Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P26619 (PGFRA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Gene names
Name:pdgfra
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length1087 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. 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.

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 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 By similarity.

Subcellular location

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

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 By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 10871063Platelet-derived growth factor receptor alpha
PRO_0000016763

Regions

Topological domain25 – 530506Extracellular Potential
Transmembrane531 – 55121Helical; Potential
Topological domain552 – 1087536Cytoplasmic Potential
Domain27 – 11488Ig-like C2-type 1
Domain118 – 21194Ig-like C2-type 2
Domain217 – 30993Ig-like C2-type 3
Domain315 – 40995Ig-like C2-type 4
Domain417 – 519103Ig-like C2-type 5
Domain595 – 970376Protein kinase
Nucleotide binding601 – 6099ATP By similarity

Sites

Active site8181Proton acceptor By similarity
Binding site6291ATP By similarity

Amino acid modifications

Modified residue5741Phosphotyrosine; by autocatalysis By similarity
Modified residue5761Phosphotyrosine; by autocatalysis By similarity
Modified residue7221Phosphotyrosine; by autocatalysis By similarity
Modified residue7331Phosphotyrosine; by autocatalysis By similarity
Modified residue7441Phosphotyrosine; by autocatalysis By similarity
Modified residue7561Phosphotyrosine; by autocatalysis By similarity
Modified residue7641Phosphotyrosine; by autocatalysis By similarity
Modified residue8491Phosphotyrosine; by autocatalysis By similarity
Modified residue9881Phosphotyrosine; by autocatalysis By similarity
Modified residue10171Phosphotyrosine; by autocatalysis By similarity
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation2821N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Glycosylation4711N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 101 By similarity
Disulfide bond151 ↔ 192 By similarity
Disulfide bond238 ↔ 293 By similarity
Disulfide bond438 ↔ 503 By similarity

Sequences

Sequence LengthMass (Da)Tools
P26619 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: A621E6B0A5BADCA6

FASTA1,087122,699
        10         20         30         40         50         60 
MMPAMRASLI LGCLLIIGPW AILAENPLPT IFPDKDELVQ ALHSSFTLKC TGESEVSWQN 

        70         80         90        100        110        120 
PNSNPEKQNV VIRSEENNSG LFVSILEVSD ASAFDTGLYT CYHNHTQTEE SEIEGTDIYI 

       130        140        150        160        170        180 
YVPDPNVPFA PPGLFDHIIV VEEDESALVP CRTTDPSSEV TLKNIESSRT VFAFYDSKQG 

       190        200        210        220        230        240 
FAGNFPPGSY ICETTSNKMV YQTEPYILQT WKATHNISVE MEAPKTMFRA GETIAIDCIV 

       250        260        270        280        290        300 
LDNEVVDLKW TYPGKQRGVG IRNVEESKVP YQRLVYTLTL ANATTEDSGE YECAVIHATL 

       310        320        330        340        350        360 
DNRVVKKTNI TVHEKGFIDL EPMFGSEEFA NLHEVKSFIV NLHAYPTPGL FWLKDNRTLS 

       370        380        390        400        410        420 
ENLTEITTSI VTTKETRFQS KLKLIRAKEE DSGLYTLVAQ NDRETKSYSF ILQIKVPALI 

       430        440        450        460        470        480 
LELVDKHHGA SGEQTVGCLA KGMPVPDVEW LVCKDIKRCN NDTLWSILAT NGSEISMETH 

       490        500        510        520        530        540 
QDDEQIESQV TFKKIEETMA IRCIAKNELG VVARELKLVA PTLRSELTVA AAVLVLLVIV 

       550        560        570        580        590        600 
IISLIVLVII WKQKPRYEIR WRVIESISPD GHEYIYVDPM QLPYDSRWEF PRDGLVLGRI 

       610        620        630        640        650        660 
LGSGAFGKVV EGAAYGLSRS QPVMKVAVKM LKPTARSSEK QALMSELKIM THLGAHLNIV 

       670        680        690        700        710        720 
NLLGACTKSG PIYIITEYCF YGDLVNYLHK NRDNFQSRHP EKPKKDLDIF GLNPADESTR 

       730        740        750        760        770        780 
SYVILSFENN GDYMDMKQAD TMQYVPMLEM KEPSKYSDIQ RSLYDRPASY KKKPLSEVKN 

       790        800        810        820        830        840 
ILSDDGFEGL TVLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAHGK IVKICDFGLA 

       850        860        870        880        890        900 
RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS FGILLWEIFS LGGTPYPGMI 

       910        920        930        940        950        960 
VDSTFYNKIK SGYRMAKPDH ATHEVYDIMV KCWNSEPEKR PSFRHLSDIV ESLLPMEYKR 

       970        980        990       1000       1010       1020 
CYETVLHDFL KSDHPAVTRM RSDSDNSYIG VTYKNEHKMK DRESGFDEQR LSADSGYIIP 

      1030       1040       1050       1060       1070       1080 
LPDIDPVSED ESGKRNRHSS QTSEESAIET GSSSSTFIKR DDETIEDIDM MDDIGIDSSD 


LVEDSFL 

« Hide

References

[1]"The Xenopus platelet-derived growth factor alpha receptor: cDNA cloning and demonstration that mesoderm induction establishes the lineage-specific pattern of ligand and receptor gene expression."
Jones S.D., Ho L., Smith J.C., Yordan C., Stiles C.D., Mercola M.
Dev. Genet. 14:185-193(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80798 mRNA. Translation: AAA49929.1.
PIRI51552.
UniGeneXl.20029.

3D structure databases

ProteinModelPortalP26619.
SMRP26619. Positions 553-695, 785-951.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-6072934. pdgfra.

Phylogenomic databases

HOVERGENHBG004335.

Enzyme and pathway databases

BRENDA2.7.10.1. 6726.

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.
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. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF500950. Alpha-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTSM00409. IG. 2 hits.
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...

Entry information

Entry namePGFRA_XENLA
AccessionPrimary (citable) accession number: P26619
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 108 of the entry and version 1 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