A0A1S3EJP8 · A0A1S3EJP8_DIPOR

Function

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.

Catalytic activity

Activity 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.

Features

Showing features for binding site, active site, site.

110891002003004005006007008009001,000
Type
IDPosition(s)Description
Binding site572Mg2+ (UniProtKB | ChEBI)
Binding site599-607ATP (UniProtKB | ChEBI)
Binding site600-607ATP (UniProtKB | ChEBI)
Binding site627ATP (UniProtKB | ChEBI)
Binding site675-681ATP (UniProtKB | ChEBI)
Active site818Proton acceptor
Binding site822ATP (UniProtKB | ChEBI)
Binding site823Mg2+ (UniProtKB | ChEBI)
Binding site836Mg2+ (UniProtKB | ChEBI)
Site962Important for interaction with phosphotyrosine-binding proteins

GO annotations

AspectTerm
Cellular Componentcell junction
Cellular Componentcilium
Cellular Componentexternal side of plasma membrane
Cellular ComponentGolgi apparatus
Cellular Componentmicrovillus
Cellular Componentnucleoplasm
Cellular Componentreceptor complex
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionphospholipase C activator activity
Molecular Functionplatelet-derived growth factor alpha-receptor activity
Molecular Functionplatelet-derived growth factor binding
Molecular Functionplatelet-derived growth factor receptor binding
Molecular Functionprotein homodimerization activity
Molecular Functionprotein-containing complex binding
Molecular Functionvascular endothelial growth factor binding
Molecular Functionvascular endothelial growth factor receptor activity
Biological Processadrenal gland development
Biological Processcardiac myofibril assembly
Biological Processcell chemotaxis
Biological Processcellular response to amino acid stimulus
Biological Processcellular response to reactive oxygen species
Biological Processembryonic cranial skeleton morphogenesis
Biological Processembryonic digestive tract morphogenesis
Biological Processestrogen metabolic process
Biological Processextracellular matrix organization
Biological Processface morphogenesis
Biological Processhematopoietic progenitor cell differentiation
Biological Processin utero embryonic development
Biological ProcessLeydig cell differentiation
Biological Processlung development
Biological Processluteinization
Biological Processmale genitalia development
Biological Processmetanephric glomerular capillary formation
Biological Processnegative regulation of platelet activation
Biological Processodontogenesis of dentin-containing tooth
Biological Processpeptidyl-tyrosine phosphorylation
Biological Processplatelet aggregation
Biological Processpositive regulation of calcium-mediated signaling
Biological Processpositive regulation of cell migration
Biological Processpositive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway
Biological Processpositive regulation of chemotaxis
Biological Processpositive regulation of ERK1 and ERK2 cascade
Biological Processpositive regulation of fibroblast proliferation
Biological Processpositive regulation of kinase activity
Biological Processprotein autophosphorylation
Biological Processregulation of mesenchymal stem cell differentiation
Biological Processretina vasculature development in camera-type eye
Biological Processroof of mouth development
Biological Processsignal transduction involved in regulation of gene expression
Biological Processwhite fat cell differentiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Platelet-derived growth factor receptor alpha
  • EC number
  • Short names
    PDGF-R-alpha
    ; PDGFR-alpha
  • Alternative names
    • Alpha platelet-derived growth factor receptor
    • Alpha-type platelet-derived growth factor receptor

Gene names

    • Name
      Pdgfra

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Castorimorpha > Heteromyidae > Dipodomyinae > Dipodomys

Accessions

  • Primary accession
    A0A1S3EJP8

Proteomes

Subcellular Location

Cell membrane
; Single-pass type I membrane protein
Membrane
; Single-pass type I membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane525-549Helical

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-23
ChainPRO_501020071824-1089Platelet-derived growth factor receptor alpha
Disulfide bond49↔100
Disulfide bond150↔189
Disulfide bond235↔290
Disulfide bond435↔501

Keywords

Interaction

Subunit

Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound ligand.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain28-113Ig-like
Domain228-306Ig-like
Domain593-954Protein kinase
Region1018-1089Disordered
Compositional bias1029-1044Basic and acidic residues
Compositional bias1045-1060Polar residues

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,089
  • Mass (Da)
    122,692
  • Last updated
    2017-04-12 v1
  • Checksum
    CD70F514F894C9EC
MGTSHQAFLVFGCLLTGPSLIFCQVSLPSILPNENEKVVQLNSSFTLRCFGESEVSWQYPMFEEENPSVEIRNEENNSGLFVTVLEVVGASAAHTGLYTCYYNHTQTEESEIEGRDIYIFVPDPDVAFVPLGMMDSLVIVEEDDSAIIPCRTTDPETPVILRNSDGLVPASYDSRQGFNGTFSMGPYICEATVQGRTFQSTQFNVYALKATSELDLEMEALKTVYKSGETVVVTCAVFNNEVVDLQWAYPGEVKGKGITMLEEIKVPAIKLVYTLTVPDATVKDSGDYECTARQATKEVKEMKKVTISVHEKGFVEIKPTFGQLEAVNLHEVKHFVVEVQAYPPPRISWLKDNSTLIENLTEITTDVEKIQEIRYRSKLKLIRAKEEDSGHYTVIVQNEDDVKSYTFELLTQVPSSILELVDDHHASGGGQTVRCMARGVPLPDVEWMICKDIKKCNNETSWTFLANNVSNILTEIHPRDKSTVEGRVTFAKVEETIAVRCLAKNLLGTGNRELKLVAPTLRSELTVAAAVLVLLVIVIISLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSQSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFLSHHPEKPKKELDIFGLKPTDESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSVLDSEVKNLLSDDNSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVQCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGSLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1S3EJM5A0A1S3EJM5_DIPORPdgfra1054

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1029-1044Basic and acidic residues
Compositional bias1045-1060Polar residues

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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