| IED ID | IndEnz0002013937 |
| Enzyme Type ID | protease013937 |
| Protein Name |
Renin EC 3.4.23.15 Angiotensinogenase |
| Gene Name | Ren1 Ren |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MGGRRMPLWALLLLWTSCSFSLPTDTASFGRILLKKMPSVREILEERGVDMTRISAEWGEFIKKSSFTNVTSPVVLTNYLDTQYYGEIGIGTPSQTFKVIFDTGSANLWVPSTKCGPLYTACEIHNLYDSSESSSYMENGTEFTIHYGSGKVKGFLSQDVVTVGGIIVTQTFGEVTELPLIPFMLAKFDGVLGMGFPAQAVDGVIPVFDHILSQRVLKEEVFSVYYSRESHLLGGEVVLGGSDPQHYQGNFHYVSISKAGSWQITMKGVSVGPATLLCEEGCMAVVDTGTSYISGPTSSLQLIMQALGVKEKRANNYVVNCSQVPTLPDISFYLGGRTYTLSNMDYVQKNPFRNDDLCILALQGLDIPPPTGPVWVLGATFIRKFYTEFDRHNNRIGFALAR |
| Enzyme Length | 402 |
| Uniprot Accession Number | P08424 |
| Absorption | |
| Active Site | ACT_SITE 102; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 287; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | ACTIVITY REGULATION: Interaction with ATP6AP2 results in a 5-fold increased efficiency in angiotensinogen processing. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.; EC=3.4.23.15; |
| DNA Binding | |
| EC Number | 3.4.23.15 |
| Enzyme Function | FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (24); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (3); Helix (12); Propeptide (1); Sequence conflict (3); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Aspartyl protease;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Membrane {ECO:0000250}. Note=Associated to membranes via binding to ATP6AP2. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000305 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5MLG; |
| Mapped Pubmed ID | 11247783; 12242043; 1278112; 15489960; 16467505; 16512638; 21321306; 21963836; 22266601; 22342485; 22609375; 22796710; 23817491; 24709336; 25841323; 7042704; 7060565; 8446257; 8567976; 9671794; 9933256; |
| Motif | |
| Gene Encoded By | |
| Mass | 44,276 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |