PDGFA_RABIT
ID PDGFA_RABIT Reviewed; 213 AA.
AC P34007;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Platelet-derived growth factor subunit A;
DE Short=PDGF subunit A;
DE AltName: Full=PDGF-1;
DE AltName: Full=Platelet-derived growth factor A chain;
DE AltName: Full=Platelet-derived growth factor alpha polypeptide;
DE Flags: Precursor;
GN Name=PDGFA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORMS A1; A2 AND A3).
RC TISSUE=Vascular smooth muscle;
RX PubMed=1575749; DOI=10.1016/0006-291x(92)90662-5;
RA Nakahara K., Nishimura H., Kuro-o M., Takewaki S., Iwase M., Ohkubo A.,
RA Yazaki Y., Nagai R.;
RT "Identification of three types of PDGF-A chain gene transcripts in rabbit
RT vascular smooth muscle and their regulated expression during development
RT and by angiotensin II.";
RL Biochem. Biophys. Res. Commun. 184:811-818(1992).
CC -!- FUNCTION: Growth factor that plays an essential role in the regulation
CC of embryonic development, cell proliferation, cell migration, survival
CC and chemotaxis. Potent mitogen for cells of mesenchymal origin.
CC Required for normal lung alveolar septum formation during
CC embryogenesis, normal development of the gastrointestinal tract, normal
CC development of Leydig cells and spermatogenesis. Required for normal
CC oligodendrocyte development and normal myelination in the spinal cord
CC and cerebellum. Plays an important role in wound healing. Signaling is
CC modulated by the formation of heterodimers with PDGFB (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; antiparallel disulfide-linked dimer. Heterodimer
CC with PDGFB; antiparallel disulfide-linked dimer. The PDGFA homodimer
CC interacts with PDGFRA homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB
CC interacts with PDGFRA homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB. Interacts with CSPG4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon
CC wounding. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A2;
CC IsoId=P34007-1; Sequence=Displayed;
CC Name=A1;
CC IsoId=P34007-2; Sequence=VSP_004606, VSP_004607;
CC Name=A3;
CC IsoId=P34007-3; Sequence=VSP_004608;
CC -!- INDUCTION: The form A3 is selectively induced by angiotensin II.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR PIR; JS0735; JS0735.
DR PIR; PS0387; PS0387.
DR AlphaFoldDB; P34007; -.
DR SMR; P34007; -.
DR STRING; 9986.ENSOCUP00000004907; -.
DR eggNOG; ENOG502QVAU; Eukaryota.
DR InParanoid; P34007; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0050919; P:negative chemotaxis; ISS:UniProtKB.
DR GO; GO:0010512; P:negative regulation of phosphatidylinositol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010544; P:negative regulation of platelet activation; ISS:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0014910; P:regulation of smooth muscle cell migration; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR CDD; cd00135; PDGF; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR023581; PD_growth_factor_CS.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR InterPro; IPR006782; PDGF_N.
DR Pfam; PF00341; PDGF; 1.
DR Pfam; PF04692; PDGF_N; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00249; PDGF_1; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Disulfide bond; Glycoprotein;
KW Growth factor; Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT PROPEP 21..89
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023360"
FT CHAIN 90..213
FT /note="Platelet-derived growth factor subunit A"
FT /id="PRO_0000023361"
FT REGION 158..162
FT /note="Receptor binding site"
FT /evidence="ECO:0000255"
FT REGION 181..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 131..179
FT /evidence="ECO:0000250"
FT DISULFID 134
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 135..181
FT /evidence="ECO:0000250"
FT VAR_SEQ 196..198
FT /note="GRR -> DVR (in isoform A1)"
FT /evidence="ECO:0000305"
FT /id="VSP_004606"
FT VAR_SEQ 197..213
FT /note="RRRESGKKRKRKRLRPT -> TLLPAPGGVHPQGCLRAHDGCQSSRNHMQAL
FT GWKKKM (in isoform A3)"
FT /evidence="ECO:0000305"
FT /id="VSP_004608"
FT VAR_SEQ 199..213
FT /note="Missing (in isoform A1)"
FT /evidence="ECO:0000305"
FT /id="VSP_004607"
SQ 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
