| IED ID | IndEnz0002014014 |
| Enzyme Type ID | protease014014 |
| Protein Name |
Carboxypeptidase A6 EC 3.4.17.- |
| Gene Name | CPA6 CPAH |
| 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 | MKCLGKRRGQAAAFLPLCWLFLKILQPGHSHLYNNRYAGDKVIRFIPKTEEEAYALKKISYQLKVDLWQPSSISYVSEGTVTDVHIPQNGSRALLAFLQEANIQYKVLIEDLQKTLEKGSSLHTQRNRRSLSGYNYEVYHSLEEIQNWMHHLNKTHSGLIHMFSIGRSYEGRSLFILKLGRRSRLKRAVWIDCGIHAREWIGPAFCQWFVKEALLTYKSDPAMRKMLNHLYFYIMPVFNVDGYHFSWTNDRFWRKTRSRNSRFRCRGVDANRNWKVKWCDEGASMHPCDDTYCGPFPESEPEVKAVANFLRKHRKHIRAYLSFHAYAQMLLYPYSYKYATIPNFRCVESAAYKAVNALQSVYGVRYRYGPASTTLYVSSGSSMDWAYKNGIPYAFAFELRDTGYFGFLLPEMLIKPTCTETMLAVKNITMHLLKKCP |
| Enzyme Length | 437 |
| Uniprot Accession Number | Q8N4T0 |
| Absorption | |
| Active Site | ACT_SITE 398; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
| Activity Regulation | |
| Binding Site | BINDING 254; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730; BINDING 376; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II (PubMed:18178555). Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine (PubMed:20855895). {ECO:0000269|PubMed:18178555, ECO:0000269|PubMed:20855895}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:20855895}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (3); Binding site (2); Chain (1); Disulfide bond (1); Erroneous translation (1); Glycosylation (3); Metal binding (3); Natural variant (5); Propeptide (1); Region (3); Signal peptide (1) |
| Keywords | Alternative splicing;Carboxypeptidase;Chromosomal rearrangement;Cleavage on pair of basic residues;Disease variant;Disulfide bond;Epilepsy;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18178555}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,008 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=266 uM for 3-(2-furyl)acryloyl-Phe-Phe {ECO:0000269|PubMed:20855895}; KM=100 uM for 3-(2-furyl)acryloyl-Phe-Tyr {ECO:0000269|PubMed:20855895}; KM=386 uM for 3-(2-furyl)acryloyl-Phe-Leu {ECO:0000269|PubMed:20855895}; KM=339 uM for 3-(2-furyl)acryloyl-Phe-Trp {ECO:0000269|PubMed:20855895}; KM=786 uM for 3-(2-furyl)acryloyl-Phe-Met {ECO:0000269|PubMed:20855895}; |
| Metal Binding | METAL 196; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 199; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 324; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda |