Detail Information for IndEnz0002019055
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;