IED ID | IndEnz0002004734 |
Enzyme Type ID | protease004734 |
Protein Name |
Carboxypeptidase A2 EC 3.4.17.15 |
Gene Name | Cpa2 |
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 | MRLTLLLAALLGYIYCQETFVGDQVLEIIPSHEEQIRTLLQLEAEEHLELDFWKSPTIPGETVHVRVPFASIQAVKVFLESQGIDYSIMIEDVQVLLDQEREEMLFNQQRERGGNFNFEAYHTLEEIYQEMDNLVAENPGLVSKVNLGSSFENRPMNVLKFSTGGDKPAIWLDAGIHAREWVTQATALWTANKIASDYGTDPAITSLLNTLDIFLLPVTNPDGYVFSQTTNRMWRKTRSKRSGSGCVGVDPNRNWDANFGGPGASSSPCSDSYHGPKPNSEVEVKSIVDFIKSHGKVKAFITLHSYSQLLMFPYGYKCTKPDDFNELDEVAQKAAQALKRLHGTSYKVGPICSVIYQASGGSIDWAYDLGIKYSFAFELRDTAFYGFLLPAKQILPTAEETWLGLKTIMEHVRDHPY |
Enzyme Length | 417 |
Uniprot Accession Number | P19222 |
Absorption | |
Active Site | ACT_SITE 378; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:1761558 |
Activity Regulation | |
Binding Site | BINDING 235; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730; BINDING 356; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues.; EC=3.4.17.15; |
DNA Binding | |
EC Number | 3.4.17.15 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (2); Chain (1); Disulfide bond (2); Metal binding (3); Propeptide (1); Region (3); 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. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 22178042; 8200353; |
Motif | |
Gene Encoded By | |
Mass | 46,912 |
Kinetics | |
Metal Binding | METAL 177; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:1761558; METAL 180; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:1761558; METAL 304; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:1761558 |
Rhea ID | |
Cross Reference Brenda |