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 |