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Protein

Platelet-derived growth factor receptor alpha

Gene

pdgfra

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. 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 similarity

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)DescriptionActionsGraphical viewLength
Binding sitei629ATPPROSITE-ProRule annotation1
Active sitei818Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi601 – 609ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

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. 6725.

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
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 530ExtracellularSequence analysisAdd BLAST506
Transmembranei531 – 551HelicalSequence analysisAdd BLAST21
Topological domaini552 – 1087CytoplasmicSequence analysisAdd BLAST536

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000001676325 – 1087Platelet-derived growth factor receptor alphaAdd BLAST1063

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 101PROSITE-ProRule annotation
Glycosylationi77N-linked (GlcNAc...)Sequence analysis1
Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi151 ↔ 192PROSITE-ProRule annotation
Glycosylationi216N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi238 ↔ 293PROSITE-ProRule annotation
Glycosylationi282N-linked (GlcNAc...)Sequence analysis1
Glycosylationi309N-linked (GlcNAc...)Sequence analysis1
Glycosylationi356N-linked (GlcNAc...)Sequence analysis1
Glycosylationi362N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi438 ↔ 503PROSITE-ProRule annotation
Glycosylationi461N-linked (GlcNAc...)Sequence analysis1
Glycosylationi471N-linked (GlcNAc...)Sequence analysis1
Modified residuei574Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei576Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei722Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei733Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei744Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei756Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei764Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei849Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei988Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1017Phosphotyrosine; by autocatalysisBy similarity1

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

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

Structurei

3D structure databases

ProteinModelPortaliP26619.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 114Ig-like C2-type 1Add BLAST88
Domaini118 – 211Ig-like C2-type 2Add BLAST94
Domaini217 – 309Ig-like C2-type 3Add BLAST93
Domaini315 – 409Ig-like C2-type 4Add BLAST95
Domaini417 – 519Ig-like C2-type 5Add BLAST103
Domaini595 – 970Protein kinasePROSITE-ProRule annotationAdd BLAST376

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

HOVERGENiHBG004335.

Family and domain databases

Gene3Di2.60.40.10. 5 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. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500950. Alpha-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00220. S_TKc. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. 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]

Sequencei

Sequence statusi: Complete.

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

P26619-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMPAMRASLI LGCLLIIGPW AILAENPLPT IFPDKDELVQ ALHSSFTLKC
60 70 80 90 100
TGESEVSWQN PNSNPEKQNV VIRSEENNSG LFVSILEVSD ASAFDTGLYT
110 120 130 140 150
CYHNHTQTEE SEIEGTDIYI YVPDPNVPFA PPGLFDHIIV VEEDESALVP
160 170 180 190 200
CRTTDPSSEV TLKNIESSRT VFAFYDSKQG FAGNFPPGSY ICETTSNKMV
210 220 230 240 250
YQTEPYILQT WKATHNISVE MEAPKTMFRA GETIAIDCIV LDNEVVDLKW
260 270 280 290 300
TYPGKQRGVG IRNVEESKVP YQRLVYTLTL ANATTEDSGE YECAVIHATL
310 320 330 340 350
DNRVVKKTNI TVHEKGFIDL EPMFGSEEFA NLHEVKSFIV NLHAYPTPGL
360 370 380 390 400
FWLKDNRTLS ENLTEITTSI VTTKETRFQS KLKLIRAKEE DSGLYTLVAQ
410 420 430 440 450
NDRETKSYSF ILQIKVPALI LELVDKHHGA SGEQTVGCLA KGMPVPDVEW
460 470 480 490 500
LVCKDIKRCN NDTLWSILAT NGSEISMETH QDDEQIESQV TFKKIEETMA
510 520 530 540 550
IRCIAKNELG VVARELKLVA PTLRSELTVA AAVLVLLVIV IISLIVLVII
560 570 580 590 600
WKQKPRYEIR WRVIESISPD GHEYIYVDPM QLPYDSRWEF PRDGLVLGRI
610 620 630 640 650
LGSGAFGKVV EGAAYGLSRS QPVMKVAVKM LKPTARSSEK QALMSELKIM
660 670 680 690 700
THLGAHLNIV NLLGACTKSG PIYIITEYCF YGDLVNYLHK NRDNFQSRHP
710 720 730 740 750
EKPKKDLDIF GLNPADESTR SYVILSFENN GDYMDMKQAD TMQYVPMLEM
760 770 780 790 800
KEPSKYSDIQ RSLYDRPASY KKKPLSEVKN ILSDDGFEGL TVLDLLSFTY
810 820 830 840 850
QVARGMEFLA SKNCVHRDLA ARNVLLAHGK IVKICDFGLA RDIMHDSNYV
860 870 880 890 900
SKGSTFLPVK WMAPESIFDN LYTTLSDVWS FGILLWEIFS LGGTPYPGMI
910 920 930 940 950
VDSTFYNKIK SGYRMAKPDH ATHEVYDIMV KCWNSEPEKR PSFRHLSDIV
960 970 980 990 1000
ESLLPMEYKR CYETVLHDFL KSDHPAVTRM RSDSDNSYIG VTYKNEHKMK
1010 1020 1030 1040 1050
DRESGFDEQR LSADSGYIIP LPDIDPVSED ESGKRNRHSS QTSEESAIET
1060 1070 1080
GSSSSTFIKR DDETIEDIDM MDDIGIDSSD LVEDSFL
Length:1,087
Mass (Da):122,699
Last modified:August 1, 1992 - v1
Checksum:iA621E6B0A5BADCA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80798 mRNA. Translation: AAA49929.1.
PIRiI51552.
UniGeneiXl.20029.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80798 mRNA. Translation: AAA49929.1.
PIRiI51552.
UniGeneiXl.20029.

3D structure databases

ProteinModelPortaliP26619.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004335.

Enzyme and pathway databases

BRENDAi2.7.10.1. 6725.

Family and domain databases

Gene3Di2.60.40.10. 5 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. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500950. Alpha-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00220. S_TKc. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPGFRA_XENLA
AccessioniPrimary (citable) accession number: P26619
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 30, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.