| IED ID | IndEnz0002014330 |
| Enzyme Type ID | protease014330 |
| Protein Name |
Atrial natriuretic peptide-converting enzyme EC 3.4.21.- Corin Pro-ANP-converting enzyme Cleaved into: Atrial natriuretic peptide-converting enzyme, N-terminal propeptide; Atrial natriuretic peptide-converting enzyme, activated protease fragment; Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment |
| Gene Name | Corin |
| 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 | MGRVSFNVRVSSVRRARCSCPGRCYLSCRVPPTTALHALNGFGRAGVLGETAGGTVGLGPSGTRGFLSGSKFQASGSLKDCFGAPPAPDVLRADSSVGEGCPQKLVTANLLRFLLLVLIPCICALIVLLAILLSFVGTLKKVYFKSNDSEPLVTDGEVRVPGVIHVNRYENTGAPSMPPSQSIPAWTPRAPSLEDQSHGNTSTCVNITHRQCQILPYHSTLAPLLPIVKNMDTEKFLKFFTYLHRLGCYQHILLFGCSLAFPKCIVDGDDRHGLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQFRYHTENNSDASRICFSLQQEHGKQSLCGGGESFLCTSGLCISKKLQCNGYNDCDDWSDEAHCNCSEDLFHCGTGKCLHHSLVCDGYDDCGDLSDEQNCDCNLTKEHRCGDGRCIAAEWVCDGDHDCVDKSDEVNCSCPSQGLVECRSGQCIPSTFQCDGDEDCKDGSDEENCSDRPTPCPGGDRGCLDSSCVESCAGSSLCDSDSSLSNCSHCEPITLELCMNLPYNLTHYPNYLGHRTQKEASISWESALFPALVQTNCYKYLMFFACTILVPKCDVNTGQRVPPCRLLCEHSKERCESVLGIVGLQWPEDTDCSQFPEQSSDNQTCLLPNEDVEECSPSHFKCRSGRCVLGSRRCDGQADCDDDSDEENCGCKERDLWECPLNKQCLKHTLICDGFPDCSDSMDEKNCSFCQDDELECANHECVPRDLWCDGWTDCSDSSDEWGCVTLSKNGNSSSFLTVHRSARDHHVCADGWQETLSQLACRQMGLGEPSVTELVQGQEGQQWLRLHSSWENLNGSTLQELLVHRRSCPSGSEISLLCTKQDCGRRPAARMNKRILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGREDADVWKVVFGINNLDHPSGFMQTRFVKTILLHPRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPREFLEPDTYCYITGWGHMGNKMPFKLQEGEVRIIPLEQCQSYFDMKTITNRMICAGYESGTVDSCMIDSGGPLVCERPGGQWTLFGLTSWGSVCFSKVLGPGVYSNVSYFVDWIERQIYIQTFLQKKSQG |
| Enzyme Length | 1111 |
| Uniprot Accession Number | Q80YN4 |
| Absorption | |
| Active Site | ACT_SITE 908; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 957; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 1050; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine-type endopeptidase involved in atrial natriuretic peptide (NPPA) processing (PubMed:17660514). Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation (By similarity). Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus (By similarity). Also acts as a regulator of sodium reabsorption in kidney (PubMed:20613715). May also process pro-NPPB the B-type natriuretic peptide (By similarity). {ECO:0000250|UniProtKB:Q9Y5Q5, ECO:0000250|UniProtKB:Q9Z319, ECO:0000269|PubMed:17660514, ECO:0000269|PubMed:20613715}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (4); Disulfide bond (35); Domain (11); Glycosylation (5); Motif (1); Mutagenesis (3); Sequence conflict (3); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | INDUCTION: Down-regulated upon experimental heart failure. {ECO:0000269|PubMed:15155264}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Cytoplasmic vesicle.; SUBCELLULAR LOCATION: [Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment]: Secreted {ECO:0000250}. Note=Soluble form produced following cleavage by ADAM10. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated; required for processing and activation. {ECO:0000269|PubMed:17660514}.; PTM: Activated through proteolytic processing by a trypsin-like protease; cleaved into a N-terminal propeptide and an activated corin protease fragment. Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment is produced by cleavage by ADAM10. Cleavage by ADAM10 to produce soluble 180 kDa soluble fragment takes place after the transmembrane region and before FZ 1 (Probable). {ECO:0000305|PubMed:17660514}.; PTM: A disulfide bond links the activated corin protease fragment and the N-terminal propeptide. The disulfide bond also links the activated corin protease fragment with Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment (Probable). {ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15191894; |
| Motif | MOTIF 93..96; /note=DDNN motif |
| Gene Encoded By | |
| Mass | 122,757 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |