| IED ID | IndEnz0002014512 |
| Enzyme Type ID | protease014512 |
| Protein Name |
Carboxypeptidase A1 EC 3.4.17.1 |
| Gene Name | Cpa1 Cpa |
| 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 | MKRLLILSLLLEAVCGNENFVGHQVLRISAADEAQVQKVKELEDLEHLQLDFWRDAARAGIPIDVRVPFPSIQSVKAFLEYHGISYEIMIEDVQLLLDEEKQQMSAFQARALSTDSFNYATYHTLDEIYEFMDLLVAEHPQLVSKIQIGNTFEGRPIHVLKFSTGGTNRPAIWIDTGIHSREWVTQASGVWFAKKITKDYGQDPTFTAVLDNMDIFLEIVTNPDGFAYTHKTNRMWRKTRSHTQGSLCVGVDPNRNWDAGFGMAGASSNPCSETYRGKFPNSEVEVKSIVDFVTSHGNIKAFISIHSYSQLLLYPYGYTSEPAPDQAELDQLAKSAVTALTSLHGTKFKYGSIIDTIYQASGSTIDWTYSQGIKYSFTFELRDTGLRGFLLPASQIIPTAEETWLALLTIMDHTVKHPY |
| Enzyme Length | 419 |
| Uniprot Accession Number | P00731 |
| Absorption | |
| Active Site | ACT_SITE 380; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
| Activity Regulation | |
| Binding Site | BINDING 237; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730; BINDING 358; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1; Evidence={ECO:0000250|UniProtKB:P15085}; CATALYTIC ACTIVITY: Reaction=H2O + leukotriene C4 = glycine + leukotriene F4; Xref=Rhea:RHEA:50740, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:57973, ChEBI:CHEBI:133618; Evidence={ECO:0000250|UniProtKB:P00730};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50741; Evidence={ECO:0000250|UniProtKB:P00730}; |
| DNA Binding | |
| EC Number | 3.4.17.1 |
| Enzyme Function | FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (By similarity). Catalyzes the conversion of leukotriene C4 to leukotriene F4 via the hydrolysis of an amide bond (By similarity). {ECO:0000250|UniProtKB:P00730, ECO:0000250|UniProtKB:P15085}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (1); Disulfide bond (1); Metal binding (3); Propeptide (1); Region (3); Sequence conflict (6); Signal peptide (1) |
| Keywords | Carboxypeptidase;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15085}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15865404; 21572518; 22178042; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,197 |
| Kinetics | |
| Metal Binding | METAL 179; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 182; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 306; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | RHEA:50740; RHEA:50741 |
| Cross Reference Brenda | 3.4.17.1; |