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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_MOUSE             Reviewed;         345 AA.
Q8CI19; Q99JM4; Q9JHV8; Q9QY71;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
20-JUN-2018, entry version 117.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
STRAIN=Swiss Webster / NIH;
PubMed=10960785; DOI=10.1016/S0925-4773(00)00425-1;
Ding H., Wu X., Kim I., Tam P.P., Koh G.Y., Nagy A.;
"The mouse Pdgfc gene: dynamic expression in embryonic tissues during
organogenesis.";
Mech. Dev. 96:209-213(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
Tsai Y.-J., Lee R.K.-K., Chen Y.-H., Lin S.-P., Cheng W.T.-K.;
"cDNA cloning of fallotein from mouse ovary.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
Gao Z., Hart C., Piddington C., Sheppard P., Shoemaker K.,
Gilbertson D., West J., O'Hara P.J.;
"Platelet-derived growth factor C (PDGF-C), a novel growth factor that
binds to PDGF alpha receptor.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cecum, Cerebellum, and Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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).
[6]
FUNCTION, SUBUNIT, AND DEVELOPMENTAL STAGE.
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).
[7]
FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
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).
[8]
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).
[9]
TISSUE SPECIFICITY.
PubMed=11744381; DOI=10.1016/S0925-4773(01)00560-3;
Aase K., Abramsson A., Karlsson L., Betsholtz C., Eriksson U.;
"Expression analysis of PDGF-C in adult and developing mouse
tissues.";
Mech. Dev. 110:187-191(2002).
[10]
FUNCTION.
PubMed=12875986; DOI=10.1016/S0002-9440(10)63694-2;
Ponten A., Li X., Thoren P., Aase K., Sjoblom T., Ostman A.,
Eriksson U.;
"Transgenic overexpression of platelet-derived growth factor-C in the
mouse heart induces cardiac fibrosis, hypertrophy, and dilated
cardiomyopathy.";
Am. J. Pathol. 163:673-682(2003).
[11]
FUNCTION, AND INDUCTION BY BLEOMYCIN.
PubMed=12972405; DOI=10.1152/ajplung.00083.2003;
Zhuo Y., Zhang J., Laboy M., Lasky J.A.;
"Modulation of PDGF-C and PDGF-D expression during bleomycin-induced
lung fibrosis.";
Am. J. Physiol. 286:L182-L188(2004).
[12]
DEVELOPMENTAL STAGE.
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).
[13]
REVIEW.
PubMed=15207812; DOI=10.1016/j.cytogfr.2004.03.003;
Tallquist M., Kazlauskas A.;
"PDGF signaling in cells and mice.";
Cytokine Growth Factor Rev. 15:205-213(2004).
[14]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND ACTIVATION BY
PROTEOLYTIC CLEAVAGE.
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).
[15]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15361870; DOI=10.1038/ng1415;
Ding H., Wu X., Bostrom H., Kim I., Wong N., Tsoi B., O'Rourke M.,
Koh G.Y., Soriano P., Betsholtz C., Hart T.C., Marazita M.L.,
Field L.L., Tam P.P., Nagy A.;
"A specific requirement for PDGF-C in palate formation and PDGFR-alpha
signaling.";
Nat. Genet. 36:1111-1116(2004).
[16]
FUNCTION, INDUCTION BY COXSACKIEVIRUS B3 INFECTION, AND DISEASE.
PubMed=15757957; DOI=10.1093/eurheartj/ehi201;
Yang D., Qiu D.;
"Linkage between elevated PDGF-C expression and myocardial
fibrogenesis in coxsackievirus B3-induced chronic myocarditis.";
Eur. Heart J. 26:642-643(2005).
[17]
INDUCTION.
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).
[18]
INDUCTION BY RETINOIC ACID.
PubMed=17066417; DOI=10.1002/bdrb.20094;
Han J., Xiao Y., Lin J., Li Y.;
"PDGF-C controls proliferation and is down-regulated by retinoic acid
in mouse embryonic palatal mesenchymal cells.";
Birth Defects Res. B Dev. Reprod. Toxicol. 77:438-444(2006).
[19]
TISSUE SPECIFICITY, AND INDUCTION BY GONADOTROPIN.
PubMed=16344272; DOI=10.1093/carcin/bgi305;
Chen X., Aravindakshan J., Yang Y., Tiwari-Pandey R., Sairam M.R.;
"Aberrant expression of PDGF ligands and receptors in the tumor prone
ovary of follitropin receptor knockout (FORKO) mouse.";
Carcinogenesis 27:903-915(2006).
[20]
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).
[21]
TISSUE SPECIFICITY, AND INDUCTION BY IL13.
PubMed=16951379; DOI=10.4049/jimmunol.177.6.4141;
Ingram J.L., Antao-Menezes A., Mangum J.B., Lyght O., Lee P.J.,
Elias J.A., Bonner J.C.;
"Opposing actions of Stat1 and Stat6 on IL-13-induced up-regulation of
early growth response-1 and platelet-derived growth factor ligands in
pulmonary fibroblasts.";
J. Immunol. 177:4141-4148(2006).
[22]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=18184860; DOI=10.1681/ASN.2007030290;
Eitner F., Bucher E., van Roeyen C., Kunter U., Rong S., Seikrit C.,
Villa L., Boor P., Fredriksson L., Backstrom G., Eriksson U.,
Ostman A., Floege J., Ostendorf T.;
"PDGF-C is a proinflammatory cytokine that mediates renal interstitial
fibrosis.";
J. Am. Soc. Nephrol. 19:281-289(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:11297552, ECO:0000269|PubMed:12875986,
ECO:0000269|PubMed:12972405, ECO:0000269|PubMed:15361870,
ECO:0000269|PubMed:15372073, ECO:0000269|PubMed:15757957,
ECO:0000269|PubMed:18184860}.
-!- 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) (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:16443219}. Secreted
{ECO:0000269|PubMed:15372073}. Nucleus
{ECO:0000250|UniProtKB:Q9NRA1}. Cytoplasmic granule
{ECO:0000250|UniProtKB:Q9NRA1}. Cell membrane
{ECO:0000269|PubMed:16443219}. Note=Sumoylated form is predominant
in the nucleus (PubMed:16443219). Stored in alpha granules in
platelets (By similarity). {ECO:0000250|UniProtKB:Q9NRA1,
ECO:0000269|PubMed:16443219}.
-!- TISSUE SPECIFICITY: Mainly expressed in kidney, testis, liver,
heart and brain (at protein level). Highly expressed in airway
epithelium, interstitial cells and alveolar macrophages in the
lung of mice overexpressing IL13. Expressed in the ovaries.
{ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11744381,
ECO:0000269|PubMed:16344272, ECO:0000269|PubMed:16951379,
ECO:0000269|PubMed:18184860}.
-!- DEVELOPMENTAL STAGE: In stage E9.5-E15.5, widely expressed in the
surface ectoderm and later in the germinal layer of the skin, the
olfactory and otic placode and their derivatives and the lining of
the oral cavity. In stages E14.5-17.5 expressed in ducts connected
to epidermis, and in developing epidermal openings. Highly
expressed in the early stages of the developing kidney, in the
metanephric mesenchymal aggregates, prefusion skeletal muscle,
cardiac myoblasts, and in visceral and vascular smooth muscle.
{ECO:0000269|PubMed:10806482, ECO:0000269|PubMed:10960785,
ECO:0000269|PubMed:15061151, ECO:0000269|PubMed:15372073}.
-!- INDUCTION: Expression decreased by hypoxia. Up-regulated by EWS-
FLI1 transcription factor in tumor-derived cells. Up-regulated by
IL13 overexpression in the lung via STAT6 and EGR1. Elevated
expression induced by coxsackievirus B3 infection in
immunodeficient mice. Overexpressed in the renal fibrosis.
Expression in the lung is significantly increased after bleomycin
treatment. Down-regulated by retinoic acid and gonadotropin.
{ECO:0000269|PubMed:11313995, ECO:0000269|PubMed:12972405,
ECO:0000269|PubMed:15757957, ECO:0000269|PubMed:15911618,
ECO:0000269|PubMed:16344272, ECO:0000269|PubMed:16951379,
ECO:0000269|PubMed:17066417}.
-!- 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
(By similarity). {ECO:0000250}.
-!- PTM: Sumoylated by SUMO1. {ECO:0000269|PubMed:16443219}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- DISEASE: Note=Involved in the development of myocarditis and
subsequent fibrosis in the experimental model of coxsackievirus
B3-induced chronic myocarditis. {ECO:0000269|PubMed:15757957}.
-!- DISRUPTION PHENOTYPE: Perinatal lethality. Mice have feeding and
respiratory difficulties due to a complete cleft of the secondary
palate. However, they have reduction of renal fibrogenesis. Mice
lacking both PDGFA and PDGFC develop a cleft face, subepidermal
blistering, deficiency of renal cortex mesenchyme, spina bifida
and skeletal and vascular defects. {ECO:0000269|PubMed:15361870,
ECO:0000269|PubMed:18184860}.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
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EMBL; AF286725; AAF91483.1; -; mRNA.
EMBL; AF117608; AAF22516.1; -; mRNA.
EMBL; AF266467; AAK58566.1; -; mRNA.
EMBL; AK033734; BAC28455.1; -; mRNA.
EMBL; AK042767; BAC31358.1; -; mRNA.
EMBL; AK052947; BAC35216.1; -; mRNA.
EMBL; BC006027; AAH06027.1; -; mRNA.
EMBL; BC037696; AAH37696.1; -; mRNA.
CCDS; CCDS17425.1; -.
RefSeq; NP_064355.1; NM_019971.2.
UniGene; Mm.331089; -.
ProteinModelPortal; Q8CI19; -.
SMR; Q8CI19; -.
ComplexPortal; CPX-2909; Platelet-derived growth factor CC complex.
ComplexPortal; CPX-2912; PDGF receptor alpha - PDGF-CC complex.
ComplexPortal; CPX-2913; PDGF receptor alpha-beta - PDGF-CC complex.
ComplexPortal; CPX-2914; PDGF receptor beta - PDGF-CC complex.
STRING; 10090.ENSMUSP00000029652; -.
PhosphoSitePlus; Q8CI19; -.
PaxDb; Q8CI19; -.
PeptideAtlas; Q8CI19; -.
PRIDE; Q8CI19; -.
Ensembl; ENSMUST00000029652; ENSMUSP00000029652; ENSMUSG00000028019.
GeneID; 54635; -.
KEGG; mmu:54635; -.
UCSC; uc008poi.1; mouse.
CTD; 56034; -.
MGI; MGI:1859631; Pdgfc.
eggNOG; ENOG410IETQ; Eukaryota.
eggNOG; ENOG410XQ91; LUCA.
GeneTree; ENSGT00390000005171; -.
HOGENOM; HOG000261610; -.
HOVERGEN; HBG057324; -.
InParanoid; Q8CI19; -.
KO; K05450; -.
OMA; HTYPRNM; -.
OrthoDB; EOG091G0BFZ; -.
PhylomeDB; Q8CI19; -.
TreeFam; TF332130; -.
Reactome; R-MMU-186797; Signaling by PDGF.
ChiTaRS; Pdgfc; mouse.
PRO; PR:Q8CI19; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000028019; -.
ExpressionAtlas; Q8CI19; baseline and differential.
Genevisible; Q8CI19; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005576; C:extracellular region; IDA:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IDA:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
GO; GO:0060348; P:bone development; IGI:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0048565; P:digestive tract development; IGI:MGI.
GO; GO:0009790; P:embryo development; IEA:InterPro.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:MGI.
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:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
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; IDA:MGI.
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;
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_0000343873.
CHAIN ? 345 Platelet-derived growth factor C,
receptor-binding form.
/FTId=PRO_0000343874.
DOMAIN 46 163 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
SITE 225 226 Cleavage. {ECO:0000250}.
SITE 231 232 Cleavage. {ECO:0000250}.
SITE 234 235 Cleavage. {ECO:0000250}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 104 124 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 250 294 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 274 274 Interchain (with C-286).
{ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 280 335 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 286 286 Interchain (with C-274).
{ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 287 337 {ECO:0000255|PROSITE-ProRule:PRU00059}.
CONFLICT 86 86 I -> T (in Ref. 1; AAF91483).
{ECO:0000305}.
CONFLICT 103 103 I -> L (in Ref. 5; AAH37696).
{ECO:0000305}.
CONFLICT 127 127 G -> E (in Ref. 1; AAF91483).
{ECO:0000305}.
CONFLICT 230 230 G -> V (in Ref. 1; AAF91483).
{ECO:0000305}.
CONFLICT 269 269 I -> R (in Ref. 1; AAF91483).
{ECO:0000305}.
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


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