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CD140a; PDGF-R-alpha; alpha-type platelet-derived growth factor receptor; CD140 antigen-like family member A; CD140a antigen (PDGFRA)
Function:
- cell surface receptor
- binds both PDGFA & PDGFB
- has tyrosine-protein kinase activity
- homodimer, & heterodimer with PDGFRB
- interacts with SH2 domain of SHB via phosphorylated Tyr-720 (putative)
- interacts with SH2 domain of SHF via phosphorylated Tyr-720
Structure:
- belongs to the protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
- contains 5 Ig-like C2-type domain (immunoglobulin-like) domains
- contains 1 protein kinase domain
Compartment: membrane
Alternative splicing: named isoforms=2
Pathology:
- fusion of PDGFRA & FIP1L1 (FIP1L1-PDGFRA), due to an interstitial chromosomal deletion, is the cause of some cases of hypereosinophilic syndrome
Pharmacology:
- olaratumab (Lartruvo), a PDGFRA inhibitor, used in combination with doxorubicin for treatment of advanced soft tissue sarcomas
Related
PDGF receptor alpha (PDGFRA) gene mutation
PDGFR-alpha Ag in tissue
PDGFRA gene rearrangement
General
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
oligomerizing protein
platelet-derived growth factor [PDGF] receptor
Properties
SIZE: entity length = 1089 aa
MW = 123 kD
COMPARTMENT: cellular membrane
STATE: active state
MOTIF: signal sequence {1-23}
immunoglobulin superfamily domain {24-113}
MOTIF: N-glycosylation site {N42}
cysteine residue {C49}
MODIFICATION: cysteine residue {C100}
N-glycosylation site {N76}
cysteine residue {C100}
MODIFICATION: cysteine residue {C49}
N-glycosylation site {N103}
immunoglobulin superfamily domain {117-201}
MOTIF: cysteine residue {C150}
MODIFICATION: cysteine residue {C189}
N-glycosylation site {N179}
cysteine residue {C189}
MODIFICATION: cysteine residue {C150}
immunoglobulin superfamily domain {202-306}
MOTIF: cysteine residue {C235}
MODIFICATION: cysteine residue {C290}
cysteine residue {C290}
MODIFICATION: cysteine residue {C235}
immunoglobulin superfamily domain {319-410}
MOTIF: N-glycosylation site {N353}
N-glycosylation site {N359}
immunoglobulin superfamily domain {414-517}
MOTIF: cysteine residue {C435}
MODIFICATION: cysteine residue {C501}
N-glycosylation site {N458}
N-glycosylation site {N468}
cysteine residue {C501}
MODIFICATION: cysteine residue {C435}
transmembrane domain {525-549}
breakpoint {578-579}
kinase domain
SITE: 593-954
MOTIF: ATP-binding site
NAME: ATP-binding site
SITE: 599-607
ATP-binding site
NAME: ATP-binding site
SITE: 627-627
Tyr phosphorylation site {Y720}
Tyr phosphorylation site {Y762}
Tyr phosphorylation site {Y768}
aspartate residue {D818}
Tyr phosphorylation site {Y849}
Tyr phosphorylation site {Y1018}
serine-rich region {1041-1087}
MOTIF: serine residue (SEVERAL)
Database Correlations
OMIM correlations
MORBIDMAP 173490
UniProt P16234
PFAM correlations
Kegg hsa:5156
References
- UniProt :accession P16234
- Cross M, Dexter TM.
Growth factors in development, transformation, and tumorigenesis.
Cell. 1991 Jan 25;64(2):271-80. Review.
PMID: 1988148
Component-of
PDGF receptor-alpha/beta