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Protein

Platelet-derived growth factor receptor alpha

Gene

PDGFRA

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Tyrosine-protein kinase that acts as 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. Required for normal development of the gastrointestinal tract. 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 (By similarity).By similarity1 Publication

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 (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

GO - Biological processi

  • chemotaxis Source: UniProtKB-KW
  • embryonic skeletal system morphogenesis 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

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
Gene namesi
Name:PDGFRA
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 528505ExtracellularSequence analysisAdd
BLAST
Transmembranei529 – 54921HelicalSequence analysisAdd
BLAST
Topological domaini550 – 1087538CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 10871064Platelet-derived growth factor receptor alphaPRO_0000248883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence analysis
Disulfide bondi49 ↔ 99PROSITE-ProRule annotation
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence analysis
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence analysis
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi149 ↔ 189PROSITE-ProRule annotation
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
Modified residuei572 – 5721Phosphotyrosine; by autocatalysisBy similarity
Modified residuei574 – 5741Phosphotyrosine; by autocatalysisBy similarity
Modified residuei720 – 7201Phosphotyrosine; by autocatalysisBy similarity
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 residuei988 – 9881Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1017 – 10171Phosphotyrosine; by autocatalysisBy similarity

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 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9PUF6.
PRIDEiQ9PUF6.

Expressioni

Developmental stagei

Expressed throughout the mesenchyme of early limb buds. At later stages, present in the condensing chondrogenic mesenchyme, then the perichondrium. Down-regulated in areas that will not give rise to cartilage and is then lost from cartilage forming areas after they begin to differentiate.1 Publication

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000009175.

Structurei

3D structure databases

ProteinModelPortaliQ9PUF6.
SMRiQ9PUF6. Positions 551-694, 787-951.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 10479Ig-like C2-type 1Add
BLAST
Domaini116 – 20893Ig-like C2-type 2Add
BLAST
Domaini213 – 312100Ig-like C2-type 3Add
BLAST
Domaini314 – 41198Ig-like C2-type 4Add
BLAST
Domaini414 – 517104Ig-like C2-type 5Add
BLAST
Domaini593 – 954362Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1052 – 10554Poly-Ser

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

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000112009.
HOVERGENiHBG004335.
InParanoidiQ9PUF6.
PhylomeDBiQ9PUF6.

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. 3 hits.
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. 4 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 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]

Sequencei

Sequence statusi: Complete.

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

Q9PUF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTPPRTFLI LGCFLTGPLL TLCQLPLPTI VPNRNEMVVQ LNSNFTLKCS
60 70 80 90 100
GDSEVSWQYP VTEGSHRIDI RHEENNSGLF VTVLEVGNAS AAHTGMYVCY
110 120 130 140 150
YNHTQVEDGE VEGKDIYIYV PDPDMPFVPS LPEDQFILVE EGDPTVIPCR
160 170 180 190 200
TSDPSAEVTL VNSLDKPVYA FYDSKQGFVG NFLAGPYTCK TMVKGVEFKS
210 220 230 240 250
DEFLIYILRA TSQLPVEIEA LKTVYKTGET IVVTCVVFDN EVVNLQWNYP
260 270 280 290 300
GKVKEKGLIK LDDIKVPSQK LVYMLTIPDV LVKDTGDYEC TARHATKEVK
310 320 330 340 350
ENKKVVITVH DKGFIHLEPQ FSPLEAVNLH EVKNFVVDVQ AYPAPKMYWL
360 370 380 390 400
KDNVTLIENL TEIVTSSNRV QETRFQSVLK LIRAKEEDSG TILWLLKNED
410 420 430 440 450
EIKRYTFSLL IQVPALILDL MDDHQGSAGR QTVRCLAEGT PLPDVEWLVC
460 470 480 490 500
KDIKKCSNDT SWTLLTNNIS DIHMEAHLDE RNMVESQVTF QKVEETLAVR
510 520 530 540 550
CVARNDLGAV TRELKLVAPT LRSELTVAAA VLVLLVIVII SLIVLVIIWK
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 DNFLSRHPEK
710 720 730 740 750
PKKDLDIFGM NPADESTRSY VILSFENTGE YMDMKQADTT QYVPMLERKE
760 770 780 790 800
GSKYSDIQRS VYDRPASYKK KSLSESEVKN LLSDDGSEGL SLLDLLSFTY
810 820 830 840 850
QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA RDIMHDSNYV
860 870 880 890 900
SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGILYPGMM
910 920 930 940 950
VDSTFYNKIK SGYRMAKPDH ATNEVYEIMV KCWNNEPEKR PSFYHLSEIV
960 970 980 990 1000
ESLLPGEYKK SYEKIHLDFL KSDHPAVTRM RGDCDNAYIG VTYKNEDKIK
1010 1020 1030 1040 1050
DRESGFDEQR LSADSGYITP LPDIDPVSED ELGKRNRHSS QTSEESAIET
1060 1070 1080
GSSSSTFIKR EDETIEDIDM MDDIGIDSSD LVEDSFL
Length:1,087
Mass (Da):122,941
Last modified:May 1, 2000 - v1
Checksum:iF3306BDD3D983E31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188842 mRNA. Translation: AAF01460.1.
UniGeneiGga.274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188842 mRNA. Translation: AAF01460.1.
UniGeneiGga.274.

3D structure databases

ProteinModelPortaliQ9PUF6.
SMRiQ9PUF6. Positions 551-694, 787-951.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000009175.

Proteomic databases

PaxDbiQ9PUF6.
PRIDEiQ9PUF6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000112009.
HOVERGENiHBG004335.
InParanoidiQ9PUF6.
PhylomeDBiQ9PUF6.

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. 3 hits.
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. 4 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPGFRA_CHICK
AccessioniPrimary (citable) accession number: Q9PUF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 108 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.