PDGFB_SHEEP
ID PDGFB_SHEEP Reviewed; 241 AA.
AC Q95229;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Platelet-derived growth factor subunit B;
DE Short=PDGF subunit B;
DE AltName: Full=PDGF-2;
DE AltName: Full=Platelet-derived growth factor B chain;
DE AltName: Full=Platelet-derived growth factor beta polypeptide;
DE Flags: Precursor;
GN Name=PDGFB;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Texel; TISSUE=Spleen;
RA Woodall C.J., Zhang Z., Watt N.J.;
RT "The entire coding sequence of sheep platelet-derived growth factor B
RT subunit cDNA.";
RL Submitted (SEP-1996) 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 proliferation and recruitment of pericytes and
CC vascular smooth muscle cells in the central nervous system, skin, lung,
CC heart and placenta. Required for normal blood vessel development, and
CC for normal development of kidney glomeruli. Plays an important role in
CC wound healing. Signaling is modulated by the formation of heterodimers
CC with PDGFA (By similarity). {ECO:0000250|UniProtKB:P01127,
CC ECO:0000250|UniProtKB:P31240}.
CC -!- SUBUNIT: Antiparallel homodimer; disulfide-linked. Antiparallel
CC heterodimer with PDGFA; disulfide-linked. The PDGFB homodimer interacts
CC with PDGFRA and PDGFRB homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB
CC interacts with PDGFRB homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB. Interacts with XLKD1 (By similarity). Interacts with
CC LRP1 (By similarity). Interacts with SORL1 (via the N-terminal
CC ectodomain) (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P01127}.
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; X97123; CAA65790.1; -; mRNA.
DR RefSeq; NP_001009471.1; NM_001009471.1.
DR AlphaFoldDB; Q95229; -.
DR SMR; Q95229; -.
DR STRING; 9940.ENSOARP00000017621; -.
DR PRIDE; Q95229; -.
DR GeneID; 443545; -.
DR KEGG; oas:443545; -.
DR CTD; 5155; -.
DR eggNOG; ENOG502S2VW; Eukaryota.
DR OrthoDB; 1439735at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0016176; F:superoxide-generating NADPH oxidase activator activity; ISS:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0071506; P:cellular response to mycophenolic acid; ISS:UniProtKB.
DR GO; GO:0001892; P:embryonic placenta development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0072255; P:metanephric glomerular mesangial cell development; ISS:UniProtKB.
DR GO; GO:0002548; P:monocyte 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:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0038001; P:paracrine signaling; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell 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:0003104; P:positive regulation of glomerular filtration; ISS:UniProtKB.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; 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:2000591; P:positive regulation of metanephric mesenchymal cell migration; 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:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; 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:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; 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 InterPro; IPR015583; PDGF_suB.
DR PANTHER; PTHR11633:SF2; PTHR11633:SF2; 1.
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; Proto-oncogene; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT PROPEP 21..81
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023380"
FT CHAIN 82..190
FT /note="Platelet-derived growth factor subunit B"
FT /id="PRO_0000023381"
FT PROPEP 191..241
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023382"
FT REGION 217..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 108
FT /note="Involved in receptor binding"
FT SITE 111
FT /note="Involved in receptor binding"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..141
FT /evidence="ECO:0000250"
FT DISULFID 124
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 130..178
FT /evidence="ECO:0000250"
FT DISULFID 133
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 134..180
FT /evidence="ECO:0000250"
SQ SEQUENCE 241 AA; 27331 MW; 37BE1EC12E7D2863 CRC64;
MNRCWALFLS LCCYLRLVSA EGDPIPEELY EMLSDHSIRS FDDLQRLLHG DSLDEDGAEL
DLNLTRSHSG GELESLSRGR RSLGSPTVAE PAVIAECKTR TEVSEISRRL IDRTNANFLV
WPPCVEVQRC SGCCNNRNVQ CRPTQVQDRK VQVKKIEIVR KKKIFKKATV TLVDHLACRC
ETVMARAVTR TPGSSQEQRA ARTPQTRVTI RTVRVRRPPK GKHRKFKHTH DKTALKETLG
A
