P26618 (PGFRA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1089 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Chemotaxis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from mutant phenotype PubMed 19056881. Source: MGI adrenal gland development Inferred from genetic interaction PubMed 19056881. Source: MGI cardiac myofibril assembly Inferred from genetic interaction PubMed 11239463. Source: UniProtKB cell chemotaxis Inferred from mutant phenotype Ref.11. Source: UniProtKB cellular response to amino acid stimulus Inferred from direct assay PubMed 20548288. Source: MGI elevation of cytosolic calcium ion concentration Inferred from sequence or structural similarity. Source: UniProtKB 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 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 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 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 by VEGF-activated platelet derived growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL 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: Compara protein autophosphorylation Inferred from direct assay Ref.11. Source: UniProtKB regulation of chemotaxis Inferred from electronic annotation. Source: Compara 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 vascular endothelial growth factor receptor signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB external side of plasma membrane Inferred from direct assay PubMed 17350578. Source: MGI integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 1089	1065	Platelet-derived growth factor receptor alpha		PRO_0000016761
Regions
	Topological domain	25 – 528	504	Extracellular Potential
	Transmembrane	529 – 549	21	Helical; Potential
	Topological domain	550 – 1089	540	Cytoplasmic Potential
	Domain	25 – 113	89	Ig-like C2-type 1
	Domain	117 – 201	85	Ig-like C2-type 2
	Domain	202 – 306	105	Ig-like C2-type 3
	Domain	319 – 410	92	Ig-like C2-type 4
	Domain	414 – 517	104	Ig-like C2-type 5
	Domain	593 – 954	362	Protein kinase
	Nucleotide binding	599 – 607	9	ATP By similarity
Sites
	Active site	818	1	Proton acceptor By similarity
	Binding site	627	1	ATP By similarity
Amino acid modifications
	Modified residue	555	1	Phosphotyrosine By similarity
	Modified residue	572	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	574	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	582	1	Phosphotyrosine By similarity
	Modified residue	720	1	Phosphotyrosine; by autocatalysis Probable
	Modified residue	731	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	742	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	754	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	762	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	768	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	849	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	944	1	Phosphotyrosine By similarity
	Modified residue	958	1	Phosphotyrosine By similarity
	Modified residue	962	1	Phosphotyrosine By similarity
	Modified residue	988	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	993	1	Phosphotyrosine By similarity
	Modified residue	1018	1	Phosphotyrosine; by autocatalysis
	Glycosylation	42	1	N-linked (GlcNAc...) Potential
	Glycosylation	76	1	N-linked (GlcNAc...) Potential
	Glycosylation	89	1	N-linked (GlcNAc...) Potential
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	179	1	N-linked (GlcNAc...) Potential
	Glycosylation	353	1	N-linked (GlcNAc...) Potential
	Glycosylation	359	1	N-linked (GlcNAc...) Potential
	Glycosylation	458	1	N-linked (GlcNAc...) Potential
	Glycosylation	468	1	N-linked (GlcNAc...) Potential
	Glycosylation	506	1	N-linked (GlcNAc...) Potential
	Disulfide bond	49 ↔ 100		By similarity
	Disulfide bond	150 ↔ 189		By similarity
	Disulfide bond	235 ↔ 290		By similarity
	Disulfide bond	435 ↔ 501		By similarity
Natural variations
	Alternative sequence	775 – 790	16	DSEVK…DSEGL → GKSAHAHSGKYDLSVV in isoform 2.		VSP_031877
	Alternative sequence	791 – 1089	299	Missing in isoform 2.		VSP_031878
Experimental info
	Sequence conflict	65	1	D → E in AAA39733. Ref.1
	Sequence conflict	65	1	D → E in AAA39904. Ref.2
	Sequence conflict	192	1	T → A in AAA39733. Ref.1
	Sequence conflict	202	1	E → A in AAA39733. Ref.1
	Sequence conflict	252	1	E → G in AAA39733. Ref.1
	Sequence conflict	271	1	L → V in AAA39733. Ref.1
	Sequence conflict	322	1	G → S in AAA39733. Ref.1
	Sequence conflict	326	1	A → P in AAA39733. Ref.1
	Sequence conflict	439 – 440	2	GT → EG in AAA39733. Ref.1
	Sequence conflict	472	1	I → V in BAE37548. Ref.3
	Sequence conflict	529	1	A → E in AAA39733. Ref.1
	Sequence conflict	737	1	A → D in AAA39733. Ref.1
	Sequence conflict	849	1	Y → D in AAA39733. Ref.1
	Sequence conflict	936	1	E → D in AAA39733. Ref.1
	Sequence conflict	950	1	V → L in AAA39733. Ref.1
	Sequence conflict	1005	1	G → S in AAA39904. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: 07AAFD2BAA12533A	FASTA	1,089	122,683
	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
	Isoform 2 [UniParc]. Checksum: FE13756876B68B95	FASTA	790	88,629
	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 KSMLGKSAHA 790 HSGKYDLSVV

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00844650. IPI00885559.
PIR	S33727. I57511.
RefSeq	NP_001076785.1. NM_001083316.1. NP_035188.2. NM_011058.2.
UniGene	Mm.221403.
3D structure databases
ProteinModelPortal	P26618.
SMR	P26618. Positions 28-507, 572-997.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4107325.
PTM databases
PhosphoSite	P26618.
Proteomic databases
PaxDb	P26618.
PRIDE	P26618.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000000476; ENSMUSP00000000476; ENSMUSG00000029231. ENSMUST00000168162; ENSMUSP00000127173; ENSMUSG00000029231.
GeneID	18595.
KEGG	mmu:18595.
UCSC	uc008xub.1. mouse. uc008xuc.1. mouse.
Organism-specific databases
CTD	5156.
MGI	MGI:97530. Pdgfra.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00660000095142.
HOGENOM	HOG000112009.
HOVERGEN	HBG004335.
InParanoid	P26618.
KO	K04363.
OMA	DLQWTYP.
OrthoDB	EOG4XWFX0.
Enzyme and pathway databases
BRENDA	2.7.10.1. 3474.
Gene expression databases
ArrayExpress	P26618.
Bgee	P26618.
Genevestigator	P26618.
GermOnline	ENSMUSG00000029231. Mus musculus.
Family and domain databases
Gene3D	2.60.40.10. 4 hits.
InterPro	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_cat_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. IPR009134. Tyr_kinase_VEGFR_rcpt_N. [Graphical view]
Pfam	PF07679. I-set. 2 hits. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PIRSF	PIRSF500950. Alpha-PDGF_receptor. 1 hit. PIRSF000615. TyrPK_CSF1-R. 1 hit.
PRINTS	PR01832. VEGFRECEPTOR.
SMART	SM00409. IG. 2 hits. SM00408. IGc2. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	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. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P26618.
ChEMBL	CHEMBL3466.
ChiTaRS	PDGFRA. mouse.
NextBio	294480.
SOURCE	Search...

Entry information

Entry name

PGFRA_MOUSE

Accession

Primary (citable) accession number: P26618
Secondary accession number(s): Q3TQ37 , Q62046, Q7TSJ3, Q8C4N3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 26, 2008
Last modified:	May 29, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program