Detail Information for IndEnz0002001782
IED ID IndEnz0002001782
Enzyme Type ID protease001782
Protein Name Trypsin-3
EC 3.4.21.4
Brain trypsinogen
Mesotrypsin
Mesotrypsinogen
Serine protease 3
Serine protease 4
Trypsin III
Trypsin IV
Gene Name PRSS3 PRSS4 TRY3 TRY4
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 MCGPDDRCPARWPGPGRAVKCGKGLAAARPGRVERGGAQRGGAGLELHPLLGGRTWRAARDADGCEALGTVAVPFDDDDKIVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAHCYKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKYNRDTLDNDIMLIKLSSPAVINARVSTISLPTTPPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSMFCVGFLEGGKDSCQRDSGGPVVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS
Enzyme Length 304
Uniprot Accession Number P35030
Absorption
Active Site ACT_SITE 120; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000305|PubMed:27810896"; ACT_SITE 164; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000305|PubMed:27810896"; ACT_SITE 257; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000305|PubMed:27810896"
Activity Regulation ACTIVITY REGULATION: Not inhibited by Kunitz-type trypsin inhibitors. {ECO:0000269|PubMed:18077447, ECO:0000269|PubMed:9099703}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; Evidence={ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:14507909, ECO:0000269|PubMed:18077447, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0000269|PubMed:6698368, ECO:0000269|PubMed:9099703};
DNA Binding
EC Number 3.4.21.4
Enzyme Function FUNCTION: Digestive protease that cleaves proteins preferentially after an Arg residue and has proteolytic activity toward Kunitz-type trypsin inhibitors. {ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:14507909, ECO:0000269|PubMed:18077447, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0000269|PubMed:9099703}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:6698368};
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (4); Beta strand (17); Chain (1); Disulfide bond (5); Domain (1); Helix (4); Metal binding (5); Modified residue (1); Mutagenesis (1); Natural variant (4); Propeptide (1); Sequence conflict (3); Signal peptide (1); Site (1); Turn (3)
Keywords 3D-structure;Alternative splicing;Calcium;Digestion;Disulfide bond;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Sulfation;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6698368}.
Modified Residue MOD_RES 211; /note=Sulfotyrosine; /evidence=ECO:0000250
Post Translational Modification
Signal Peptide SIGNAL 1..?; /evidence=ECO:0000255
Structure 3D X-ray crystallography (14)
Cross Reference PDB 1H4W; 2R9P; 3L33; 3L3T; 3P92; 3P95; 4DG4; 4U30; 4U32; 5C67; 5JBT; 5TP0; 6BX8; 6GFI;
Mapped Pubmed ID 15174051; 15299926; 15572765; 15855826; 15987713; 16013053; 16412431; 16492676; 16759229; 17406981; 17623652; 18094465; 18363639; 18665091; 19095652; 19249338; 19254208; 19920152; 20035377; 20057044; 20124702; 20484962; 20711500; 20861008; 20947888; 21806544; 22042864; 22547309; 22610453; 22900303; 23650620; 24146905; 24189400; 24872419; 25609649; 26175157; 26318044; 26957636; 28423522; 28463992; 28844099; 29629340; 30258049; 30700553; 30755669; 30908656; 31810373; 31911942; 32014997; 33515547;
Motif
Gene Encoded By
Mass 32,529
Kinetics
Metal Binding METAL 132; /note="Calcium"; /evidence="ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0"; METAL 134; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0"; METAL 137; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0"; METAL 139; /note="Calcium"; /evidence="ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT"; METAL 142; /note="Calcium"; /evidence="ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0"
Rhea ID
Cross Reference Brenda