PDGFB_RAT
ID PDGFB_RAT Reviewed; 225 AA.
AC Q05028;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 171.
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; Fragment;
GN Name=Pdgfb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8318539; DOI=10.1016/0167-4781(93)90127-y;
RA Herren B., Weyer K.A., Rouge M., Loetscher P., Pech M.;
RT "Conservation in sequence and affinity of human and rodent PDGF ligands and
RT receptors.";
RL Biochim. Biophys. Acta 1173:294-302(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-182.
RC STRAIN=Sprague-Dawley; TISSUE=Smooth muscle;
RX PubMed=7758166; DOI=10.1161/01.res.76.6.951;
RA Lindner V., Giachelli C.M., Schwartz S.M., Reidy M.A.;
RT "A subpopulation of smooth muscle cells in injured rat arteries expresses
RT platelet-derived growth factor-B chain mRNA.";
RL Circ. Res. 76:951-957(1995).
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 -!- TISSUE SPECIFICITY: Expressed in a distinct subpopulation of smooth
CC muscle cells in injured arteries.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; Z14117; CAA78487.1; -; mRNA.
DR EMBL; L40991; AAA70048.1; -; mRNA.
DR PIR; S25097; S25097.
DR RefSeq; NP_113712.1; NM_031524.1.
DR AlphaFoldDB; Q05028; -.
DR SMR; Q05028; -.
DR ComplexPortal; CPX-6591; Platelet-derived growth factor AB complex.
DR STRING; 10116.ENSRNOP00000023196; -.
DR GlyGen; Q05028; 1 site.
DR PhosphoSitePlus; Q05028; -.
DR PaxDb; Q05028; -.
DR PRIDE; Q05028; -.
DR GeneID; 24628; -.
DR KEGG; rno:24628; -.
DR UCSC; RGD:3283; rat.
DR CTD; 5155; -.
DR RGD; 3283; Pdgfb.
DR eggNOG; ENOG502S2VW; Eukaryota.
DR InParanoid; Q05028; -.
DR OrthoDB; 1439735at2759; -.
DR PhylomeDB; Q05028; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-186797; Signaling by PDGF.
DR Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:1990265; C:platelet-derived growth factor complex; ISO:RGD.
DR GO; GO:0042056; F:chemoattractant activity; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IMP:UniProtKB.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
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:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0030031; P:cell projection assembly; ISO:RGD.
DR GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0071506; P:cellular response to mycophenolic acid; IDA:UniProtKB.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISS:ARUK-UCL.
DR GO; GO:0001892; P:embryonic placenta development; ISS:UniProtKB.
DR GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; ISO:RGD.
DR GO; GO:0042462; P:eye photoreceptor cell development; ISO:RGD.
DR GO; GO:0021782; P:glial cell development; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0072264; P:metanephric glomerular endothelium development; ISO:RGD.
DR GO; GO:0072255; P:metanephric glomerular mesangial cell development; ISS:UniProtKB.
DR GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; ISO:RGD.
DR GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:RGD.
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:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1905064; P:negative regulation of vascular associated smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0016322; P:neuron remodeling; ISO:RGD.
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; IMP:RGD.
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:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:RGD.
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:0045740; P:positive regulation of DNA replication; IMP:RGD.
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:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
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:2000491; P:positive regulation of hepatic stellate cell activation; IMP:RGD.
DR GO; GO:1904899; P:positive regulation of hepatic stellate cell proliferation; IMP:RGD.
DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA: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; IDA: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:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; ISO:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
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; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1905176; P:positive regulation of vascular associated smooth muscle cell dedifferentiation; ISO:RGD.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEP:RGD.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; ISO:RGD.
DR GO; GO:0006929; P:substrate-dependent cell migration; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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..12
FT /evidence="ECO:0000250"
FT PROPEP 13..73
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023377"
FT CHAIN 74..182
FT /note="Platelet-derived growth factor subunit B"
FT /id="PRO_0000023378"
FT PROPEP 183..225
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023379"
FT SITE 100
FT /note="Involved in receptor binding"
FT SITE 103
FT /note="Involved in receptor binding"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..133
FT /evidence="ECO:0000250"
FT DISULFID 116
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 122..170
FT /evidence="ECO:0000250"
FT DISULFID 125
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 126..172
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 225
SQ SEQUENCE 225 AA; 25603 MW; 0DAE138B0AA70F0F CRC64;
LPLCCYLRLV SAEGDPIPEE LYEMLSDHSI RSFDDLQRLL HRDSVDEDGA ELDLNMTRAH
SGVESESSSR GRRSLGSLAA AEPAVIAECK TRTEVFQISR NLIDRTNANF LVWPPCVEVQ
RCSGCCNNRN VQCRASQVQM RPVQVRKIEI VRKKPVFKKA TVTLEDHLAC KCETVVTPRP
VTRSPGTSRE HRAKTPQTRV TVRTVRIRRP PKGKHRKFKH THDKK
