Detail Information for IndEnz0002009584
IED ID IndEnz0002009584
Enzyme Type ID protease009584
Protein Name Trypsin-2
EC 3.4.21.4
Anionic trypsinogen
Serine protease 2
Trypsin II
Gene Name PRSS2 TRY2 TRYP2
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 MNLLLILTFVAAAVAAPFDDDDKIVGGYICEENSVPYQVSLNSGYHFCGGSLISEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPKYNSRTLDNDILLIKLSSPAVINSRVSAISLPTAPPAAGTESLISGWGNTLSSGADYPDELQCLDAPVLSQAECEASYPGKITNNMFCVGFLEGGKDSCQGDSGGPVVSNGELQGIVSWGYGCAQKNRPGVYTKVYNYVDWIKDTIAANS
Enzyme Length 247
Uniprot Accession Number P07478
Absorption
Active Site ACT_SITE 63; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 107; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 200; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
DNA Binding
EC Number 3.4.21.4
Enzyme Function FUNCTION: In the ileum, may be involved in defensin processing, including DEFA5. {ECO:0000269|PubMed:12021776}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (4); Domain (1); Metal binding (4); Modified residue (1); Natural variant (2); Propeptide (1); Signal peptide (1); Site (1)
Keywords Calcium;Digestion;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Sulfation;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space.
Modified Residue MOD_RES 154; /note="Sulfotyrosine"; /evidence="ECO:0000305|PubMed:17087724, ECO:0000305|PubMed:25010489"
Post Translational Modification PTM: Sulfated on tyrosine. {ECO:0000269|PubMed:17087724}.; PTM: Sulfation at Tyr-154 increases selectivity towards basic versus apolar residues at the P2' position of inhibitors that bind in a substrate-like fashion. Although the increase in selectivity is relatively small, it may facilitate digestion of a broader range of dietary proteins. {ECO:0000269|PubMed:25010489}.
Signal Peptide SIGNAL 1..15; /evidence=ECO:0000269|PubMed:2598466
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12709065; 12949286; 14695529; 15257288; 15651064; 15776435; 16699518; 17640760; 18062964; 18063422; 18362849; 18428024; 18461367; 19052022; 19077465; 19095652; 19096130; 19254208; 19690177; 19752771; 2005102; 20304780; 20428826; 20484960; 20517765; 20625975; 2176865; 21792081; 21946810; 22481290; 22909050; 23143602; 23882137; 25253127; 2557753; 25916077; 26110235; 27846138; 3038863; 33202925; 33515547; 34794144; 4216367; 6263256; 6270089; 7890717; 8576151; 8692836; 9261109;
Motif
Gene Encoded By
Mass 26,488
Kinetics
Metal Binding METAL 75; /note=Calcium; /evidence=ECO:0000250; METAL 77; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 80; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 85; /note=Calcium; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda