| IED ID | IndEnz0002019055 |
| Enzyme Type ID | protease019055 |
| Protein Name |
Carboxypeptidase A2 EC 3.4.17.15 |
| Gene Name | CPA2 |
| 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 | MAMRLILFFGALFGHIYCLETFVGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSPTTPGETAHVRVPFVNVQAVKVFLESQGIAYSIMIEDVQVLLDKENEEMLFNRRRERSGNFNFGAYHTLEEISQEMDNLVAEHPGLVSKVNIGSSFENRPMNVLKFSTGGDKPAIWLDAGIHAREWVTQATALWTANKIVSDYGKDPSITSILDALDIFLLPVTNPDGYVFSQTKNRMWRKTRSKVSGSLCVGVDPNRNWDAGFGGPGASSNPCSDSYHGPSANSEVEVKSIVDFIKSHGKVKAFITLHSYSQLLMFPYGYKCTKLDDFDELSEVAQKAAQSLRSLHGTKYKVGPICSVIYQASGGSIDWSYDYGIKYSFAFELRDTGRYGFLLPARQILPTAEETWLGLKAIMEHVRDHPY |
| Enzyme Length | 419 |
| Uniprot Accession Number | P48052 |
| 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=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); Beta strand (18); Binding site (2); Chain (1); Disulfide bond (2); Erroneous gene model prediction (1); Erroneous initiation (4); Helix (16); Metal binding (3); Natural variant (1); Propeptide (1); Region (3); Sequence conflict (3); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Carboxypeptidase;Direct protein sequencing;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..18; /evidence=ECO:0000255 |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (2) |
| Cross Reference PDB | 1AYE; 1DTD; 1O6X; |
| Mapped Pubmed ID | 11743734; 17196978; 19401682; 19817500; 20379614; 21098023; 26115097; 26316592; 27358403; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,030 |
| Kinetics | |
| Metal Binding | METAL 179; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570"; METAL 182; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570"; METAL 306; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.15; |