Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NRA1 (PDGFC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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=SCDGF
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
ORF Names:UNQ174/PRO200
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.2 Ref.3 Ref.4 Ref.14 Ref.15 Ref.18 Ref.19 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27

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). Ref.17 Ref.19 Ref.22

Subcellular location

Cytoplasm. Secreted. Nucleus. Cytoplasmic granule. Note: Sumoylated form is predominant in the nucleus. Stored in alpha granules in platelets. Membrane associated when bound to receptors. Ref.2 Ref.3 Ref.4 Ref.18 Ref.19 Ref.22 Ref.26

Tissue specificity

Expressed in the fallopian tube, vascular smooth muscle cells in kidney, breast and colon and in visceral smooth muscle of the gastrointestinal tract. Highly expressed in retinal pigment epithelia. Expressed in medulloblastoma. In the kidney, constitutively expressed in parietal epithelial cells of Bowman's capsule, tubular epithelial cells and in arterial endothelial cells (at protein level). Highly expressed in the platelets, prostate, testis and uterus. Higher expression is observed in uterine leiomyomata. Weaker expression in the spleen, thymus, heart, pancreas, liver, ovary cells and small intestine, and negligible expression in the colon and peripheral blood leukocytes. Ref.1 Ref.3 Ref.4 Ref.11 Ref.13 Ref.14 Ref.18 Ref.27 Ref.28

Developmental stage

In the fetal kidney, detected in the developing mesangium, ureteric bud epithelium and the undifferentiated mesenchyme (at protein level). Ref.16

Induction

Up-regulated by EWS-FLI1 chimeric transcription factor in tumor derived cells. Up-regulated in podocytes and interstitial cells after injury/activation of these cells. FGF2 activates PDGFC transcription via EGR1. Up-regulated by TGFB1 in concert with FGF2. Ref.12 Ref.16 Ref.20 Ref.25

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.

Sumoylated with SUMO1. Ref.26

N-glycosylated. Ref.14

Miscellaneous

A lower molecular weight form (around 43 kDa) is present in patients with papillary thyroid carcinoma.

Sequence similarities

Belongs to the PDGF/VEGF growth factor family.

Contains 1 CUB domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionDevelopmental protein
Growth factor
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of transmembrane receptor protein tyrosine kinase activity

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Traceable author statement Ref.2. Source: UniProtKB

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

platelet-derived growth factor receptor signaling pathway

Inferred from direct assay Ref.3. Source: BHF-UCL

positive regulation of DNA replication

Inferred from direct assay Ref.3. Source: BHF-UCL

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of fibroblast proliferation

Inferred from direct assay Ref.3. Source: BHF-UCL

regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

cell surface

Inferred from direct assay Ref.3. Source: BHF-UCL

cytoplasm

Inferred from direct assay. Source: HPA

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay Ref.3. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionplatelet-derived growth factor receptor binding

Inferred from physical interaction Ref.3. Source: BHF-UCL

protein homodimerization activity

Inferred from physical interaction Ref.3. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDGFRAP162342EBI-8833587,EBI-2861522

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRA1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NRA1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     244-306: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9NRA1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     155-167: GFCIHYNIVMPQF → SNRGGKIIQLHTS
     168-345: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9NRA1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 345323Platelet-derived growth factor C, latent form
PRO_0000343871
Chain? – 345Platelet-derived growth factor C, receptor-binding formPRO_0000343872

Regions

Domain46 – 163118CUB

Sites

Site225 – 2262Cleavage
Site231 – 2322Cleavage Potential
Site234 – 2352Cleavage Potential

Amino acid modifications

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

Natural variations

Alternative sequence1 – 163163Missing in isoform 4.
VSP_047606
Alternative sequence155 – 16713GFCIH…VMPQF → SNRGGKIIQLHTS in isoform 3.
VSP_034701
Alternative sequence168 – 345178Missing in isoform 3.
VSP_034702
Alternative sequence244 – 30663Missing in isoform 2.
VSP_034703

Experimental info

Mutagenesis1241C → S: Loss of mitogenic activity of CUB domain in coronary artery smooth muscle cells. Ref.14
Mutagenesis2311R → A: Essential for cleavage by PLAT. Ref.22
Mutagenesis2321K → A: Not essential for cleavage by PLAT. Ref.22
Mutagenesis2341R → A: Not essential for cleavage by PLAT. Ref.22
Sequence conflict91L → V in AAF80597. Ref.3
Sequence conflict181Q → R in AAF80597. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: CDE9E51F40633E78

FASTA34539,029
        10         20         30         40         50         60 
MSLFGLLLLT SALAGQRQGT QAESNLSSKF QFSSNKEQNG VQDPQHERII TVSTNGSIHS 

        70         80         90        100        110        120 
PRFPHTYPRN TVLVWRLVAV EENVWIQLTF DERFGLEDPE DDICKYDFVE VEEPSDGTIL 

       130        140        150        160        170        180 
GRWCGSGTVP GKQISKGNQI RIRFVSDEYF PSEPGFCIHY NIVMPQFTEA VSPSVLPPSA 

       190        200        210        220        230        240 
LPLDLLNNAI TAFSTLEDLI RYLEPERWQL DLEDLYRPTW QLLGKAFVFG RKSRVVDLNL 

       250        260        270        280        290        300 
LTEEVRLYSC TPRNFSVSIR EELKRTDTIF WPGCLLVKRC GGNCACCLHN CNECQCVPSK 

       310        320        330        340 
VTKKYHEVLQ LRPKTGVRGL HKSLTDVALE HHEECDCVCR GSTGG 

« Hide

Isoform 2 [UniParc].

Checksum: 8426CEB8FF9AA45B
Show »

FASTA28231,808
Isoform 3 [UniParc].

Checksum: 60023851D9FE5E65
Show »

FASTA16718,784
Isoform 4 [UniParc].

Checksum: F5B9733D3794B1B7
Show »

FASTA18220,609

References

« Hide 'large scale' references
[1]"Identification of a novel platelet-derived growth factor-like gene, fallotein, in the human reproductive tract."
Tsai Y.J., Lee R.K., Lin S.P., Chen Y.H.
Biochim. Biophys. Acta 1492:196-202(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Uterus.
[2]"A novel gene derived from developing spinal cords, SCDGF, is a unique member of the PDGF/VEGF family."
Hamada T., Ui-Tei K., Miyata Y.
FEBS Lett. 475:97-102(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
Tissue: Brain.
[3]"PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor."
Li X., Ponten A., Aase K., Karlsson L., Abramsson A., Uutela M., Backstrom G., Hellstrom M., Bostrom H., Li H., Soriano P., Betsholtz C., Heldin C.H., Alitalo K., Ostman A., Eriksson U.
Nat. Cell Biol. 2:302-309(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Lung.
[4]"Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor."
Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O., Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M., Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.
J. Biol. Chem. 276:27406-27414(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[5]"An N-terminally truncated isoform of human PDGF-C regulates the secretion of full-length PDGF-C and is deregulated in renal cell carcinoma."
Zhao J., Liu Z., Liu T., Nilsson S., Nister M.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Fetal brain.
[6]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Prostate.
[8]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[11]"Chromosomal location, exon structure, and vascular expression patterns of the human PDGFC and PDGFC genes."
Uutela M., Lauren J., Bergsten E., Li X., Horelli-Kuitunen N., Eriksson U., Alitalo K.
Circulation 103:2242-2247(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"PDGF-C is an EWS/FLI induced transforming growth factor in Ewing family tumors."
Zwerner J.P., May W.A.
Oncogene 20:626-633(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[13]"Platelet-derived growth factor-B and -C and active alpha-receptors in medulloblastoma cells."
Andrae J., Molander C., Smits A., Funa K., Nister M.
Biochem. Biophys. Res. Commun. 296:604-611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[14]"Characterization of platelet-derived growth factor-C (PDGF-C): expression in normal and tumor cells, biological activity and chromosomal localization."
Dijkmans J., Xu J., Masure S., Dhanaraj S., Gosiewska A., Geesin J., Sprengel J., Harris S., Verhasselt P., Gordon R., Yon J.
Int. J. Biochem. Cell Biol. 34:414-426(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), GLYCOSYLATION, MUTAGENESIS OF CYS-124.
[15]"Dominant negative PDGF-C inhibits growth of Ewing family tumor cell lines."
Zwerner J.P., May W.A.
Oncogene 21:3847-3854(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"PDGF-C expression in the developing and normal adult human kidney and in glomerular diseases."
Eitner F., Ostendorf T., Kretzler M., Cohen C.D., Eriksson U., Grone H.J., Floege J.
J. Am. Soc. Nephrol. 14:1145-1153(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, INDUCTION.
[17]"Platelet-derived growth factor (PDGF)-C, a PDGF family member with a vascular endothelial growth factor-like structure."
Reigstad L.J., Sande H.M., Fluge O., Bruland O., Muga A., Varhaug J.E., Martinez A., Lillehaug J.R.
J. Biol. Chem. 278:17114-17120(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF SECRETED ACTIVE FORM, SUBUNIT, DISULFIDE BONDS, 3D-STRUCTURE MODELING.
[18]"PDGF C is a selective alpha platelet-derived growth factor receptor agonist that is highly expressed in platelet alpha granules and vascular smooth muscle."
Fang L., Yan Y., Komuves L.G., Yonkovich S., Sullivan C.M., Stringer B., Galbraith S., Lokker N.A., Hwang S.S., Nurden P., Phillips D.R., Giese N.A.
Arterioscler. Thromb. Vasc. Biol. 24:787-792(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[19]"Tissue plasminogen activator is a potent activator of PDGF-CC."
Fredriksson L., Li H., Fieber C., Li X., Eriksson U.
EMBO J. 23:3793-3802(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLAT.
[20]"Fibroblast growth factor-2 induction of platelet-derived growth factor-C chain transcription in vascular smooth muscle cells is ERK-dependent but not JNK-dependent and mediated by Egr-1."
Midgley V.C., Khachigian L.M.
J. Biol. Chem. 279:40289-40295(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY EGR1.
[21]"Structural and functional specificities of PDGF-C and PDGF-D, the novel members of the platelet-derived growth factors family."
Reigstad L.J., Varhaug J.E., Lillehaug J.R.
FEBS J. 272:5723-5741(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[22]"Structural requirements for activation of latent platelet-derived growth factor CC by tissue plasminogen activator."
Fredriksson L., Ehnman M., Fieber C., Eriksson U.
J. Biol. Chem. 280:26856-26862(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PLAT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-231; LYS-232 AND ARG-234.
[23]"Regulation of fibrogenic/fibrolytic genes by platelet-derived growth factor C, a novel growth factor, in human dermal fibroblasts."
Jinnin M., Ihn H., Mimura Y., Asano Y., Yamane K., Tamaki K.
J. Cell. Physiol. 202:510-517(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Platelet-derived growth factor C induces liver fibrosis, steatosis, and hepatocellular carcinoma."
Campbell J.S., Hughes S.D., Gilbertson D.G., Palmer T.E., Holdren M.S., Haran A.C., Odell M.M., Bauer R.L., Ren H.P., Haugen H.S., Yeh M.M., Fausto N.
Proc. Natl. Acad. Sci. U.S.A. 102:3389-3394(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Fibroblast growth factor 2 and transforming growth factor beta1 synergism in human bronchial smooth muscle cell proliferation."
Bosse Y., Thompson C., Stankova J., Rola-Pleszczynski M.
Am. J. Respir. Cell Mol. Biol. 34:746-753(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[26]"Nuclear localisation of endogenous SUMO-1-modified PDGF-C in human thyroid tissue and cell lines."
Reigstad L.J., Martinez A., Varhaug J.E., Lillehaug J.R.
Exp. Cell Res. 312:782-795(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUMOYLATION.
[27]"PDGF-C and -D induced proliferation/migration of human RPE is abolished by inflammatory cytokines."
Li R., Maminishkis A., Wang F.E., Miller S.S.
Invest. Ophthalmol. Vis. Sci. 48:5722-5732(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[28]"Increased expression of platelet-derived growth factor C messenger ribonucleic acid in uterine leiomyomata."
Hwu Y.M., Li S.H., Lee R.K., Tsai Y.H., Yeh T.S., Lin S.Y.
Fertil. Steril. 89:468-471(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[29]"Plasmin is the major protease responsible for processing PDGF-C in the vitreous of patients with proliferative vitreoretinopathy."
Lei H., Velez G., Hovland P., Hirose T., Kazlauskas A.
Invest. Ophthalmol. Vis. Sci. 49:42-48(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY PLG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF091434 mRNA. Translation: AAF00049.1.
AB033831 mRNA. Translation: BAB03266.1.
AF244813 mRNA. Translation: AAF80597.1.
AF260738 mRNA. Translation: AAK51637.1.
AM922296 mRNA. Translation: CAP58278.1.
AY358493 mRNA. Translation: AAQ88857.1.
AK300480 mRNA. Translation: BAG62196.1.
AC092608 Genomic DNA. Translation: AAY40906.1.
AC093325 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04874.1.
CH471056 Genomic DNA. Translation: EAX04875.1.
BC136662 mRNA. Translation: AAI36663.1.
RefSeqNP_057289.1. NM_016205.2.
UniGeneHs.570855.

3D structure databases

ProteinModelPortalQ9NRA1.
SMRQ9NRA1. Positions 9-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121032. 5 interactions.
DIPDIP-59339N.
IntActQ9NRA1. 1 interaction.
STRING9606.ENSP00000274071.

PTM databases

PhosphoSiteQ9NRA1.

Polymorphism databases

DMDM205830662.

Proteomic databases

PaxDbQ9NRA1.
PRIDEQ9NRA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000422544; ENSP00000410048; ENSG00000145431. [Q9NRA1-2]
ENST00000502773; ENSP00000422464; ENSG00000145431. [Q9NRA1-1]
ENST00000541126; ENSP00000442943; ENSG00000145431. [Q9NRA1-4]
GeneID56034.
KEGGhsa:56034.
UCSCuc003iph.2. human. [Q9NRA1-1]

Organism-specific databases

CTD56034.
GeneCardsGC04M157682.
HGNCHGNC:8801. PDGFC.
HPAHPA009134.
MIM608452. gene.
neXtProtNX_Q9NRA1.
PharmGKBPA33146.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG74970.
HOGENOMHOG000185996.
HOVERGENHBG057324.
InParanoidQ9NRA1.
KOK05450.
OMADCVCRGN.
OrthoDBEOG7VB2FN.
PhylomeDBQ9NRA1.
TreeFamTF332130.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ9NRA1.

Gene expression databases

ArrayExpressQ9NRA1.
BgeeQ9NRA1.
CleanExHS_PDGFC.
GenevestigatorQ9NRA1.

Family and domain databases

Gene3D2.60.120.290. 1 hit.
InterProIPR000859. CUB_dom.
IPR000072. PDGF/VEGF_dom.
IPR027123. PDGFC/D.
[Graphical view]
PANTHERPTHR10127:SF13. PTHR10127:SF13. 1 hit.
PfamPF00431. CUB. 1 hit.
PF00341. PDGF. 1 hit.
[Graphical view]
SMARTSM00042. CUB. 1 hit.
SM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMSSF49854. SSF49854. 1 hit.
PROSITEPS01180. CUB. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPDGFC.
GenomeRNAi56034.
NextBio35475084.
PROQ9NRA1.
SOURCESearch...

Entry information

Entry namePDGFC_HUMAN
AccessionPrimary (citable) accession number: Q9NRA1
Secondary accession number(s): B4DU34 expand/collapse secondary AC list , B9EGR8, Q4W5M9, Q9UL22
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: April 16, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM