV QCWNSEPEKR PSFYHLSEIV ENLLPGQYKK 

       970        980        990       1000       1010       1020 
SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII 

      1030       1040       1050       1060       1070       1080 
PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS 


SDLVEDSFL 

« Hide

Isoform 2 [UniParc].

Checksum: FE13756876B68B95
Show »

FASTA79088,629

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS19351.1. [P26618-1]
PIRS33727. I57511.
RefSeqNP_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]
UniGeneMm.221403.

3D structure databases

ProteinModelPortalP26618.
SMRP26618. Positions 28-507, 553-997.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202088. 1 interaction.
IntActP26618. 3 interactions.
MINTMINT-4107325.

Chemistry

BindingDBP26618.
ChEMBLCHEMBL2096980.

PTM databases

PhosphoSiteP26618.

Proteomic databases

PaxDbP26618.
PRIDEP26618.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000476; ENSMUSP00000000476; ENSMUSG00000029231. [P26618-1]
ENSMUST00000168162; ENSMUSP00000127173; ENSMUSG00000029231. [P26618-1]
GeneID18595.
KEGGmmu:18595.
UCSCuc008xub.1. mouse. [P26618-2]
uc008xuc.1. mouse. [P26618-1]

Organism-specific databases

CTD5156.
MGIMGI:97530. Pdgfra.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108490.
HOGENOMHOG000112009.
HOVERGENHBG004335.
InParanoidP26618.
KOK04363.
OMADYECAAR.
OrthoDBEOG71G9T1.
PhylomeDBP26618.
TreeFamTF325768.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressP26618.
BgeeP26618.
GenevestigatorP26618.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR007110. 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]
PANTHERPTHR24416:SF52. PTHR24416:SF52. 1 hit.
PfamPF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF500950. Alpha-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. 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]
ProtoNetSearch...

Other

ChiTaRSPDGFRA. mouse.
NextBio294480.
PROP26618.
SOURCESearch...

Entry information

Entry namePGFRA_MOUSE
AccessionPrimary (citable) accession number: P26618
Secondary accession number(s): Q3TQ37 expand/collapse secondary AC list , Q62046, Q7TSJ3, Q8C4N3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 26, 2008
Last modified: July 9, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot