Detail Information for IndEnz0002017130
IED ID IndEnz0002017130
Enzyme Type ID protease017130
Protein Name Chymase
EC 3.4.21.39
Alpha-chymase
Mast cell protease I
Gene Name CMA1 CYH CYM
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 MLLLPLPLLLFLLCSRAEAGEIIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
Enzyme Length 247
Uniprot Accession Number P23946
Absorption
Active Site ACT_SITE 66; /note=Charge relay system; ACT_SITE 110; /note=Charge relay system; ACT_SITE 203; /note=Charge relay system
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa.; EC=3.4.21.39;
DNA Binding
EC Number 3.4.21.39
Enzyme Function FUNCTION: Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Beta strand (15); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (2); Helix (3); Natural variant (3); Propeptide (1); Sequence conflict (2); Signal peptide (1); Turn (3)
Keywords 3D-structure;Alternative splicing;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Mast cell granules.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19
Structure 3D X-ray crystallography (20)
Cross Reference PDB 1KLT; 1NN6; 1PJP; 1T31; 2HVX; 3N7O; 3S0N; 4AFQ; 4AFS; 4AFU; 4AFZ; 4AG1; 4AG2; 4K2Y; 4K5Z; 4K60; 4K69; 4KP0; 5YJM; 5YJP;
Mapped Pubmed ID 10550754; 10830912; 10899625; 10917873; 11096141; 11173969; 11208365; 11303326; 11502696; 11696688; 11852067; 11893690; 12047032; 12062105; 12097409; 12165749; 12359984; 12446192; 12484503; 12531890; 12614156; 12815038; 14592513; 14701812; 14757520; 15106801; 15227657; 15248847; 15449728; 15526160; 15555355; 15638376; 15741158; 15788353; 15914614; 15919053; 15924217; 16020275; 16134991; 16317101; 16446531; 16520412; 16786130; 16962475; 17035401; 17199219; 17334631; 17344430; 17361995; 17460374; 17851694; 18079408; 18641516; 18845543; 18856058; 18958543; 18973102; 19126871; 19332265; 19380825; 19494363; 19520069; 19697770; 19853701; 19899640; 20423454; 20424473; 20599788; 20628086; 20659024; 20670150; 20736038; 20800603; 21150220; 21274549; 21733690; 2176865; 21786536; 21796807; 22102069; 22180785; 22194960; 22363824; 22653218; 2266130; 22679278; 23659209; 24121339; 24257755; 24344642; 24507159; 24516344; 24560885; 24823657; 24874976; 25102745; 25120737; 25797204; 28053237; 28205588; 28878298; 29191554; 29973268; 31466718; 31888494; 32129682; 32361612; 32678248; 33309638; 34884420; 6807977; 9256427; 9257865; 9748697; 9794357;
Motif
Gene Encoded By
Mass 27,325
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.39;