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Q9EQX6 (PDGFC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Platelet-derived growth factor C, latent form
    Short name=PDGFC latent form
  2. Platelet-derived growth factor C, receptor-binding form
    Short name=PDGFC receptor-binding form
Gene names
Name:Pdgfc
Synonyms:Scdgf
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

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.

Subcellular location

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

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). Ref.3 Ref.4

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. Ref.4 Ref.5 Ref.8

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. Ref.3 Ref.6 Ref.7

Post-translational modification

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.

Sumoylated with SUMO1 By similarity.

N-glycosylated By similarity.

Sequence similarities

Belongs to the PDGF/VEGF growth factor family.

Contains 1 CUB domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 345323Platelet-derived growth factor C, latent form
PRO_0000343875
Chain? – 345Platelet-derived growth factor C, receptor-binding formPRO_0000343876

Regions

Domain46 – 163118CUB

Sites

Site225 – 2262Cleavage By similarity
Site231 – 2322Cleavage By similarity
Site234 – 2352Cleavage By similarity

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation551N-linked (GlcNAc...) Potential
Disulfide bond104 ↔ 124 By similarity
Disulfide bond250 ↔ 294 By similarity
Disulfide bond274Interchain (with C-286) By similarity
Disulfide bond280 ↔ 335 By similarity
Disulfide bond286Interchain (with C-274) By similarity
Disulfide bond287 ↔ 337 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9EQX6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F296DA6E9B765D10

FASTA34538,734
        10         20         30         40         50         60 
MLLLGLLLLT SALAGQRTGT RAESNLSSKL QLSSDKEQNG VQDPRHERVV TISGNGSIHS 

        70         80         90        100        110        120 
PKFPHTYPRN TVLVWRLVAV DENVRIQLTF DERFGLEDPE DDLCKYDFVE VEEPSDGSVL 

       130        140        150        160        170        180 
GRWCGSGTVP GKQTSKGNHI RIRFVSDEYF PSEPGFCIHY SIIMPQVTET TSPSVLPPSA 

       190        200        210        220        230        240 
LSLDLLNNAV TAFSTVEELI RFLEPDRWQI DLDSLYKPTW PLLGKAFLYG KKSKAVNLNL 

       250        260        270        280        290        300 
LKEEVKLYSC TPRNFSVSIR EELKRTDTIF WPGCLLVKRC GGNCACCLHN CNECQCVPRK 

       310        320        330        340 
VTKKYHEVLQ LRPKIGVKGL HKSLTDVALE HHEECDCVCR GNTEG 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB033830 mRNA. Translation: BAB19969.1.
AF508348 mRNA. Translation: AAM47265.1.
RefSeqNP_112607.1. NM_031317.1.
UniGeneRn.211987.

3D structure databases

ProteinModelPortalQ9EQX6.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9EQX6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015081; ENSRNOP00000015081; ENSRNOG00000010695.
GeneID79429.
KEGGrno:79429.
UCSCRGD:68410. rat.

Organism-specific databases

CTD56034.
RGD68410. Pdgfc.

Phylogenomic databases

eggNOGNOG74970.
GeneTreeENSGT00390000005171.
HOGENOMHOG000261610.
HOVERGENHBG057324.
InParanoidQ9EQX6.
KOK05450.
OMADCVCRGN.
OrthoDBEOG7VB2FN.
PhylomeDBQ9EQX6.
TreeFamTF332130.

Gene expression databases

GenevestigatorQ9EQX6.

Family and domain databases

Gene3D2.10.90.10. 1 hit.
2.60.120.290. 1 hit.
InterProIPR000859. CUB_dom.
IPR029034. Cystine-knot_cytokine.
IPR000072. PDGF/VEGF_dom.
[Graphical view]
PfamPF00431. CUB. 1 hit.
PF00341. PDGF. 1 hit.
[Graphical view]
SMARTSM00042. CUB. 1 hit.
SM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMSSF49854. SSF49854. 1 hit.
SSF57501. SSF57501. 1 hit.
PROSITEPS01180. CUB. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio614787.
PROQ9EQX6.

Entry information

Entry namePDGFC_RAT
AccessionPrimary (citable) accession number: Q9EQX6
Secondary accession number(s): Q8K429
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families