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Platelet-derived growth factor C (PDGF-C) (Fallotein) (Spinal cord-derived growth factor) (rScdfg) (VEGF-E) [Cleaved into: Platelet-derived growth factor C, latent form (PDGFC latent form); Platelet-derived growth factor C, receptor-binding form (PDGFC receptor-binding form)]

 PDGFC_RAT               Reviewed;         345 AA.
Q9EQX6; Q8K429;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 109.
RecName: Full=Platelet-derived growth factor C;
Short=PDGF-C;
AltName: Full=Fallotein;
AltName: Full=Spinal cord-derived growth factor;
Short=rScdfg;
AltName: Full=VEGF-E;
Contains:
RecName: Full=Platelet-derived growth factor C, latent form;
Short=PDGFC latent form;
Contains:
RecName: Full=Platelet-derived growth factor C, receptor-binding form;
Short=PDGFC receptor-binding form;
Flags: Precursor;
Name=Pdgfc; Synonyms=Scdgf;
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].
STRAIN=Wistar; TISSUE=Kidney;
PubMed=11162582; DOI=10.1006/bbrc.2000.4187;
Hamada T., Ui-Tei K., Imaki J., Miyata Y.;
"Molecular cloning of SCDGF-B, a novel growth factor homologous to
SCDGF/PDGF-C/fallotein.";
Biochem. Biophys. Res. Commun. 280:733-737(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 42-299.
STRAIN=Sprague-Dawley; TISSUE=Skin;
Brown S.A., Coberly D.M., Rohrich R.R., Chao J.J.;
"Platelet derived growth factor C (PDGF-C) expression in wound
healing.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11912250;
Eitner F., Ostendorf T., Van Roeyen C., Kitahara M., Li X., Aase K.,
Grone H.J., Eriksson U., Floege J.;
"Expression of a novel PDGF isoform, PDGF-C, in normal and diseased
rat kidney.";
J. Am. Soc. Nephrol. 13:910-917(2002).
[4]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11850188; DOI=10.1016/S0925-4773(01)00625-6;
Hamada T., Ui-Tei K., Imaki J., Takahashi F., Onodera H., Mishima T.,
Miyata Y.;
"The expression of SCDGF/PDGF-C/fallotein and SCDGF-B/PDGF-D in the
rat central nervous system.";
Mech. Dev. 112:161-164(2002).
[5]
DEVELOPMENTAL STAGE.
PubMed=15267171; DOI=10.1080/00016480410016577;
Lee Y.W., Ozeki M., Juhn S.K., Lin J.;
"Expression of platelet-derived growth factor in the developing
cochlea of rats.";
Acta Oto-Laryngol. 124:558-562(2004).
[6]
INDUCTION BY FIBROGENESIS.
PubMed=16039137; DOI=10.1016/j.cyto.2005.06.005;
Breitkopf K., Roeyen C., Sawitza I., Wickert L., Floege J.,
Gressner A.M.;
"Expression patterns of PDGF-A, -B, -C and -D and the PDGF-receptors
alpha and beta in activated rat hepatic stellate cells (HSC).";
Cytokine 31:349-357(2005).
[7]
INDUCTION BY INDOXYL SULFATE.
PubMed=16612331; DOI=10.1038/sj.ki.5000340;
Yamamoto H., Tsuruoka S., Ioka T., Ando H., Ito C., Akimoto T.,
Fujimura A., Asano Y., Kusano E.;
"Indoxyl sulfate stimulates proliferation of rat vascular smooth
muscle cells.";
Kidney Int. 69:1780-1785(2006).
[8]
DEVELOPMENTAL STAGE.
PubMed=18272536; DOI=10.1093/nar/gkm923;
Sanchez-Guerrero E., Midgley V.C., Khachigian L.M.;
"Angiotensin II induction of PDGF-C expression is mediated by AT1
receptor-dependent Egr-1 transactivation.";
Nucleic Acids Res. 36:1941-1951(2008).
-!- FUNCTION: Growth factor that plays an essential role in the
regulation of embryonic development, cell proliferation, cell
migration, survival and chemotaxis. Potent mitogen and
chemoattractant for cells of mesenchymal origin. Required for
normal skeleton formation during embryonic development, especially
for normal development of the craniofacial skeleton and for normal
development of the palate. Required for normal skin morphogenesis
during embryonic development. Plays an important role in wound
healing, where it appears to be involved in three stages:
inflammation, proliferation and remodeling. Plays an important
role in angiogenesis and blood vessel development. Involved in
fibrotic processes, in which transformation of interstitial
fibroblasts into myofibroblasts plus collagen deposition occurs.
The CUB domain has mitogenic activity in coronary artery smooth
muscle cells, suggesting a role beyond the maintenance of the
latency of the PDGF domain. In the nucleus, PDGFC seems to have
additional function (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRA
homodimers, and with heterodimers formed by PDGFRA and PDGFRB.
Interacts (via CUB domain) with PLAT (via kringle domain) (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q9NRA1}. Secreted
{ECO:0000250|UniProtKB:Q9NRA1}. Nucleus
{ECO:0000250|UniProtKB:Q9NRA1}. Cytoplasmic granule
{ECO:0000250|UniProtKB:Q9NRA1}. Cell membrane
{ECO:0000250|UniProtKB:Q9NRA1}. Note=Sumoylated form is
predominant in the nucleus. Stored in alpha granules in platelets.
{ECO:0000250|UniProtKB:Q9NRA1}.
-!- TISSUE SPECIFICITY: Highly expressed in the kidney and adrenal
gland. In the kidney, it is expressed in arteriolar smooth muscle
cells and in epithelial cells of individual segments (at protein
level). {ECO:0000269|PubMed:11850188,
ECO:0000269|PubMed:11912250}.
-!- DEVELOPMENTAL STAGE: Expressed in the floor plate of the spinal
cord at E11 and also in the ventricular zone at E16, but not in
adult. In the brain, expression is more significant at E16 than at
adult, with high expression in the cortex, pontine area and
choroid plexus. Detected in the otocyst at E16.
{ECO:0000269|PubMed:11850188, ECO:0000269|PubMed:15267171,
ECO:0000269|PubMed:18272536}.
-!- INDUCTION: Up-regulated in mesangial, visceral epithelial, and
interstitial cells after predominant injury to these cells.
Expression levels increase in hepatic cells undergoing in vitro
transdifferentiation, which represents a model for hepatic
fibrogenesis. Expression induced by indoxyl sulfate. Expression
induced by angiotensin-2 via EGR1 in smooth muscle cells in
neonatal but not in adult rats. {ECO:0000269|PubMed:11912250,
ECO:0000269|PubMed:16039137, ECO:0000269|PubMed:16612331}.
-!- PTM: Proteolytic removal of the N-terminal CUB domain releasing
the core domain is necessary for unmasking the receptor-binding
epitopes of the core domain. Cleavage after basic residues in the
hinge region (region connecting the CUB and growth factor domains)
gives rise to the receptor-binding form. Cleaved by PLAT and PLG
(By similarity). {ECO:0000250}.
-!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB033830; BAB19969.1; -; mRNA.
EMBL; AF508348; AAM47265.1; -; mRNA.
RefSeq; NP_112607.1; NM_031317.1.
UniGene; Rn.211987; -.
ProteinModelPortal; Q9EQX6; -.
SMR; Q9EQX6; -.
STRING; 10116.ENSRNOP00000015081; -.
PaxDb; Q9EQX6; -.
PRIDE; Q9EQX6; -.
Ensembl; ENSRNOT00000015081; ENSRNOP00000015081; ENSRNOG00000010695.
GeneID; 79429; -.
KEGG; rno:79429; -.
UCSC; RGD:68410; rat.
CTD; 56034; -.
RGD; 68410; Pdgfc.
eggNOG; ENOG410IETQ; Eukaryota.
eggNOG; ENOG410XQ91; LUCA.
GeneTree; ENSGT00940000158645; -.
HOGENOM; HOG000261610; -.
HOVERGEN; HBG057324; -.
InParanoid; Q9EQX6; -.
KO; K05450; -.
OMA; HTYPRNM; -.
OrthoDB; EOG091G0BFZ; -.
PhylomeDB; Q9EQX6; -.
TreeFam; TF332130; -.
Reactome; R-RNO-186797; Signaling by PDGF.
PRO; PR:Q9EQX6; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000010695; Expressed in 9 organ(s), highest expression level in adult mammalian kidney.
ExpressionAtlas; Q9EQX6; baseline and differential.
Genevisible; Q9EQX6; RN.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IEA:Ensembl.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0048568; P:embryonic organ development; IEA:InterPro.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; IBA:GO_Central.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IBA:GO_Central.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
CDD; cd00041; CUB; 1.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.90.10; -; 1.
Gene3D; 2.60.120.290; -; 1.
InterPro; IPR000859; CUB_dom.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR029817; PDGF-C.
InterPro; IPR000072; PDGF/VEGF_dom.
InterPro; IPR035914; Sperma_CUB_dom_sf.
PANTHER; PTHR11633:SF5; PTHR11633:SF5; 1.
Pfam; PF00431; CUB; 1.
Pfam; PF00341; PDGF; 1.
SMART; SM00042; CUB; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS50278; PDGF_2; 1.
1: Evidence at protein level;
Cell membrane; Cleavage on pair of basic residues; Complete proteome;
Cytoplasm; Developmental protein; Disulfide bond; Glycoprotein;
Growth factor; Membrane; Mitogen; Nucleus; Reference proteome;
Secreted; Signal; Ubl conjugation.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 345 Platelet-derived growth factor C, latent
form.
/FTId=PRO_0000343875.
CHAIN ? 345 Platelet-derived growth factor C,
receptor-binding form.
/FTId=PRO_0000343876.
DOMAIN 46 163 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
SITE 225 226 Cleavage. {ECO:0000250}.
SITE 231 232 Cleavage. {ECO:0000250}.
SITE 234 235 Cleavage. {ECO:0000250}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 104 124 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 250 294 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 274 274 Interchain (with C-286).
{ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 280 335 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 286 286 Interchain (with C-274).
{ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 287 337 {ECO:0000255|PROSITE-ProRule:PRU00059}.
SEQUENCE 345 AA; 38734 MW; F296DA6E9B765D10 CRC64;
MLLLGLLLLT SALAGQRTGT RAESNLSSKL QLSSDKEQNG VQDPRHERVV TISGNGSIHS
PKFPHTYPRN TVLVWRLVAV DENVRIQLTF DERFGLEDPE DDLCKYDFVE VEEPSDGSVL
GRWCGSGTVP GKQTSKGNHI RIRFVSDEYF PSEPGFCIHY SIIMPQVTET TSPSVLPPSA
LSLDLLNNAV TAFSTVEELI RFLEPDRWQI DLDSLYKPTW PLLGKAFLYG KKSKAVNLNL
LKEEVKLYSC TPRNFSVSIR EELKRTDTIF WPGCLLVKRC GGNCACCLHN CNECQCVPRK
VTKKYHEVLQ LRPKIGVKGL HKSLTDVALE HHEECDCVCR GNTEG


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