| IED ID | IndEnz0002018849 |
| Enzyme Type ID | protease018849 |
| Protein Name |
Calcium-dependent serine proteinase CASP EC 3.4.21.- Cleaved into: Calcium-dependent serine proteinase heavy chain; Calcium-dependent serine proteinase light chain |
| Gene Name | |
| Organism | Mesocricetus auratus (Golden hamster) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Cricetidae Cricetinae (hamsters) Mesocricetus Mesocricetus auratus (Golden hamster) |
| Enzyme Sequence | MGKSSEAWCIVLFSVFASFSAEPTMHGEILSPNYPQAYPNEMEKTWDIEVPEGFGVRLYFTHLDMELSENCEYDSVQIISGGVEEGRLCGQRTSKNANSPIVEEFQIPYNKLQVIFRSDFSNEERFTGFAAYYAAIDVNECTDFTDVPCSHFCNNFIGGYFCSCPPEYFLHDDMRNCGVNCSGNVFTALIGEISSPNYPNPYPENSRCEYQILLEEGFQVVVTIQREDFDVEPADSQGNCQDSLLFAAKNRQFGPFCGNGFPGPLTIETHSNTLDIVFQTDLTEQKKGWKLRYHGDPIPCPKEITANSVWAPEKAKYVFKDVVKISCVDGFEAVEGNVGSTFFYSTCQSNGQWSNSRLRCQPVDCGIPEPIQNGKVDDPENTLFGSVIHYSCEEPYYYMEHAEHGGEYRCAANGSWVNDELGIELPKCVPVCGVPTEPFRIQQRIFGGFPAKIQSFPWQVFFEFPRAGGALIGEHWVLTAAHVVEGNSDPSMYVGSTSVRMENLANVQKLTTDRVIIHPGWKPGDDLSTRTNFDNDIALVRLKDPVKMGPTVSPICLPGTSSEYEPSEGDLGLISGWGRTERRNIVIQLRGAKLPVTSLEKCRQVKEENPKARADDYVFTSNMICAGEKGVDSCQGDSGGAFALPVPNVRDPKFYVAGLVSWGKKCGTYGIYTKVKNYKDWILQTMQENSVPSQD |
| Enzyme Length | 695 |
| Uniprot Accession Number | P15156 |
| Absorption | |
| Active Site | ACT_SITE 482; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 536; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 638; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Capable of degrading extracellular matrix proteins. CASP degrades type I and IV collagen and fibronectin in the presence of calcium. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Disulfide bond (12); Domain (6); Glycosylation (2); Modified residue (1); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;EGF-like domain;Extracellular matrix;Glycoprotein;Hydrolase;Hydroxylation;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Sushi |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. |
| Modified Residue | MOD_RES 155; /note=(3R)-3-hydroxyasparagine; /evidence=ECO:0000255 |
| Post Translational Modification | PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000269|PubMed:2753140 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 77,493 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |