Q9NRA1 (PDGFC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.12 Ref.13 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25
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.15 Ref.17 Ref.20
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.16 Ref.17 Ref.20 Ref.24
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.9 Ref.11 Ref.12 Ref.16 Ref.25 Ref.26
Developmental stage	In the fetal kidney, detected in the developing mesangium, ureteric bud epithelium and the undifferentiated mesenchyme (at protein level). Ref.14
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.10 Ref.14 Ref.18 Ref.23
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.24 N-glycosylated. Ref.12
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 component	Cytoplasm Nucleus Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Developmental protein Growth factor Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of transmembrane receptor protein tyrosine kinase activity Inferred from electronic annotation. Source: Compara cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara central nervous system development Traceable author statement Ref.2. Source: UniProtKB organ morphogenesis Inferred from electronic annotation. Source: Compara 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: Compara vascular endothelial growth factor receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular space Inferred from direct assay Ref.3. Source: BHF-UCL nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cell surface binding Inferred from direct assay Ref.3. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 345	323	Platelet-derived growth factor C, latent form		PRO_0000343871
	Chain	? – 345		Platelet-derived growth factor C, receptor-binding form		PRO_0000343872
Regions
	Domain	46 – 163	118	CUB
Sites
	Site	225 – 226	2	Cleavage
	Site	231 – 232	2	Cleavage Potential
	Site	234 – 235	2	Cleavage Potential
Amino acid modifications
	Glycosylation	25	1	N-linked (GlcNAc...) Potential
	Glycosylation	55	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	104 ↔ 124		By similarity
	Disulfide bond	250 ↔ 294		Probable
	Disulfide bond	274		Interchain (with C-286) Probable
	Disulfide bond	280 ↔ 335		Probable
	Disulfide bond	286		Interchain (with C-274) Probable
	Disulfide bond	287 ↔ 337		Probable
Natural variations
	Alternative sequence	155 – 167	13	GFCIH…VMPQF → SNRGGKIIQLHTS in isoform 3.		VSP_034701
	Alternative sequence	168 – 345	178	Missing in isoform 3.		VSP_034702
	Alternative sequence	244 – 306	63	Missing in isoform 2.		VSP_034703
Experimental info
	Mutagenesis	124	1	C → S: Loss of mitogenic activity of CUB domain in coronary artery smooth muscle cells. Ref.12
	Mutagenesis	231	1	R → A: Essential for cleavage by PLAT. Ref.20
	Mutagenesis	232	1	K → A: Not essential for cleavage by PLAT. Ref.20
	Mutagenesis	234	1	R → A: Not essential for cleavage by PLAT. Ref.20
	Sequence conflict	9	1	L → V in AAF80597. Ref.3
	Sequence conflict	18	1	Q → R in AAF80597. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: CDE9E51F40633E78	FASTA	345	39,029
	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
	Isoform 2 [UniParc]. Checksum: 8426CEB8FF9AA45B	FASTA	282	31,808
	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 LTEEVLQLRP KTGVRGLHKS LTDVALEHHE ECDCVCRGST GG
	Isoform 3 [UniParc]. Checksum: 60023851D9FE5E65	FASTA	167	18,784
	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 GRWCGSGTVP GKQISKGNQI RIRFVSDEYF PSEPSNRGGK IIQLHTS

References

	« Hide 'large scale' referencesShow '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]	"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. , 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).
[6]	"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. , 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].
[7]	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. , 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].
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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. AY358493 mRNA. Translation: AAQ88857.1. AC092608 Genomic DNA. Translation: AAY40906.1. AC093325 Genomic DNA. No translation available. CH471056 Genomic DNA. Translation: EAX04874.1. BC136662 mRNA. Translation: AAI36663.1.
IPI	IPI00099977. IPI00900287. IPI00900346.
RefSeq	NP_057289.1. NM_016205.2.
UniGene	Hs.570855.
3D structure databases
HSSP	HSSP built from PDB template 1NT0 based on UniProtKB Q9QX89.
ProteinModelPortal	Q9NRA1.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59339N.
STRING	9606.ENSP00000274071.
PTM databases
PhosphoSite	Q9NRA1.
Polymorphism databases
DMDM	205830662.
Proteomic databases
PaxDb	Q9NRA1.
PRIDE	Q9NRA1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000422544; ENSP00000410048; ENSG00000145431. ENST00000502773; ENSP00000422464; ENSG00000145431.
GeneID	56034.
KEGG	hsa:56034.
UCSC	uc003iph.2. human.
Organism-specific databases
CTD	56034.
GeneCards	GC04M157682.
HGNC	HGNC:8801. PDGFC.
HPA	HPA009134.
MIM	608452. gene.
neXtProt	NX_Q9NRA1.
PharmGKB	PA33146.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG74970.
HOGENOM	HOG000185996.
HOVERGEN	HBG057324.
InParanoid	Q9NRA1.
KO	K05450.
OMA	HEVLQLK.
OrthoDB	EOG47D9GQ.
PhylomeDB	Q9NRA1.
Enzyme and pathway databases
Pathway_Interaction_DB	pdgfrapathway. PDGFR-alpha signaling pathway.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q9NRA1.
Bgee	Q9NRA1.
CleanEx	HS_PDGFC.
Genevestigator	Q9NRA1.
Family and domain databases
Gene3D	2.60.120.290. 1 hit.
InterPro	IPR000859. CUB_dom. IPR000072. PD_growth_factor. [Graphical view]
Pfam	PF00431. CUB. 1 hit. PF00341. PDGF. 1 hit. [Graphical view]
SMART	SM00042. CUB. 1 hit. SM00141. PDGF. 1 hit. [Graphical view]
SUPFAM	SSF49854. CUB. 1 hit.
PROSITE	PS01180. CUB. 1 hit. PS00249. PDGF_1. False negative. PS50278. PDGF_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	56034.
NextBio	61471.
SOURCE	Search...

Entry information

Entry name

PDGFC_HUMAN

Accession

Primary (citable) accession number: Q9NRA1
Secondary accession number(s): B9EGR8, Q4W5M9, Q9UL22

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	July 22, 2008
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.