Detail Information for IndEnz0002018849
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