PDGFC_MOUSE
ID PDGFC_MOUSE Reviewed; 345 AA.
AC Q8CI19; Q99JM4; Q9JHV8; Q9QY71;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Platelet-derived growth factor C;
DE Short=PDGF-C;
DE AltName: Full=Fallotein;
DE AltName: Full=Spinal cord-derived growth factor;
DE Short=SCDGF;
DE AltName: Full=VEGF-E;
DE Contains:
DE RecName: Full=Platelet-derived growth factor C, latent form;
DE Short=PDGFC latent form;
DE Contains:
DE RecName: Full=Platelet-derived growth factor C, receptor-binding form;
DE Short=PDGFC receptor-binding form;
DE Flags: Precursor;
GN Name=Pdgfc; Synonyms=Scdgf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=10960785; DOI=10.1016/s0925-4773(00)00425-1;
RA Ding H., Wu X., Kim I., Tam P.P., Koh G.Y., Nagy A.;
RT "The mouse Pdgfc gene: dynamic expression in embryonic tissues during
RT organogenesis.";
RL Mech. Dev. 96:209-213(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Tsai Y.-J., Lee R.K.-K., Chen Y.-H., Lin S.-P., Cheng W.T.-K.;
RT "cDNA cloning of fallotein from mouse ovary.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Gao Z., Hart C., Piddington C., Sheppard P., Shoemaker K., Gilbertson D.,
RA West J., O'Hara P.J.;
RT "Platelet-derived growth factor C (PDGF-C), a novel growth factor that
RT binds to PDGF alpha receptor.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum, Cerebellum, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=10806482; DOI=10.1038/35010579;
RA Li X., Ponten A., Aase K., Karlsson L., Abramsson A., Uutela M.,
RA Backstrom G., Hellstrom M., Bostrom H., Li H., Soriano P., Betsholtz C.,
RA Heldin C.H., Alitalo K., Ostman A., Eriksson U.;
RT "PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor.";
RL Nat. Cell Biol. 2:302-309(2000).
RN [7]
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=11297552; DOI=10.1074/jbc.m101056200;
RA Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O.,
RA Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M.,
RA Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.;
RT "Platelet-derived growth factor C (PDGF-C), a novel growth factor that
RT binds to PDGF alpha and beta receptor.";
RL J. Biol. Chem. 276:27406-27414(2001).
RN [8]
RP INDUCTION.
RX PubMed=11313995; DOI=10.1038/sj.onc.1204133;
RA Zwerner J.P., May W.A.;
RT "PDGF-C is an EWS/FLI induced transforming growth factor in Ewing family
RT tumors.";
RL Oncogene 20:626-633(2001).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=11744381; DOI=10.1016/s0925-4773(01)00560-3;
RA Aase K., Abramsson A., Karlsson L., Betsholtz C., Eriksson U.;
RT "Expression analysis of PDGF-C in adult and developing mouse tissues.";
RL Mech. Dev. 110:187-191(2002).
RN [10]
RP FUNCTION.
RX PubMed=12875986; DOI=10.1016/s0002-9440(10)63694-2;
RA Ponten A., Li X., Thoren P., Aase K., Sjoblom T., Ostman A., Eriksson U.;
RT "Transgenic overexpression of platelet-derived growth factor-C in the mouse
RT heart induces cardiac fibrosis, hypertrophy, and dilated cardiomyopathy.";
RL Am. J. Pathol. 163:673-682(2003).
RN [11]
RP FUNCTION, AND INDUCTION BY BLEOMYCIN.
RX PubMed=12972405; DOI=10.1152/ajplung.00083.2003;
RA Zhuo Y., Zhang J., Laboy M., Lasky J.A.;
RT "Modulation of PDGF-C and PDGF-D expression during bleomycin-induced lung
RT fibrosis.";
RL Am. J. Physiol. 286:L182-L188(2004).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=15061151; DOI=10.1161/01.atv.0000120785.82268.8b;
RA Fang L., Yan Y., Komuves L.G., Yonkovich S., Sullivan C.M., Stringer B.,
RA Galbraith S., Lokker N.A., Hwang S.S., Nurden P., Phillips D.R.,
RA Giese N.A.;
RT "PDGF C is a selective alpha platelet-derived growth factor receptor
RT agonist that is highly expressed in platelet alpha granules and vascular
RT smooth muscle.";
RL Arterioscler. Thromb. Vasc. Biol. 24:787-792(2004).
RN [13]
RP REVIEW.
RX PubMed=15207812; DOI=10.1016/j.cytogfr.2004.03.003;
RA Tallquist M., Kazlauskas A.;
RT "PDGF signaling in cells and mice.";
RL Cytokine Growth Factor Rev. 15:205-213(2004).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND ACTIVATION BY
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=15372073; DOI=10.1038/sj.emboj.7600397;
RA Fredriksson L., Li H., Fieber C., Li X., Eriksson U.;
RT "Tissue plasminogen activator is a potent activator of PDGF-CC.";
RL EMBO J. 23:3793-3802(2004).
RN [15]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15361870; DOI=10.1038/ng1415;
RA Ding H., Wu X., Bostrom H., Kim I., Wong N., Tsoi B., O'Rourke M.,
RA Koh G.Y., Soriano P., Betsholtz C., Hart T.C., Marazita M.L., Field L.L.,
RA Tam P.P., Nagy A.;
RT "A specific requirement for PDGF-C in palate formation and PDGFR-alpha
RT signaling.";
RL Nat. Genet. 36:1111-1116(2004).
RN [16]
RP FUNCTION, INDUCTION BY COXSACKIEVIRUS B3 INFECTION, AND DISEASE.
RX PubMed=15757957; DOI=10.1093/eurheartj/ehi201;
RA Yang D., Qiu D.;
RT "Linkage between elevated PDGF-C expression and myocardial fibrogenesis in
RT coxsackievirus B3-induced chronic myocarditis.";
RL Eur. Heart J. 26:642-643(2005).
RN [17]
RP INDUCTION.
RX PubMed=15911618; DOI=10.1074/jbc.m503388200;
RA Fredriksson L., Ehnman M., Fieber C., Eriksson U.;
RT "Structural requirements for activation of latent platelet-derived growth
RT factor CC by tissue plasminogen activator.";
RL J. Biol. Chem. 280:26856-26862(2005).
RN [18]
RP INDUCTION BY RETINOIC ACID.
RX PubMed=17066417; DOI=10.1002/bdrb.20094;
RA Han J., Xiao Y., Lin J., Li Y.;
RT "PDGF-C controls proliferation and is down-regulated by retinoic acid in
RT mouse embryonic palatal mesenchymal cells.";
RL Birth Defects Res. B Dev. Reprod. Toxicol. 77:438-444(2006).
RN [19]
RP TISSUE SPECIFICITY, AND INDUCTION BY GONADOTROPIN.
RX PubMed=16344272; DOI=10.1093/carcin/bgi305;
RA Chen X., Aravindakshan J., Yang Y., Tiwari-Pandey R., Sairam M.R.;
RT "Aberrant expression of PDGF ligands and receptors in the tumor prone ovary
RT of follitropin receptor knockout (FORKO) mouse.";
RL Carcinogenesis 27:903-915(2006).
RN [20]
RP SUBCELLULAR LOCATION, AND SUMOYLATION.
RX PubMed=16443219; DOI=10.1016/j.yexcr.2005.11.035;
RA Reigstad L.J., Martinez A., Varhaug J.E., Lillehaug J.R.;
RT "Nuclear localisation of endogenous SUMO-1-modified PDGF-C in human thyroid
RT tissue and cell lines.";
RL Exp. Cell Res. 312:782-795(2006).
RN [21]
RP TISSUE SPECIFICITY, AND INDUCTION BY IL13.
RX PubMed=16951379; DOI=10.4049/jimmunol.177.6.4141;
RA Ingram J.L., Antao-Menezes A., Mangum J.B., Lyght O., Lee P.J., Elias J.A.,
RA Bonner J.C.;
RT "Opposing actions of Stat1 and Stat6 on IL-13-induced up-regulation of
RT early growth response-1 and platelet-derived growth factor ligands in
RT pulmonary fibroblasts.";
RL J. Immunol. 177:4141-4148(2006).
RN [22]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18184860; DOI=10.1681/asn.2007030290;
RA Eitner F., Bucher E., van Roeyen C., Kunter U., Rong S., Seikrit C.,
RA Villa L., Boor P., Fredriksson L., Backstrom G., Eriksson U., Ostman A.,
RA Floege J., Ostendorf T.;
RT "PDGF-C is a proinflammatory cytokine that mediates renal interstitial
RT fibrosis.";
RL J. Am. Soc. Nephrol. 19:281-289(2008).
CC -!- FUNCTION: Growth factor that plays an essential role in the regulation
CC of embryonic development, cell proliferation, cell migration, survival
CC and chemotaxis. Potent mitogen and chemoattractant for cells of
CC mesenchymal origin. Required for normal skeleton formation during
CC embryonic development, especially for normal development of the
CC craniofacial skeleton and for normal development of the palate.
CC Required for normal skin morphogenesis during embryonic development.
CC Plays an important role in wound healing, where it appears to be
CC involved in three stages: inflammation, proliferation and remodeling.
CC Plays an important role in angiogenesis and blood vessel development.
CC Involved in fibrotic processes, in which transformation of interstitial
CC fibroblasts into myofibroblasts plus collagen deposition occurs. The
CC CUB domain has mitogenic activity in coronary artery smooth muscle
CC cells, suggesting a role beyond the maintenance of the latency of the
CC PDGF domain. In the nucleus, PDGFC seems to have additional function.
CC {ECO:0000269|PubMed:10806482, ECO:0000269|PubMed:11297552,
CC ECO:0000269|PubMed:12875986, ECO:0000269|PubMed:12972405,
CC ECO:0000269|PubMed:15361870, ECO:0000269|PubMed:15372073,
CC ECO:0000269|PubMed:15757957, ECO:0000269|PubMed:18184860}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRA homodimers,
CC and with heterodimers formed by PDGFRA and PDGFRB. Interacts (via CUB
CC domain) with PLAT (via kringle domain) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16443219}.
CC Secreted {ECO:0000269|PubMed:15372073}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NRA1}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q9NRA1}. Cell membrane
CC {ECO:0000269|PubMed:16443219}. Note=Sumoylated form is predominant in
CC the nucleus (PubMed:16443219). Stored in alpha granules in platelets
CC (By similarity). {ECO:0000250|UniProtKB:Q9NRA1,
CC ECO:0000269|PubMed:16443219}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in kidney, testis, liver, heart
CC and brain (at protein level). Highly expressed in airway epithelium,
CC interstitial cells and alveolar macrophages in the lung of mice
CC overexpressing IL13. Expressed in the ovaries.
CC {ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11744381,
CC ECO:0000269|PubMed:16344272, ECO:0000269|PubMed:16951379,
CC ECO:0000269|PubMed:18184860}.
CC -!- DEVELOPMENTAL STAGE: In stage 9.5 dpc-15.5 dpc, widely expressed in the
CC surface ectoderm and later in the germinal layer of the skin, the
CC olfactory and otic placode and their derivatives and the lining of the
CC oral cavity. In stages 14.5 dpc-17.5 expressed in ducts connected to
CC epidermis, and in developing epidermal openings. Highly expressed in
CC the early stages of the developing kidney, in the metanephric
CC mesenchymal aggregates, prefusion skeletal muscle, cardiac myoblasts,
CC and in visceral and vascular smooth muscle.
CC {ECO:0000269|PubMed:10806482, ECO:0000269|PubMed:10960785,
CC ECO:0000269|PubMed:15061151, ECO:0000269|PubMed:15372073}.
CC -!- INDUCTION: Expression decreased by hypoxia. Up-regulated by EWS-FLI1
CC transcription factor in tumor-derived cells. Up-regulated by IL13
CC overexpression in the lung via STAT6 and EGR1. Elevated expression
CC induced by coxsackievirus B3 infection in immunodeficient mice.
CC Overexpressed in the renal fibrosis. Expression in the lung is
CC significantly increased after bleomycin treatment. Down-regulated by
CC retinoic acid and gonadotropin. {ECO:0000269|PubMed:11313995,
CC ECO:0000269|PubMed:12972405, ECO:0000269|PubMed:15757957,
CC ECO:0000269|PubMed:15911618, ECO:0000269|PubMed:16344272,
CC ECO:0000269|PubMed:16951379, ECO:0000269|PubMed:17066417}.
CC -!- PTM: Proteolytic removal of the N-terminal CUB domain releasing the
CC core domain is necessary for unmasking the receptor-binding epitopes of
CC the core domain. Cleavage after basic residues in the hinge region
CC (region connecting the CUB and growth factor domains) gives rise to the
CC receptor-binding form. Cleaved by PLAT and PLG (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Sumoylated by SUMO1. {ECO:0000269|PubMed:16443219}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- DISEASE: Note=Involved in the development of myocarditis and subsequent
CC fibrosis in the experimental model of coxsackievirus B3-induced chronic
CC myocarditis. {ECO:0000269|PubMed:15757957}.
CC -!- DISRUPTION PHENOTYPE: Perinatal lethality. Mice have feeding and
CC respiratory difficulties due to a complete cleft of the secondary
CC palate. However, they have reduction of renal fibrogenesis. Mice
CC lacking both PDGFA and PDGFC develop a cleft face, subepidermal
CC blistering, deficiency of renal cortex mesenchyme, spina bifida and
CC skeletal and vascular defects. {ECO:0000269|PubMed:15361870,
CC ECO:0000269|PubMed:18184860}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; AF286725; AAF91483.1; -; mRNA.
DR EMBL; AF117608; AAF22516.1; -; mRNA.
DR EMBL; AF266467; AAK58566.1; -; mRNA.
DR EMBL; AK033734; BAC28455.1; -; mRNA.
DR EMBL; AK042767; BAC31358.1; -; mRNA.
DR EMBL; AK052947; BAC35216.1; -; mRNA.
DR EMBL; BC006027; AAH06027.1; -; mRNA.
DR EMBL; BC037696; AAH37696.1; -; mRNA.
DR CCDS; CCDS17425.1; -.
DR RefSeq; NP_064355.1; NM_019971.2.
DR AlphaFoldDB; Q8CI19; -.
DR SMR; Q8CI19; -.
DR ComplexPortal; CPX-2909; Platelet-derived growth factor CC complex.
DR ComplexPortal; CPX-2912; PDGF receptor alpha - PDGF-CC complex.
DR ComplexPortal; CPX-2913; PDGF receptor alpha-beta - PDGF-CC complex.
DR ComplexPortal; CPX-2914; PDGF receptor beta - PDGF-CC complex.
DR STRING; 10090.ENSMUSP00000029652; -.
DR GlyGen; Q8CI19; 2 sites.
DR PhosphoSitePlus; Q8CI19; -.
DR PaxDb; Q8CI19; -.
DR PeptideAtlas; Q8CI19; -.
DR PRIDE; Q8CI19; -.
DR ProteomicsDB; 301781; -.
DR Antibodypedia; 28096; 309 antibodies from 29 providers.
DR DNASU; 54635; -.
DR Ensembl; ENSMUST00000029652; ENSMUSP00000029652; ENSMUSG00000028019.
DR GeneID; 54635; -.
DR KEGG; mmu:54635; -.
DR UCSC; uc008poi.1; mouse.
DR CTD; 56034; -.
DR MGI; MGI:1859631; Pdgfc.
DR VEuPathDB; HostDB:ENSMUSG00000028019; -.
DR eggNOG; ENOG502QUUR; Eukaryota.
DR GeneTree; ENSGT00940000158645; -.
DR HOGENOM; CLU_037859_0_0_1; -.
DR InParanoid; Q8CI19; -.
DR OMA; LDENVWI; -.
DR OrthoDB; 962163at2759; -.
DR PhylomeDB; Q8CI19; -.
DR TreeFam; TF332130; -.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR BioGRID-ORCS; 54635; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Pdgfc; mouse.
DR PRO; PR:Q8CI19; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8CI19; protein.
DR Bgee; ENSMUSG00000028019; Expressed in indifferent gonad and 284 other tissues.
DR ExpressionAtlas; Q8CI19; baseline and differential.
DR Genevisible; Q8CI19; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0070851; F:growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IDA:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0060348; P:bone development; IGI:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0048565; P:digestive tract development; IGI:MGI.
DR GO; GO:0048568; P:embryonic organ development; IEA:InterPro.
DR GO; GO:0048144; P:fibroblast proliferation; IDA:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00135; PDGF; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR029817; PDGF-C.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR11633:SF5; PTHR11633:SF5; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00341; PDGF; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cleavage on pair of basic residues; Cytoplasm;
KW Developmental protein; Disulfide bond; Glycoprotein; Growth factor;
KW Membrane; Mitogen; Nucleus; Reference proteome; Secreted; Signal;
KW Ubl conjugation.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..345
FT /note="Platelet-derived growth factor C, latent form"
FT /id="PRO_0000343873"
FT CHAIN ?..345
FT /note="Platelet-derived growth factor C, receptor-binding
FT form"
FT /id="PRO_0000343874"
FT DOMAIN 46..163
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 225..226
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 231..232
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 234..235
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 250..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 274
FT /note="Interchain (with C-286)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 280..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 286
FT /note="Interchain (with C-274)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 287..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT CONFLICT 86
FT /note="I -> T (in Ref. 1; AAF91483)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="I -> L (in Ref. 5; AAH37696)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="G -> E (in Ref. 1; AAF91483)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="G -> V (in Ref. 1; AAF91483)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="I -> R (in Ref. 1; AAF91483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 38741 MW; 3A58A1F701B84EA2 CRC64;
MLLLGLLLLT SALAGQRTGT RAESNLSSKL QLSSDKEQNG VQDPRHERVV TISGNGSIHS
PKFPHTYPRN MVLVWRLVAV DENVRIQLTF DERFGLEDPE DDICKYDFVE VEEPSDGSVL
GRWCGSGTVP GKQTSKGNHI RIRFVSDEYF PSEPGFCIHY SIIMPQVTET TSPSVLPPSS
LSLDLLNNAV TAFSTLEELI RYLEPDRWQV DLDSLYKPTW QLLGKAFLYG KKSKVVNLNL
LKEEVKLYSC TPRNFSVSIR EELKRTDTIF WPGCLLVKRC GGNCACCLHN CNECQCVPRK
VTKKYHEVLQ LRPKTGVKGL HKSLTDVALE HHEECDCVCR GNAGG
