Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Platelet-derived growth factor C (PDGF-C) (Fallotein) (Spinal cord-derived growth factor) (SCDGF) (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_HUMAN             Reviewed;         345 AA.
Q9NRA1; B4DU34; B9EGR8; Q4W5M9; Q9UL22;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
18-JUL-2018, entry version 131.
RecName: Full=Platelet-derived growth factor C;
Short=PDGF-C;
AltName: Full=Fallotein;
AltName: Full=Spinal cord-derived growth factor;
Short=SCDGF;
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; ORFNames=UNQ174/PRO200;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Uterus;
PubMed=11004490; DOI=10.1016/S0167-4781(00)00066-X;
Tsai Y.J., Lee R.K., Lin S.P., Chen Y.H.;
"Identification of a novel platelet-derived growth factor-like gene,
fallotein, in the human reproductive tract.";
Biochim. Biophys. Acta 1492:196-202(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Brain;
PubMed=10858496; DOI=10.1016/S0014-5793(00)01640-9;
Hamada T., Ui-Tei K., Miyata Y.;
"A novel gene derived from developing spinal cords, SCDGF, is a unique
member of the PDGF/VEGF family.";
FEBS Lett. 475:97-102(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
TISSUE=Lung;
PubMed=10806482; DOI=10.1038/35010579;
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.;
"PDGF-C is a new protease-activated ligand for the PDGF alpha-
receptor.";
Nat. Cell Biol. 2:302-309(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
PubMed=11297552; DOI=10.1074/jbc.M101056200;
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.;
"Platelet-derived growth factor C (PDGF-C), a novel growth factor that
binds to PDGF alpha and beta receptor.";
J. Biol. Chem. 276:27406-27414(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Fetal brain;
Zhao J., Liu Z., Liu T., Nilsson S., Nister M.;
"An N-terminally truncated isoform of human PDGF-C regulates the
secretion of full-length PDGF-C and is deregulated in renal cell
carcinoma.";
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
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.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
TISSUE SPECIFICITY.
PubMed=11342471; DOI=10.1161/01.CIR.103.18.2242;
Uutela M., Lauren J., Bergsten E., Li X., Horelli-Kuitunen N.,
Eriksson U., Alitalo K.;
"Chromosomal location, exon structure, and vascular expression
patterns of the human PDGFC and PDGFC genes.";
Circulation 103:2242-2247(2001).
[12]
INDUCTION.
PubMed=11313995; DOI=10.1038/sj.onc.1204133;
Zwerner J.P., May W.A.;
"PDGF-C is an EWS/FLI induced transforming growth factor in Ewing
family tumors.";
Oncogene 20:626-633(2001).
[13]
TISSUE SPECIFICITY.
PubMed=12176024; DOI=10.1016/S0006-291X(02)00917-8;
Andrae J., Molander C., Smits A., Funa K., Nister M.;
"Platelet-derived growth factor-B and -C and active alpha-receptors in
medulloblastoma cells.";
Biochem. Biophys. Res. Commun. 296:604-611(2002).
[14]
FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 2 AND 3),
GLYCOSYLATION, AND MUTAGENESIS OF CYS-124.
PubMed=11854040; DOI=10.1016/S1357-2725(01)00124-8;
Dijkmans J., Xu J., Masure S., Dhanaraj S., Gosiewska A., Geesin J.,
Sprengel J., Harris S., Verhasselt P., Gordon R., Yon J.;
"Characterization of platelet-derived growth factor-C (PDGF-C):
expression in normal and tumor cells, biological activity and
chromosomal localization.";
Int. J. Biochem. Cell Biol. 34:414-426(2002).
[15]
FUNCTION.
PubMed=12032822; DOI=10.1038/sj.onc.1205486;
Zwerner J.P., May W.A.;
"Dominant negative PDGF-C inhibits growth of Ewing family tumor cell
lines.";
Oncogene 21:3847-3854(2002).
[16]
DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=12707385; DOI=10.1097/01.ASN.0000062964.75006.A8;
Eitner F., Ostendorf T., Kretzler M., Cohen C.D., Eriksson U.,
Grone H.J., Floege J.;
"PDGF-C expression in the developing and normal adult human kidney and
in glomerular diseases.";
J. Am. Soc. Nephrol. 14:1145-1153(2003).
[17]
CHARACTERIZATION OF SECRETED ACTIVE FORM, SUBUNIT, DISULFIDE BONDS,
AND 3D-STRUCTURE MODELING.
PubMed=12598536; DOI=10.1074/jbc.M301728200;
Reigstad L.J., Sande H.M., Fluge O., Bruland O., Muga A.,
Varhaug J.E., Martinez A., Lillehaug J.R.;
"Platelet-derived growth factor (PDGF)-C, a PDGF family member with a
vascular endothelial growth factor-like structure.";
J. Biol. Chem. 278:17114-17120(2003).
[18]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15061151; DOI=10.1161/01.ATV.0000120785.82268.8b;
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.;
"PDGF C is a selective alpha platelet-derived growth factor receptor
agonist that is highly expressed in platelet alpha granules and
vascular smooth muscle.";
Arterioscler. Thromb. Vasc. Biol. 24:787-792(2004).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLAT.
PubMed=15372073; DOI=10.1038/sj.emboj.7600397;
Fredriksson L., Li H., Fieber C., Li X., Eriksson U.;
"Tissue plasminogen activator is a potent activator of PDGF-CC.";
EMBO J. 23:3793-3802(2004).
[20]
INDUCTION BY EGR1.
PubMed=15247255; DOI=10.1074/jbc.M406063200;
Midgley V.C., Khachigian L.M.;
"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.";
J. Biol. Chem. 279:40289-40295(2004).
[21]
REVIEW.
PubMed=16279938; DOI=10.1111/j.1742-4658.2005.04989.x;
Reigstad L.J., Varhaug J.E., Lillehaug J.R.;
"Structural and functional specificities of PDGF-C and PDGF-D, the
novel members of the platelet-derived growth factors family.";
FEBS J. 272:5723-5741(2005).
[22]
FUNCTION, INTERACTION WITH PLAT, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF ARG-231; LYS-232 AND ARG-234.
PubMed=15911618; DOI=10.1074/jbc.M503388200;
Fredriksson L., Ehnman M., Fieber C., Eriksson U.;
"Structural requirements for activation of latent platelet-derived
growth factor CC by tissue plasminogen activator.";
J. Biol. Chem. 280:26856-26862(2005).
[23]
FUNCTION.
PubMed=15389578; DOI=10.1002/jcp.20154;
Jinnin M., Ihn H., Mimura Y., Asano Y., Yamane K., Tamaki K.;
"Regulation of fibrogenic/fibrolytic genes by platelet-derived growth
factor C, a novel growth factor, in human dermal fibroblasts.";
J. Cell. Physiol. 202:510-517(2005).
[24]
FUNCTION.
PubMed=15728360; DOI=10.1073/pnas.0409722102;
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.;
"Platelet-derived growth factor C induces liver fibrosis, steatosis,
and hepatocellular carcinoma.";
Proc. Natl. Acad. Sci. U.S.A. 102:3389-3394(2005).
[25]
FUNCTION, AND INDUCTION.
PubMed=16439802; DOI=10.1165/rcmb.2005-0309OC;
Bosse Y., Thompson C., Stankova J., Rola-Pleszczynski M.;
"Fibroblast growth factor 2 and transforming growth factor beta1
synergism in human bronchial smooth muscle cell proliferation.";
Am. J. Respir. Cell Mol. Biol. 34:746-753(2006).
[26]
SUBCELLULAR LOCATION, AND SUMOYLATION.
PubMed=16443219; DOI=10.1016/j.yexcr.2005.11.035;
Reigstad L.J., Martinez A., Varhaug J.E., Lillehaug J.R.;
"Nuclear localisation of endogenous SUMO-1-modified PDGF-C in human
thyroid tissue and cell lines.";
Exp. Cell Res. 312:782-795(2006).
[27]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18055825; DOI=10.1167/iovs.07-0327;
Li R., Maminishkis A., Wang F.E., Miller S.S.;
"PDGF-C and -D induced proliferation/migration of human RPE is
abolished by inflammatory cytokines.";
Invest. Ophthalmol. Vis. Sci. 48:5722-5732(2007).
[28]
TISSUE SPECIFICITY.
PubMed=17482170; DOI=10.1016/j.fertnstert.2007.02.031;
Hwu Y.M., Li S.H., Lee R.K., Tsai Y.H., Yeh T.S., Lin S.Y.;
"Increased expression of platelet-derived growth factor C messenger
ribonucleic acid in uterine leiomyomata.";
Fertil. Steril. 89:468-471(2008).
[29]
CLEAVAGE BY PLG.
PubMed=18172073; DOI=10.1167/iovs.07-0776;
Lei H., Velez G., Hovland P., Hirose T., Kazlauskas A.;
"Plasmin is the major protease responsible for processing PDGF-C in
the vitreous of patients with proliferative vitreoretinopathy.";
Invest. Ophthalmol. Vis. Sci. 49:42-48(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. {ECO:0000269|PubMed:10806482,
ECO:0000269|PubMed:10858496, ECO:0000269|PubMed:11297552,
ECO:0000269|PubMed:11854040, ECO:0000269|PubMed:12032822,
ECO:0000269|PubMed:15061151, ECO:0000269|PubMed:15372073,
ECO:0000269|PubMed:15389578, ECO:0000269|PubMed:15728360,
ECO:0000269|PubMed:15911618, ECO:0000269|PubMed:16439802,
ECO:0000269|PubMed:18055825}.
-!- 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).
{ECO:0000269|PubMed:12598536, ECO:0000269|PubMed:15372073,
ECO:0000269|PubMed:15911618}.
-!- INTERACTION:
P16234:PDGFRA; NbExp=2; IntAct=EBI-8833587, EBI-2861522;
P16234-1:PDGFRA; NbExp=2; IntAct=EBI-15499301, EBI-15499330;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:16443219}. Secreted
{ECO:0000269|PubMed:10806482, ECO:0000269|PubMed:10858496,
ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:15061151,
ECO:0000269|PubMed:15372073, ECO:0000269|PubMed:15911618}. Nucleus
{ECO:0000269|PubMed:16443219}. Cytoplasmic granule
{ECO:0000269|PubMed:15061151}. Cell membrane
{ECO:0000269|PubMed:16443219}. Note=Sumoylated form is predominant
in the nucleus (PubMed:15247255). Stored in alpha granules in
platelets (PubMed:15061151). {ECO:0000269|PubMed:16443219}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9NRA1-1; Sequence=Displayed;
Name=2;
IsoId=Q9NRA1-2; Sequence=VSP_034703;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NRA1-3; Sequence=VSP_034701, VSP_034702;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9NRA1-4; Sequence=VSP_047606;
Note=No experimental confirmation available.;
-!- 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. {ECO:0000269|PubMed:10806482,
ECO:0000269|PubMed:11004490, ECO:0000269|PubMed:11297552,
ECO:0000269|PubMed:11342471, ECO:0000269|PubMed:11854040,
ECO:0000269|PubMed:12176024, ECO:0000269|PubMed:15061151,
ECO:0000269|PubMed:17482170, ECO:0000269|PubMed:18055825}.
-!- DEVELOPMENTAL STAGE: In the fetal kidney, detected in the
developing mesangium, ureteric bud epithelium and the
undifferentiated mesenchyme (at protein level).
{ECO:0000269|PubMed:12707385}.
-!- 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. {ECO:0000269|PubMed:11313995, ECO:0000269|PubMed:12707385,
ECO:0000269|PubMed:15247255, ECO:0000269|PubMed:16439802}.
-!- 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.
-!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:16443219}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:11854040}.
-!- MISCELLANEOUS: A lower molecular weight form (around 43 kDa) is
present in patients with papillary thyroid carcinoma.
-!- 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; AF091434; AAF00049.1; -; mRNA.
EMBL; AB033831; BAB03266.1; -; mRNA.
EMBL; AF244813; AAF80597.1; -; mRNA.
EMBL; AF260738; AAK51637.1; -; mRNA.
EMBL; AM922296; CAP58278.1; -; mRNA.
EMBL; AY358493; AAQ88857.1; -; mRNA.
EMBL; AK300480; BAG62196.1; -; mRNA.
EMBL; AC092608; AAY40906.1; -; Genomic_DNA.
EMBL; AC093325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471056; EAX04874.1; -; Genomic_DNA.
EMBL; CH471056; EAX04875.1; -; Genomic_DNA.
EMBL; BC136662; AAI36663.1; -; mRNA.
CCDS; CCDS3795.1; -. [Q9NRA1-1]
RefSeq; NP_057289.1; NM_016205.2. [Q9NRA1-1]
RefSeq; XP_016863945.1; XM_017008456.1. [Q9NRA1-2]
UniGene; Hs.570855; -.
ProteinModelPortal; Q9NRA1; -.
SMR; Q9NRA1; -.
BioGrid; 121032; 7.
ComplexPortal; CPX-2879; Platelet-derived growth factor CC complex.
ComplexPortal; CPX-2887; PDGF receptor alpha - PDGF-CC complex.
ComplexPortal; CPX-2888; PDGF receptor alpha-beta - PDGF-CC complex.
ComplexPortal; CPX-2891; PDGF receptor beta - PDGF-CC complex.
DIP; DIP-59339N; -.
IntAct; Q9NRA1; 4.
STRING; 9606.ENSP00000422464; -.
iPTMnet; Q9NRA1; -.
PhosphoSitePlus; Q9NRA1; -.
BioMuta; PDGFC; -.
DMDM; 205830662; -.
EPD; Q9NRA1; -.
PaxDb; Q9NRA1; -.
PeptideAtlas; Q9NRA1; -.
PRIDE; Q9NRA1; -.
ProteomicsDB; 82318; -.
ProteomicsDB; 82319; -. [Q9NRA1-2]
ProteomicsDB; 82320; -. [Q9NRA1-3]
Ensembl; ENST00000422544; ENSP00000410048; ENSG00000145431. [Q9NRA1-2]
Ensembl; ENST00000502773; ENSP00000422464; ENSG00000145431. [Q9NRA1-1]
GeneID; 56034; -.
KEGG; hsa:56034; -.
UCSC; uc003iph.3; human. [Q9NRA1-1]
CTD; 56034; -.
DisGeNET; 56034; -.
EuPathDB; HostDB:ENSG00000145431.10; -.
GeneCards; PDGFC; -.
HGNC; HGNC:8801; PDGFC.
HPA; HPA009134; -.
MIM; 608452; gene.
neXtProt; NX_Q9NRA1; -.
OpenTargets; ENSG00000145431; -.
PharmGKB; PA33146; -.
eggNOG; ENOG410IETQ; Eukaryota.
eggNOG; ENOG410XQ91; LUCA.
GeneTree; ENSGT00390000005171; -.
HOGENOM; HOG000185996; -.
HOVERGEN; HBG057324; -.
InParanoid; Q9NRA1; -.
KO; K05450; -.
OMA; HTYPRNM; -.
OrthoDB; EOG091G0BFZ; -.
PhylomeDB; Q9NRA1; -.
TreeFam; TF332130; -.
Reactome; R-HSA-186797; Signaling by PDGF.
SignaLink; Q9NRA1; -.
SIGNOR; Q9NRA1; -.
ChiTaRS; PDGFC; human.
GeneWiki; PDGFC; -.
GenomeRNAi; 56034; -.
PRO; PR:Q9NRA1; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000145431; -.
CleanEx; HS_PDGFC; -.
ExpressionAtlas; Q9NRA1; baseline and differential.
Genevisible; Q9NRA1; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
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:0007596; P:blood coagulation; IBA:GO_Central.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0007417; P:central nervous system development; TAS:UniProtKB.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0009790; P:embryo development; IEA:InterPro.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
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; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
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;
Alternative splicing; 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_0000343871.
CHAIN ? 345 Platelet-derived growth factor C,
receptor-binding form.
/FTId=PRO_0000343872.
DOMAIN 46 163 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
SITE 225 226 Cleavage.
SITE 231 232 Cleavage. {ECO:0000255}.
SITE 234 235 Cleavage. {ECO:0000255}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 104 124 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 250 294 {ECO:0000305|PubMed:12598536}.
DISULFID 274 274 Interchain (with C-286).
{ECO:0000305|PubMed:12598536}.
DISULFID 280 335 {ECO:0000305|PubMed:12598536}.
DISULFID 286 286 Interchain (with C-274).
{ECO:0000305|PubMed:12598536}.
DISULFID 287 337 {ECO:0000305|PubMed:12598536}.
VAR_SEQ 1 163 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.5}.
/FTId=VSP_047606.
VAR_SEQ 155 167 GFCIHYNIVMPQF -> SNRGGKIIQLHTS (in
isoform 3). {ECO:0000305}.
/FTId=VSP_034701.
VAR_SEQ 168 345 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_034702.
VAR_SEQ 244 306 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_034703.
MUTAGEN 124 124 C->S: Loss of mitogenic activity of CUB
domain in coronary artery smooth muscle
cells. {ECO:0000269|PubMed:11854040}.
MUTAGEN 231 231 R->A: Essential for cleavage by PLAT.
{ECO:0000269|PubMed:15911618}.
MUTAGEN 232 232 K->A: Not essential for cleavage by PLAT.
{ECO:0000269|PubMed:15911618}.
MUTAGEN 234 234 R->A: Not essential for cleavage by PLAT.
{ECO:0000269|PubMed:15911618}.
CONFLICT 9 9 L -> V (in Ref. 3; AAF80597).
{ECO:0000305}.
CONFLICT 18 18 Q -> R (in Ref. 3; AAF80597).
{ECO:0000305}.
SEQUENCE 345 AA; 39029 MW; CDE9E51F40633E78 CRC64;
MSLFGLLLLT SALAGQRQGT QAESNLSSKF QFSSNKEQNG VQDPQHERII TVSTNGSIHS
PRFPHTYPRN TVLVWRLVAV EENVWIQLTF DERFGLEDPE DDICKYDFVE VEEPSDGTIL
GRWCGSGTVP GKQISKGNQI RIRFVSDEYF PSEPGFCIHY NIVMPQFTEA VSPSVLPPSA
LPLDLLNNAI TAFSTLEDLI RYLEPERWQL DLEDLYRPTW QLLGKAFVFG RKSRVVDLNL
LTEEVRLYSC TPRNFSVSIR EELKRTDTIF WPGCLLVKRC GGNCACCLHN CNECQCVPSK
VTKKYHEVLQ LRPKTGVRGL HKSLTDVALE HHEECDCVCR GSTGG


Related products :

Catalog number Product name Quantity
U0528m CLIA Fallotein,Mouse,Mus musculus,Pdgfc,PDGF-C,Platelet-derived growth factor C,SCDGF,Scdgf,Spinal cord-derived growth factor,VEGF-E 96T
E0528m ELISA Fallotein,Mouse,Mus musculus,Pdgfc,PDGF-C,Platelet-derived growth factor C,SCDGF,Scdgf,Spinal cord-derived growth factor,VEGF-E 96T
E0528m ELISA kit Fallotein,Mouse,Mus musculus,Pdgfc,PDGF-C,Platelet-derived growth factor C,SCDGF,Scdgf,Spinal cord-derived growth factor,VEGF-E 96T
E0528h ELISA kit Fallotein,Homo sapiens,Human,PDGFC,PDGF-C,Platelet-derived growth factor C,SCDGF,SCDGF,Spinal cord-derived growth factor,UNQ174_PRO200,VEGF-E 96T
E0528h ELISA Fallotein,Homo sapiens,Human,PDGFC,PDGF-C,Platelet-derived growth factor C,SCDGF,SCDGF,Spinal cord-derived growth factor,UNQ174_PRO200,VEGF-E 96T
U0528h CLIA Fallotein,Homo sapiens,Human,PDGFC,PDGF-C,Platelet-derived growth factor C,SCDGF,SCDGF,Spinal cord-derived growth factor,UNQ174_PRO200,VEGF-E 96T
U0528r CLIA Fallotein,Pdgfc,PDGF-C,Platelet-derived growth factor C,Rat,Rattus norvegicus,rScdfg,Scdgf,Spinal cord-derived growth factor,VEGF-E 96T
E0528r ELISA Fallotein,Pdgfc,PDGF-C,Platelet-derived growth factor C,Rat,Rattus norvegicus,rScdfg,Scdgf,Spinal cord-derived growth factor,VEGF-E 96T
E0528r ELISA kit Fallotein,Pdgfc,PDGF-C,Platelet-derived growth factor C,Rat,Rattus norvegicus,rScdfg,Scdgf,Spinal cord-derived growth factor,VEGF-E 96T
E0528c ELISA kit Chicken,Gallus gallus,PDGFC,PDGF-C,Platelet-derived growth factor C,SCDGF,Spinal cord-derived growth factor 96T
E0528c ELISA Chicken,Gallus gallus,PDGFC,PDGF-C,Platelet-derived growth factor C,SCDGF,Spinal cord-derived growth factor 96T
U0528c CLIA Chicken,Gallus gallus,PDGFC,PDGF-C,Platelet-derived growth factor C,SCDGF,Spinal cord-derived growth factor 96T
EIAAB30355 Iegf,Iris-expressed growth factor,Pdgfd,PDGF-D,Platelet-derived growth factor D,Rat,Rattus norvegicus,Scdgfb,SCDGF-B,Spinal cord-derived growth factor B
EIAAB30356 Homo sapiens,Human,IEGF,Iris-expressed growth factor,MSTP036,PDGFD,PDGF-D,Platelet-derived growth factor D,SCDGFB,SCDGF-B,Spinal cord-derived growth factor B,UNQ1899_PRO4345
EIAAB30357 Mouse,Mus musculus,Pdgfd,PDGF-D,Platelet-derived growth factor D,Scdgfb,SCDGF-B,Spinal cord-derived growth factor B
U0633h CLIA Homo sapiens,Human,PDGF subunit B,PDGF2,PDGF-2,PDGFB,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogene 96T
E0633h ELISA Homo sapiens,Human,PDGF subunit B,PDGF2,PDGF-2,PDGFB,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogen 96T
E0633h ELISA kit Homo sapiens,Human,PDGF subunit B,PDGF2,PDGF-2,PDGFB,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-on 96T
U0633m CLIA Mouse,Mus musculus,PDGF subunit B,PDGF-2,Pdgfb,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogene c-Sis 96T
E0633m ELISA Mouse,Mus musculus,PDGF subunit B,PDGF-2,Pdgfb,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogene c-Si 96T
E0112h ELISA kit Homo sapiens,Human,PDGF subunit A,PDGF1,PDGF-1,PDGFA,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A 96T
E0112h ELISA Homo sapiens,Human,PDGF subunit A,PDGF1,PDGF-1,PDGFA,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A 96T
E0633m ELISA kit Mouse,Mus musculus,PDGF subunit B,PDGF-2,Pdgfb,Platelet-derived growth factor B chain,Platelet-derived growth factor beta polypeptide,Platelet-derived growth factor subunit B,Proto-oncogene 96T
U0112h CLIA Homo sapiens,Human,PDGF subunit A,PDGF1,PDGF-1,PDGFA,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A 96T
E0112r ELISA kit PDGF subunit A,PDGF-1,Pdgfa,Platelet-derived growth factor A chain,Platelet-derived growth factor alpha polypeptide,Platelet-derived growth factor subunit A,Rat,Rattus norvegicus,Rpa1 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur