| IED ID | IndEnz0002000827 |
| Enzyme Type ID | protease000827 |
| Protein Name |
Platelet-derived growth factor D PDGF-D Iris-expressed growth factor Spinal cord-derived growth factor B SCDGF-B Cleaved into: Platelet-derived growth factor D, latent form PDGFD latent form ; Platelet-derived growth factor D, receptor-binding form PDGFD receptor-binding form |
| Gene Name | PDGFD IEGF SCDGFB MSTP036 UNQ1899/PRO4345 |
| 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 | MHRLIFVYTLICANFCSCRDTSATPQSASIKALRNANLRRDESNHLTDLYRRDETIQVKGNGYVQSPRFPNSYPRNLLLTWRLHSQENTRIQLVFDNQFGLEEAENDICRYDFVEVEDISETSTIIRGRWCGHKEVPPRIKSRTNQIKITFKSDDYFVAKPGFKIYYSLLEDFQPAAASETNWESVTSSISGVSYNSPSVTDPTLIADALDKKIAEFDTVEDLLKYFNPESWQEDLENMYLDTPRYRGRSYHDRKSKVDLDRLNDDAKRYSCTPRNYSVNIREELKLANVVFFPRCLLVQRCGGNCGCGTVNWRSCTCNSGKTVKKYHEVLQFEPGHIKRRGRAKTMALVDIQLDHHERCDCICSSRPPR |
| Enzyme Length | 370 |
| Uniprot Accession Number | Q9GZP0 |
| 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 for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix (By similarity). {ECO:0000250, ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:15271796}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (2); Disulfide bond (4); Domain (1); Glycosylation (1); Mutagenesis (2); Natural variant (2); Signal peptide (1); Site (2) |
| Keywords | Alternative splicing;Cleavage on pair of basic residues;Developmental protein;Disulfide bond;Glycoprotein;Growth factor;Mitogen;Proto-oncogene;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11331882}. Note=Released by platelets upon wounding. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by proteolytic cleavage. 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 Arg-247 or Arg-249 by urokinase plasminogen activator gives rise to the active form. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15207811; 16189269; 1639841; 18187181; 18258854; 18403754; 18471357; 18573494; 18600092; 18997817; 19028801; 19357108; 19544444; 19733850; 19913121; 20379614; 20406896; 20628086; 21098708; 22289441; 22415093; 22689130; 22704460; 23187740; 23505219; 24158561; 24646915; 24870786; 24938433; 25332166; 25333347; 25391964; 25760076; 26157007; 26362023; 26924050; 27507215; 27585990; 28035069; 28267575; 28346846; 28965749; 29079201; 29240605; 29955147; 30836770; 32186759; 32452055; 33640869; 34539622; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,848 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |