PDGFA_BOVIN
ID PDGFA_BOVIN Reviewed; 211 AA.
AC Q2KJ15;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Platelet-derived growth factor subunit A;
DE Short=PDGF subunit A;
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}. Note=Released by
CC platelets upon wounding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; BC105569; AAI05570.1; -; mRNA.
DR RefSeq; NP_001068699.1; NM_001075231.1.
DR AlphaFoldDB; Q2KJ15; -.
DR SMR; Q2KJ15; -.
DR STRING; 9913.ENSBTAP00000019323; -.
DR PaxDb; Q2KJ15; -.
DR PRIDE; Q2KJ15; -.
DR Ensembl; ENSBTAT00000019323; ENSBTAP00000019323; ENSBTAG00000014541.
DR GeneID; 505908; -.
DR KEGG; bta:505908; -.
DR CTD; 5154; -.
DR VEuPathDB; HostDB:ENSBTAG00000014541; -.
DR VGNC; VGNC:32689; PDGFA.
DR eggNOG; ENOG502QVAU; Eukaryota.
DR GeneTree; ENSGT00940000159039; -.
DR InParanoid; Q2KJ15; -.
DR OMA; HHKNSSH; -.
DR OrthoDB; 1439735at2759; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000014541; Expressed in prostate gland and 104 other tissues.
DR ExpressionAtlas; Q2KJ15; baseline.
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:0070851; F:growth factor receptor binding; IBA:GO_Central.
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 Cleavage on pair of basic residues; Developmental protein; Disulfide bond;
KW Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT PROPEP 21..86
FT /note="Removed in mature form"
FT /id="PRO_0000282861"
FT CHAIN 87..211
FT /note="Platelet-derived growth factor subunit A"
FT /id="PRO_0000282862"
FT REGION 158..162
FT /note="Receptor binding site"
FT /evidence="ECO:0000255"
FT REGION 180..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..140
FT /evidence="ECO:0000250"
FT DISULFID 123
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 129..177
FT /evidence="ECO:0000250"
FT DISULFID 132
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 133..179
FT /evidence="ECO:0000250"
SQ SEQUENCE 211 AA; 24009 MW; 16389873EE22785D CRC64;
MRTWACLLLL GCGYLANALA EEAEIPREVI ERLAHSQIHS IRDLQRLLEI DSVGAEEPLE
TSLRAHGGHG AKHALEKRPV PIRRKRSIEE AIPAVCKTRT VIYEIPRSQV DPTSANFLIW
PPCVEVKRCT GCCNTSSVKC QPSRVHHRNV KVAKVEYFRK KAKLKEVQVR LEEHLECTCT
SASPSPDHRE EEAGRRRESG KKRKRKRLKP T
