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Platelet-derived growth factor subunit A (PDGF subunit A) (PDGF-1) (Platelet-derived growth factor A chain) (Platelet-derived growth factor alpha polypeptide)

 PDGFA_RABIT             Reviewed;         213 AA.
P34007;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
23-MAY-2018, entry version 107.
RecName: Full=Platelet-derived growth factor subunit A;
Short=PDGF subunit A;
AltName: Full=PDGF-1;
AltName: Full=Platelet-derived growth factor A chain;
AltName: Full=Platelet-derived growth factor alpha polypeptide;
Flags: Precursor;
Name=PDGFA;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE (ISOFORMS A1; A2 AND A3).
TISSUE=Vascular smooth muscle;
PubMed=1575749; DOI=10.1016/0006-291X(92)90662-5;
Nakahara K., Nishimura H., Kuro-o M., Takewaki S., Iwase M.,
Ohkubo A., Yazaki Y., Nagai R.;
"Identification of three types of PDGF-A chain gene transcripts in
rabbit vascular smooth muscle and their regulated expression during
development and by angiotensin II.";
Biochem. Biophys. Res. Commun. 184:811-818(1992).
-!- FUNCTION: 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).
{ECO:0000250}.
-!- SUBUNIT: 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 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon
wounding. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=A2;
IsoId=P34007-1; Sequence=Displayed;
Name=A1;
IsoId=P34007-2; Sequence=VSP_004606, VSP_004607;
Name=A3;
IsoId=P34007-3; Sequence=VSP_004608;
-!- INDUCTION: The form A3 is selectively induced by angiotensin II.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
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PIR; JS0735; JS0735.
PIR; PS0387; PS0387.
ProteinModelPortal; P34007; -.
SMR; P34007; -.
STRING; 9986.ENSOCUP00000004907; -.
eggNOG; ENOG410IEXJ; Eukaryota.
eggNOG; ENOG4111GMH; LUCA.
HOGENOM; HOG000286027; -.
HOVERGEN; HBG053546; -.
InParanoid; P34007; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0050919; P:negative chemotaxis; ISS:UniProtKB.
GO; GO:0010512; P:negative regulation of phosphatidylinositol biosynthetic process; ISS:UniProtKB.
GO; GO:0010544; P:negative regulation of platelet activation; ISS:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; ISS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0014910; P:regulation of smooth muscle cell migration; ISS:UniProtKB.
GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR023581; PD_growth_factor_CS.
InterPro; IPR000072; PDGF/VEGF_dom.
InterPro; IPR006782; PDGF_N.
Pfam; PF00341; PDGF; 1.
Pfam; PF04692; PDGF_N; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00249; PDGF_1; 1.
PROSITE; PS50278; PDGF_2; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Developmental protein;
Disulfide bond; Glycoprotein; Growth factor; Mitogen;
Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000250}.
PROPEP 21 89 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000023360.
CHAIN 90 213 Platelet-derived growth factor subunit A.
/FTId=PRO_0000023361.
REGION 158 162 Receptor binding site. {ECO:0000255}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 125 125 Interchain. {ECO:0000250}.
DISULFID 131 179 {ECO:0000250}.
DISULFID 134 134 Interchain. {ECO:0000250}.
DISULFID 135 181 {ECO:0000250}.
VAR_SEQ 196 198 GRR -> DVR (in isoform A1).
{ECO:0000305}.
/FTId=VSP_004606.
VAR_SEQ 197 213 RRRESGKKRKRKRLRPT -> TLLPAPGGVHPQGCLRAHDG
CQSSRNHMQALGWKKKM (in isoform A3).
{ECO:0000305}.
/FTId=VSP_004608.
VAR_SEQ 199 213 Missing (in isoform A1). {ECO:0000305}.
/FTId=VSP_004607.
SEQUENCE 213 AA; 24005 MW; 28A9B7E50487F4C5 CRC64;
MRTWACLLLL GCGYLAHVLA EEPGIPRDVL DRLARSQIHS IRDLQRLLEI DSVGAEDAPE
PSLRAPGVHT ARHVAEKPPA PVPVRRKRTI EEAIPAICKT RTVIYEIPRS QVDPTSANFL
IWPPCVEVKR CTGCCNTSSV KCQPSRVHHR SVKVAKVEYV RKKPKLKEVQ VRLEEHLECA
CAASSAGPEH REEEAGRRRE SGKKRKRKRL RPT


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