Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Platelet-derived growth factor subunit A

Gene

PDGFA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB (By similarity).By similarity

GO - Molecular functioni

  • collagen binding Source: MGI
  • growth factor activity Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
  • platelet-derived growth factor binding Source: BHF-UCL
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • angiogenesis Source: UniProtKB
  • animal organ morphogenesis Source: UniProtKB
  • cell activation Source: BHF-UCL
  • cell-cell signaling Source: ProtInc
  • cell projection assembly Source: UniProtKB
  • embryonic lung development Source: BHF-UCL
  • extracellular matrix organization Source: Reactome
  • hair follicle development Source: UniProtKB
  • lung alveolus development Source: UniProtKB
  • MAPK cascade Source: Reactome
  • negative chemotaxis Source: BHF-UCL
  • negative regulation of phosphatidylinositol biosynthetic process Source: BHF-UCL
  • negative regulation of platelet activation Source: BHF-UCL
  • phosphatidylinositol-mediated signaling Source: Reactome
  • platelet degranulation Source: Reactome
  • platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of DNA replication Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: BHF-UCL
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of mesenchymal cell proliferation Source: UniProtKB
  • positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of protein autophosphorylation Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: BHF-UCL
  • regulation of branching involved in salivary gland morphogenesis by epithelial-mesenchymal signaling Source: UniProtKB
  • regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • regulation of smooth muscle cell migration Source: BHF-UCL
  • response to wounding Source: BHF-UCL
  • skin development Source: UniProtKB
  • wound healing Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Enzyme and pathway databases

BioCyciZFISH:G66-33143-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-186763. Downstream signal transduction.
R-HSA-186797. Signaling by PDGF.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLinkiP04085.
SIGNORiP04085.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-derived growth factor subunit A
Short name:
PDGF subunit A
Alternative name(s):
PDGF-1
Platelet-derived growth factor A chain
Platelet-derived growth factor alpha polypeptide
Gene namesi
Name:PDGFA
Synonyms:PDGF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:8799. PDGFA.

Subcellular locationi

  • Secreted

  • Note: Released by platelets upon wounding.

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • Golgi membrane Source: Reactome
  • microvillus Source: UniProtKB
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi5154.
OpenTargetsiENSG00000197461.
PharmGKBiPA33144.

Chemistry databases

ChEMBLiCHEMBL3137294.

Polymorphism and mutation databases

BioMutaiPDGFA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
PropeptideiPRO_000002335621 – 86Removed in mature formAdd BLAST66
ChainiPRO_000002335787 – 211Platelet-derived growth factor subunit AAdd BLAST125

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi96 ↔ 1401 Publication
Disulfide bondi123Interchain1 Publication
Disulfide bondi129 ↔ 1771 Publication
Disulfide bondi132Interchain1 Publication
Disulfide bondi133 ↔ 1791 Publication
Glycosylationi134N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP04085.
PeptideAtlasiP04085.
PRIDEiP04085.

PTM databases

iPTMnetiP04085.
PhosphoSitePlusiP04085.

Expressioni

Gene expression databases

BgeeiENSG00000197461.
CleanExiHS_PDGFA.
ExpressionAtlasiP04085. baseline and differential.
GenevisibleiP04085. HS.

Organism-specific databases

HPAiCAB005579.

Interactioni

Subunit structurei

Homodimer; antiparallel disulfide-linked dimer. Heterodimer with PDGFB; antiparallel disulfide-linked dimer. The PDGFA homodimer interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts with CSPG4.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDGFRAP162346EBI-2881386,EBI-2861522

GO - Molecular functioni

  • collagen binding Source: MGI
  • growth factor activity Source: UniProtKB
  • platelet-derived growth factor binding Source: BHF-UCL
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi111180. 11 interactors.
DIPiDIP-5735N.
IntActiP04085. 4 interactors.
STRINGi9606.ENSP00000346508.

Chemistry databases

BindingDBiP04085.

Structurei

Secondary structure

1211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 34Combined sources8
Helixi41 – 47Combined sources7
Beta strandi96 – 104Combined sources9
Helixi107 – 109Combined sources3
Beta strandi118 – 130Combined sources13
Beta strandi134 – 181Combined sources48

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MJKX-ray2.40A/B/E/F/X/Y21-181[»]
ProteinModelPortaliP04085.
SMRiP04085.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04085.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 162Receptor binding siteSequence analysis5

Domaini

The long form contains a basic insert which acts as a cell retention signal.

Sequence similaritiesi

Belongs to the PDGF/VEGF growth factor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IEXJ. Eukaryota.
ENOG4111GMH. LUCA.
GeneTreeiENSGT00510000046755.
HOGENOMiHOG000286027.
HOVERGENiHBG053546.
InParanoidiP04085.
KOiK04359.
OMAiHLECTCA.
OrthoDBiEOG091G0LNU.
PhylomeDBiP04085.
TreeFamiTF319554.

Family and domain databases

CDDicd00135. PDGF. 1 hit.
Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
IPR006782. PDGF_N.
[Graphical view]
PfamiPF00341. PDGF. 1 hit.
PF04692. PDGF_N. 1 hit.
[Graphical view]
SMARTiSM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P04085-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRTLACLLLL GCGYLAHVLA EEAEIPREVI ERLARSQIHS IRDLQRLLEI
60 70 80 90 100
DSVGSEDSLD TSLRAHGVHA TKHVPEKRPL PIRRKRSIEE AVPAVCKTRT
110 120 130 140 150
VIYEIPRSQV DPTSANFLIW PPCVEVKRCT GCCNTSSVKC QPSRVHHRSV
160 170 180 190 200
KVAKVEYVRK KPKLKEVQVR LEEHLECACA TTSLNPDYRE EDTGRPRESG
210
KKRKRKRLKP T
Length:211
Mass (Da):24,043
Last modified:November 1, 1986 - v1
Checksum:i48633DDE558EFA43
GO
Isoform Short (identifier: P04085-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     194-196: GRP → DVR
     197-211: Missing.

Show »
Length:196
Mass (Da):22,253
Checksum:i5EDBDB62D565904B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64 – 66RAH → TRD in AAA60045 (PubMed:2832727).Curated3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004602194 – 196GRP → DVR in isoform Short. 1 Publication3
Alternative sequenceiVSP_004603197 – 211Missing in isoform Short. 1 PublicationAdd BLAST15

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03795 mRNA. Translation: CAA27421.1.
X06374 mRNA. Translation: CAA29677.1.
M20494
, M20488, M20489, M20490, M20491, M20492, M20493 Genomic DNA. Translation: AAA60045.1.
M19988
, M21571, M19984, M19985, M19986, M19987 Genomic DNA. Translation: AAA60046.1.
M19989
, M21571, M19984, M19985, M19986, M19987 Genomic DNA. Translation: AAA60047.1.
AB451309 mRNA. Translation: BAG70123.1.
AB451439 mRNA. Translation: BAG70253.1.
AC147651 Genomic DNA. No translation available.
S62078 Genomic DNA. Translation: AAB26566.1.
CCDSiCCDS34578.1. [P04085-1]
CCDS47524.1. [P04085-2]
PIRiA28964. PFHUG1.
B28964.
RefSeqiNP_002598.4. NM_002607.5. [P04085-1]
NP_148983.1. NM_033023.4. [P04085-2]
UniGeneiHs.535898.

Genome annotation databases

EnsembliENST00000354513; ENSP00000346508; ENSG00000197461. [P04085-1]
ENST00000402802; ENSP00000383889; ENSG00000197461. [P04085-2]
GeneIDi5154.
KEGGihsa:5154.
UCSCiuc003sir.4. human. [P04085-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03795 mRNA. Translation: CAA27421.1.
X06374 mRNA. Translation: CAA29677.1.
M20494
, M20488, M20489, M20490, M20491, M20492, M20493 Genomic DNA. Translation: AAA60045.1.
M19988
, M21571, M19984, M19985, M19986, M19987 Genomic DNA. Translation: AAA60046.1.
M19989
, M21571, M19984, M19985, M19986, M19987 Genomic DNA. Translation: AAA60047.1.
AB451309 mRNA. Translation: BAG70123.1.
AB451439 mRNA. Translation: BAG70253.1.
AC147651 Genomic DNA. No translation available.
S62078 Genomic DNA. Translation: AAB26566.1.
CCDSiCCDS34578.1. [P04085-1]
CCDS47524.1. [P04085-2]
PIRiA28964. PFHUG1.
B28964.
RefSeqiNP_002598.4. NM_002607.5. [P04085-1]
NP_148983.1. NM_033023.4. [P04085-2]
UniGeneiHs.535898.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MJKX-ray2.40A/B/E/F/X/Y21-181[»]
ProteinModelPortaliP04085.
SMRiP04085.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111180. 11 interactors.
DIPiDIP-5735N.
IntActiP04085. 4 interactors.
STRINGi9606.ENSP00000346508.

Chemistry databases

BindingDBiP04085.
ChEMBLiCHEMBL3137294.

PTM databases

iPTMnetiP04085.
PhosphoSitePlusiP04085.

Polymorphism and mutation databases

BioMutaiPDGFA.

Proteomic databases

PaxDbiP04085.
PeptideAtlasiP04085.
PRIDEiP04085.

Protocols and materials databases

DNASUi5154.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354513; ENSP00000346508; ENSG00000197461. [P04085-1]
ENST00000402802; ENSP00000383889; ENSG00000197461. [P04085-2]
GeneIDi5154.
KEGGihsa:5154.
UCSCiuc003sir.4. human. [P04085-1]

Organism-specific databases

CTDi5154.
DisGeNETi5154.
GeneCardsiPDGFA.
H-InvDBHIX0167622.
HGNCiHGNC:8799. PDGFA.
HPAiCAB005579.
MIMi173430. gene.
neXtProtiNX_P04085.
OpenTargetsiENSG00000197461.
PharmGKBiPA33144.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEXJ. Eukaryota.
ENOG4111GMH. LUCA.
GeneTreeiENSGT00510000046755.
HOGENOMiHOG000286027.
HOVERGENiHBG053546.
InParanoidiP04085.
KOiK04359.
OMAiHLECTCA.
OrthoDBiEOG091G0LNU.
PhylomeDBiP04085.
TreeFamiTF319554.

Enzyme and pathway databases

BioCyciZFISH:G66-33143-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-186763. Downstream signal transduction.
R-HSA-186797. Signaling by PDGF.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLinkiP04085.
SIGNORiP04085.

Miscellaneous databases

EvolutionaryTraceiP04085.
GeneWikiiPDGFA.
GenomeRNAii5154.
PROiP04085.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197461.
CleanExiHS_PDGFA.
ExpressionAtlasiP04085. baseline and differential.
GenevisibleiP04085. HS.

Family and domain databases

CDDicd00135. PDGF. 1 hit.
Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
IPR006782. PDGF_N.
[Graphical view]
PfamiPF00341. PDGF. 1 hit.
PF04692. PDGF_N. 1 hit.
[Graphical view]
SMARTiSM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDGFA_HUMAN
AccessioniPrimary (citable) accession number: P04085
Secondary accession number(s): B5BU73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: November 30, 2016
This is version 177 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.