| IED ID | IndEnz0002018211 |
| Enzyme Type ID | protease018211 |
| Protein Name |
Cartilage intermediate layer protein 1 CILP-1 Cleaved into: Cartilage intermediate layer protein 1 C2 Fragment |
| Gene Name | CILP NTPPH |
| Organism | Sus scrofa (Pig) |
| 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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | QHYPLGDMDGEDPMGELEIPSKSFYRQNGEPYTGKVKASVTFLDPRNISTATAAQSDLNFINDEGDTFPLRTYGMFSVDFTDEAASESLNVGKVKVHLDSTQVKMPEHVPMMKLWSLNPDTGLWEEEGDFRFESQRRKRREDRTFLVGNMEIRERRLFNLDVPESRRCFIKVRAYRSERFLPSEQIQGVVVSVINLEPRAGFSSNPRAWGRFDSVLTGPNGACLPAFCDDQSPDAYSAYVLASLAGEELEAVESSPKFNPNAIGVPQPYLNKLKYRRTDHEDPRVKKTAFQISMAKPRPNSAEESNGPIYAFENLQACEEAPPSAAHFRFYQIEGDRYDYNTVPFNEDDPMSWTEDYLAWWPKPMEFRACYIKVKIVGPLEVNVRSRNMGGTHRQTVGKLYGIRDVKSTRDRDQPNVSSACLEFKCSGMLYDQDRVDRTLVKVIPQGSCHRASVNSMLHEYLVNHLPLAVNNDTSEYTMLAPLDPLGHNYGIYTVTDQDPRTAKEIALGRCFDGSSDGSSRVMKSNVGVALTFNCVERQVGRQSAFQYLQSTSARPSPASTVRGRAPSRRQRASSGSQRQPRGVASLRFPGVAQQPLSN |
| Enzyme Length | 599 |
| Uniprot Accession Number | O19112 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Glycosylation (3); Non-terminal residue (1); Region (1); Sequence conflict (2) |
| Keywords | Direct protein sequencing;Extracellular matrix;Glycoprotein;Reference proteome;Secreted |
| Interact With | |
| Induction | INDUCTION: Up-regulated upon TGFB1 treatment, and down-regulated by IGF1. {ECO:0000269|PubMed:11145028}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved into 2 chains possibly by a furin-like protease upon or preceding secretion. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 67,433 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |