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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_RAT               Reviewed;         204 AA.
P28576;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
20-DEC-2017, entry version 145.
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; Synonyms=Rpa1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-204.
PubMed=8318539; DOI=10.1016/0167-4781(93)90127-Y;
Herren B., Weyer K.A., Rouge M., Loetscher P., Pech M.;
"Conservation in sequence and affinity of human and rodent PDGF
ligands and receptors.";
Biochim. Biophys. Acta 1173:294-302(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8447423;
Katayose D., Ohe M., Yamauchi K., Ogata M., Shirato K., Fujita H.,
Shibahara S., Takishima T.;
"Increased expression of PDGF A- and B-chain genes in rat lungs with
hypoxic pulmonary hypertension.";
Am. J. Physiol. 264:L100-L106(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Xia Y., Feng L., Tang W.W., Wilson C.B.;
"Cloning and expression of rat platelet-derived growth factor A-
chain.";
J. Am. Soc. Nephrol. 3:622-622(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 58-196 (ISOFORM SHORT).
STRAIN=Fischer 344; TISSUE=Smooth muscle;
PubMed=8469035; DOI=10.1016/0047-6374(93)90113-6;
Szabo P., Weksler D., Whittington E., Weksler B.B.;
"The age-dependent proliferation of rat aortic smooth muscle cells is
independent of differential splicing of PDGF A-chain mRNA.";
Mech. Ageing Dev. 67:79-89(1993).
-!- 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=2;
Name=Long;
IsoId=P28576-1; Sequence=Displayed;
Name=Short;
IsoId=P28576-2; Sequence=VSP_004609, VSP_004610;
-!- DEVELOPMENTAL STAGE: In kidney epithelial tissues, the shorter
form predominates in young (1 day old) rats while the longer form
becomes more prevalant during aging.
-!- DOMAIN: The long form contains a basic insert which acts as a cell
retention signal.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; L06894; AAB59693.1; -; mRNA.
EMBL; Z14120; CAA78490.1; -; mRNA.
EMBL; D10106; BAA00987.1; -; mRNA.
EMBL; L06238; AAA41932.1; -; mRNA.
EMBL; S57864; AAB26134.2; -; mRNA.
PIR; A48851; A48851.
PIR; S25096; S25096.
RefSeq; NP_036933.1; NM_012801.1.
UniGene; Rn.10999; -.
ProteinModelPortal; P28576; -.
SMR; P28576; -.
STRING; 10116.ENSRNOP00000001775; -.
PaxDb; P28576; -.
Ensembl; ENSRNOT00000001775; ENSRNOP00000001775; ENSRNOG00000001312. [P28576-2]
Ensembl; ENSRNOT00000042117; ENSRNOP00000040116; ENSRNOG00000001312. [P28576-2]
GeneID; 25266; -.
KEGG; rno:25266; -.
UCSC; RGD:3282; rat. [P28576-1]
CTD; 5154; -.
RGD; 3282; Pdgfa.
eggNOG; ENOG410IEXJ; Eukaryota.
eggNOG; ENOG4111GMH; LUCA.
GeneTree; ENSGT00510000046755; -.
HOVERGEN; HBG053546; -.
InParanoid; P28576; -.
KO; K04359; -.
PhylomeDB; P28576; -.
Reactome; R-RNO-114608; Platelet degranulation.
Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
Reactome; R-RNO-186763; Downstream signal transduction.
Reactome; R-RNO-186797; Signaling by PDGF.
Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
PRO; PR:P28576; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000001312; -.
ExpressionAtlas; P28576; baseline and differential.
Genevisible; P28576; RN.
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:0005902; C:microvillus; ISS:UniProtKB.
GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0009887; P:animal organ morphogenesis; ISS:UniProtKB.
GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
GO; GO:0060348; P:bone development; ISO:RGD.
GO; GO:0030031; P:cell projection assembly; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
GO; GO:0048565; P:digestive tract development; ISO:RGD.
GO; GO:1990401; P:embryonic lung development; ISO:RGD.
GO; GO:0001942; P:hair follicle development; ISS:UniProtKB.
GO; GO:0048839; P:inner ear development; IEP:RGD.
GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB.
GO; GO:0008584; P:male gonad development; IEP:RGD.
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; IMP:RGD.
GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
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:0002053; P:positive regulation of mesenchymal cell proliferation; 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:0060683; P:regulation of branching involved in salivary gland morphogenesis by epithelial-mesenchymal signaling; ISS:UniProtKB.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0014910; P:regulation of smooth muscle cell migration; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
GO; GO:0043588; P:skin development; ISS:UniProtKB.
GO; GO:0042060; P:wound healing; IEP:RGD.
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; Cleavage on pair of basic residues;
Complete proteome; Developmental protein; Disulfide bond;
Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted;
Signal.
SIGNAL 1 20 {ECO:0000250}.
PROPEP 21 85 Removed in mature form.
/FTId=PRO_0000023362.
CHAIN 86 204 Platelet-derived growth factor subunit A.
/FTId=PRO_0000023363.
REGION 158 162 Receptor binding site. {ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 96 140 {ECO:0000250}.
DISULFID 123 123 Interchain. {ECO:0000250}.
DISULFID 129 177 {ECO:0000250}.
DISULFID 132 132 Interchain. {ECO:0000250}.
DISULFID 133 179 {ECO:0000250}.
VAR_SEQ 194 196 GRR -> DVR (in isoform Short).
{ECO:0000303|PubMed:8469035,
ECO:0000303|Ref.3}.
/FTId=VSP_004609.
VAR_SEQ 197 204 Missing (in isoform Short).
{ECO:0000303|PubMed:8469035,
ECO:0000303|Ref.3}.
/FTId=VSP_004610.
CONFLICT 85 111 KRSIEEAIPAVCKTRTVIYEIPRSQVD -> REVLRKPFPQ
FARPGRSFTRYLGARWT (in Ref. 2; BAA00987).
{ECO:0000305}.
CONFLICT 119 119 I -> T (in Ref. 3; AAA41932).
{ECO:0000305}.
SEQUENCE 204 AA; 23307 MW; FA413F74E86F742C CRC64;
MRTWACLLLL GCGYLAHALA EEAEIPRELI ERLARSQIHS IRDLQRLLEI DSVGAEDALE
TNLRAHGSHT VKHVPEKRPV PIRRKRSIEE AIPAVCKTRT VIYEIPRSQV DPTSANFLIW
PPCVEVKRCT GCCNTSSVKC QPSRVHHRSV KVAKVEYVRK KPKLKEVQVR LEEHLECACA
TSNLNPDHRE EETGRRRESG KKRK


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