| IED ID | IndEnz0002009579 |
| Enzyme Type ID | protease009579 |
| Protein Name |
Serine protease 1 EC 3.4.21.4 Anionic trypsin I Anionic trypsin-I Beta-trypsin Cationic trypsinogen Pretrypsinogen I Trypsin I Trypsin-1 Cleaved into: Alpha-trypsin chain 1; Alpha-trypsin chain 2 |
| Gene Name | PRSS1 TRP1 TRY1 TRYP1 |
| 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 | MNPLLILTFVAAALAAPFDDDDKIVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS |
| Enzyme Length | 247 |
| Uniprot Accession Number | P07477 |
| Absorption | |
| Active Site | ACT_SITE 63; /note=Charge relay system; ACT_SITE 107; /note=Charge relay system; ACT_SITE 200; /note=Charge relay system |
| 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: Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates. {ECO:0000269|PubMed:7945238}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (15); Chain (3); Disulfide bond (5); Domain (1); Helix (4); Metal binding (4); Modified residue (1); Mutagenesis (1); Natural variant (13); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Calcium;Digestion;Direct protein sequencing;Disease variant;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: Occurs in a single-chain form and a two-chain form, produced by proteolytic cleavage after Arg-122.; 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, ECO:0000269|PubMed:7945238" |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 1FXY; 1TRN; 2RA3; 4WWY; 4WXV; |
| Mapped Pubmed ID | 10835640; 11549837; 11702203; 11708864; 11719509; 11932257; 11938439; 12120220; 12120234; 12360463; 12529713; 12765848; 12792776; 12939655; 1370825; 1390635; 14526128; 15017610; 15082592; 15174051; 15329520; 15651064; 15678497; 15725718; 15749231; 15786540; 16327984; 16534247; 16685108; 16954950; 17003641; 17069643; 17474147; 17480209; 17489851; 17613931; 17641559; 17981921; 18063422; 18076731; 18077447; 18184119; 18272034; 18428024; 18461367; 18511571; 18522894; 18580441; 18702646; 18755888; 18852684; 18946221; 18953248; 18986377; 19096130; 19156129; 19433603; 19454815; 19550412; 19593166; 19654461; 19657220; 19690177; 19801634; 19951905; 20001681; 20198321; 20452997; 20484960; 20502448; 20676769; 20950468; 21415673; 21499207; 2159879; 2176865; 21792085; 21922221; 21952138; 22088471; 22109105; 22427236; 22539344; 22547309; 22699143; 22722260; 22900303; 23143602; 23430245; 23474566; 23601753; 23745029; 23745036; 23751316; 23801884; 23864476; 23882137; 23951356; 24134754; 24236450; 24366813; 24403079; 24413785; 24513262; 24525505; 24722290; 24777884; 24909264; 25003218; 25253127; 25383785; 2546891; 25546417; 2557753; 25609649; 25835118; 25981744; 26110235; 26175157; 26376395; 26546433; 26658045; 26692446; 26822915; 27129265; 27409067; 27432637; 27578509; 27714503; 27846138; 28502372; 28861620; 28913878; 29476405; 29479871; 29641165; 29870887; 3058116; 31221819; 31300697; 31521106; 31550238; 31593019; 31911942; 32221727; 32530995; 33202925; 33515547; 33867821; 4216367; 6263256; 7826345; 8663255; 9261109; 9707558; |
| Motif | |
| Gene Encoded By | |
| Mass | 26,558 |
| Kinetics | |
| Metal Binding | METAL 75; /note=Calcium; METAL 77; /note=Calcium; via carbonyl oxygen; METAL 80; /note=Calcium; via carbonyl oxygen; METAL 85; /note=Calcium |
| Rhea ID | |
| Cross Reference Brenda |