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Q9EQX6

- PDGFC_RAT

UniProt

Q9EQX6 - PDGFC_RAT

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Protein

Platelet-derived growth factor C

Gene

Pdgfc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei225 – 2262CleavageBy similarity
Sitei231 – 2322CleavageBy similarity
Sitei234 – 2352CleavageBy similarity

GO - Biological processi

  1. activation of transmembrane receptor protein tyrosine kinase activity Source: Ensembl
  2. cellular response to amino acid stimulus Source: Ensembl
  3. organ morphogenesis Source: Ensembl
  4. platelet-derived growth factor receptor signaling pathway Source: Ensembl
  5. positive regulation of cell division Source: UniProtKB-KW
  6. positive regulation of DNA replication Source: Ensembl
  7. positive regulation of fibroblast proliferation Source: Ensembl
  8. regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Enzyme and pathway databases

ReactomeiREACT_212371. Signaling by PDGF.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-derived growth factor C
Short name:
PDGF-C
Alternative name(s):
Fallotein
Spinal cord-derived growth factor
Short name:
rScdfg
VEGF-E
Cleaved into the following 2 chains:
Platelet-derived growth factor C, receptor-binding form
Short name:
PDGFC receptor-binding form
Gene namesi
Name:Pdgfc
Synonyms:Scdgf
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi68410. Pdgfc.

Subcellular locationi

Cytoplasm By similarity. Secreted By similarity. Nucleus By similarity. Cytoplasmic granule By similarity
Note: Sumoylated form is predominant in the nucleus. Stored in alpha granules in platelets. Membrane associated when bound to receptors.By similarity

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. cytoplasm Source: UniProtKB-KW
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
  5. nucleus Source: UniProtKB-KW
  6. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 345Platelet-derived growth factor C, receptor-binding formPRO_0000343876
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 345323Platelet-derived growth factor C, latent formPRO_0000343875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi104 ↔ 124PROSITE-ProRule annotation
Disulfide bondi250 ↔ 294PROSITE-ProRule annotation
Disulfide bondi274 – 274Interchain (with C-286)PROSITE-ProRule annotation
Disulfide bondi280 ↔ 335PROSITE-ProRule annotation
Disulfide bondi286 – 286Interchain (with C-274)PROSITE-ProRule annotation
Disulfide bondi287 ↔ 337PROSITE-ProRule annotation

Post-translational modificationi

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.By similarity
Sumoylated with SUMO1.By similarity
N-glycosylated.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9EQX6.

Expressioni

Tissue specificityi

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).2 Publications

Developmental stagei

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 E16.3 Publications

Inductioni

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.3 Publications

Gene expression databases

GenevestigatoriQ9EQX6.

Interactioni

Subunit structurei

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.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9EQX6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 163118CUBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PDGF/VEGF growth factor family.Curated
Contains 1 CUB domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG74970.
GeneTreeiENSGT00390000005171.
HOGENOMiHOG000261610.
HOVERGENiHBG057324.
InParanoidiQ9EQX6.
KOiK05450.
OMAiDCVCRGN.
OrthoDBiEOG7VB2FN.
PhylomeDBiQ9EQX6.
TreeFamiTF332130.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
2.60.120.290. 1 hit.
InterProiIPR000859. CUB_dom.
IPR029034. Cystine-knot_cytokine.
IPR000072. PDGF/VEGF_dom.
[Graphical view]
PfamiPF00431. CUB. 1 hit.
PF00341. PDGF. 1 hit.
[Graphical view]
SMARTiSM00042. CUB. 1 hit.
SM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 1 hit.
SSF57501. SSF57501. 1 hit.
PROSITEiPS01180. CUB. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EQX6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLLGLLLLT SALAGQRTGT RAESNLSSKL QLSSDKEQNG VQDPRHERVV
60 70 80 90 100
TISGNGSIHS PKFPHTYPRN TVLVWRLVAV DENVRIQLTF DERFGLEDPE
110 120 130 140 150
DDLCKYDFVE VEEPSDGSVL GRWCGSGTVP GKQTSKGNHI RIRFVSDEYF
160 170 180 190 200
PSEPGFCIHY SIIMPQVTET TSPSVLPPSA LSLDLLNNAV TAFSTVEELI
210 220 230 240 250
RFLEPDRWQI DLDSLYKPTW PLLGKAFLYG KKSKAVNLNL LKEEVKLYSC
260 270 280 290 300
TPRNFSVSIR EELKRTDTIF WPGCLLVKRC GGNCACCLHN CNECQCVPRK
310 320 330 340
VTKKYHEVLQ LRPKIGVKGL HKSLTDVALE HHEECDCVCR GNTEG
Length:345
Mass (Da):38,734
Last modified:March 1, 2001 - v1
Checksum:iF296DA6E9B765D10
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB033830 mRNA. Translation: BAB19969.1.
AF508348 mRNA. Translation: AAM47265.1.
RefSeqiNP_112607.1. NM_031317.1.
UniGeneiRn.211987.

Genome annotation databases

EnsembliENSRNOT00000015081; ENSRNOP00000015081; ENSRNOG00000010695.
GeneIDi79429.
KEGGirno:79429.
UCSCiRGD:68410. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB033830 mRNA. Translation: BAB19969.1 .
AF508348 mRNA. Translation: AAM47265.1 .
RefSeqi NP_112607.1. NM_031317.1.
UniGenei Rn.211987.

3D structure databases

ProteinModelPortali Q9EQX6.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9EQX6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000015081 ; ENSRNOP00000015081 ; ENSRNOG00000010695 .
GeneIDi 79429.
KEGGi rno:79429.
UCSCi RGD:68410. rat.

Organism-specific databases

CTDi 56034.
RGDi 68410. Pdgfc.

Phylogenomic databases

eggNOGi NOG74970.
GeneTreei ENSGT00390000005171.
HOGENOMi HOG000261610.
HOVERGENi HBG057324.
InParanoidi Q9EQX6.
KOi K05450.
OMAi DCVCRGN.
OrthoDBi EOG7VB2FN.
PhylomeDBi Q9EQX6.
TreeFami TF332130.

Enzyme and pathway databases

Reactomei REACT_212371. Signaling by PDGF.

Miscellaneous databases

NextBioi 614787.
PROi Q9EQX6.

Gene expression databases

Genevestigatori Q9EQX6.

Family and domain databases

Gene3Di 2.10.90.10. 1 hit.
2.60.120.290. 1 hit.
InterProi IPR000859. CUB_dom.
IPR029034. Cystine-knot_cytokine.
IPR000072. PDGF/VEGF_dom.
[Graphical view ]
Pfami PF00431. CUB. 1 hit.
PF00341. PDGF. 1 hit.
[Graphical view ]
SMARTi SM00042. CUB. 1 hit.
SM00141. PDGF. 1 hit.
[Graphical view ]
SUPFAMi SSF49854. SSF49854. 1 hit.
SSF57501. SSF57501. 1 hit.
PROSITEi PS01180. CUB. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of SCDGF-B, a novel growth factor homologous to SCDGF/PDGF-C/fallotein."
    Hamada T., Ui-Tei K., Imaki J., Miyata Y.
    Biochem. Biophys. Res. Commun. 280:733-737(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Kidney.
  2. "Platelet derived growth factor C (PDGF-C) expression in wound healing."
    Brown S.A., Coberly D.M., Rohrich R.R., Chao J.J.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-299.
    Strain: Sprague-Dawley.
    Tissue: Skin.
  3. "Expression of a novel PDGF isoform, PDGF-C, in normal and diseased rat kidney."
    Eitner F., Ostendorf T., Van Roeyen C., Kitahara M., Li X., Aase K., Grone H.J., Eriksson U., Floege J.
    J. Am. Soc. Nephrol. 13:910-917(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  4. "The expression of SCDGF/PDGF-C/fallotein and SCDGF-B/PDGF-D in the rat central nervous system."
    Hamada T., Ui-Tei K., Imaki J., Takahashi F., Onodera H., Mishima T., Miyata Y.
    Mech. Dev. 112:161-164(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "Expression of platelet-derived growth factor in the developing cochlea of rats."
    Lee Y.W., Ozeki M., Juhn S.K., Lin J.
    Acta Oto-Laryngol. 124:558-562(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  6. "Expression patterns of PDGF-A, -B, -C and -D and the PDGF-receptors alpha and beta in activated rat hepatic stellate cells (HSC)."
    Breitkopf K., Roeyen C., Sawitza I., Wickert L., Floege J., Gressner A.M.
    Cytokine 31:349-357(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY FIBROGENESIS.
  7. "Indoxyl sulfate stimulates proliferation of rat vascular smooth muscle cells."
    Yamamoto H., Tsuruoka S., Ioka T., Ando H., Ito C., Akimoto T., Fujimura A., Asano Y., Kusano E.
    Kidney Int. 69:1780-1785(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY INDOXYL SULFATE.
  8. "Angiotensin II induction of PDGF-C expression is mediated by AT1 receptor-dependent Egr-1 transactivation."
    Sanchez-Guerrero E., Midgley V.C., Khachigian L.M.
    Nucleic Acids Res. 36:1941-1951(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiPDGFC_RAT
AccessioniPrimary (citable) accession number: Q9EQX6
Secondary accession number(s): Q8K429
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3