| IED ID | IndEnz0002000824 |
| Enzyme Type ID | protease000824 |
| Protein Name |
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 |
| Gene Name | PDGFC SCDGF UNQ174/PRO200 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSLFGLLLLTSALAGQRQGTQAESNLSSKFQFSSNKEQNGVQDPQHERIITVSTNGSIHSPRFPHTYPRNTVLVWRLVAVEENVWIQLTFDERFGLEDPEDDICKYDFVEVEEPSDGTILGRWCGSGTVPGKQISKGNQIRIRFVSDEYFPSEPGFCIHYNIVMPQFTEAVSPSVLPPSALPLDLLNNAITAFSTLEDLIRYLEPERWQLDLEDLYRPTWQLLGKAFVFGRKSRVVDLNLLTEEVRLYSCTPRNFSVSIREELKRTDTIFWPGCLLVKRCGGNCACCLHNCNECQCVPSKVTKKYHEVLQLRPKTGVRGLHKSLTDVALEHHEECDCVCRGSTGG |
| Enzyme Length | 345 |
| Uniprot Accession Number | Q9NRA1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | 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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (4); Chain (2); Disulfide bond (6); Domain (1); Glycosylation (2); Mutagenesis (4); Sequence conflict (2); Signal peptide (1); Site (3) |
| Keywords | Alternative splicing;Cell membrane;Cleavage on pair of basic residues;Cytoplasm;Developmental protein;Disulfide bond;Glycoprotein;Growth factor;Membrane;Mitogen;Nucleus;Reference proteome;Secreted;Signal;Ubl conjugation |
| Interact With | P16234; P16234-1 |
| Induction | 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}. |
| Subcellular Location | 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}. |
| Modified Residue | |
| Post Translational Modification | 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}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15207811; 1639841; 18573494; 18588873; 19092777; 19111878; 19553600; 19569180; 19786962; 19913121; 19968886; 20452482; 20485444; 20628086; 20634891; 20673868; 20819778; 21118967; 21993555; 22035541; 23029525; 23714575; 23929039; 24126726; 24269585; 24421315; 24612214; 25383675; 26687981; 27033449; 28267575; 28965749; 29079201; 29380207; 29529015; 31482267; 31542979; 31897468; 33603171; |
| Motif | |
| Gene Encoded By | |
| Mass | 39,029 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |