IED ID | IndEnz0002018571 |
Enzyme Type ID | protease018571 |
Protein Name |
Carboxypeptidase A6 EC 3.4.17.- |
Gene Name | Cpa6 |
Organism | Mus musculus (Mouse) |
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 Mus Mus Mus musculus (Mouse) |
Enzyme Sequence | MNFLGNPRSHTAAFLPVCWLLLNILKPGHCHSYDNRYAGDKVIRLIPKSEEEALALKNIYHQLKVDLWQPSSISYVSEGTITDVHISQNASRTLLAFLQETHIYYKVLIEDLQKAVENENSLQTQRNRRSLSEYNYEVYHSLEDIQSWLHHLNQTQPGLVRVFSIGRSYEGRPLFIMQLGRKSRAYKRAVWIDCGIHAREWIGPAFCQWFVREAILTYKTDPAMKKMLNHLYFYIMPVFNVDGYHFSWTHDRFWRKTRSRDSKFRCRGVDANRNWKVKWCDEGASAHPCDDTYCGPFPESEPEVKAVANFLRKHRKRIRAYLSFHAYAQMLLYPYSYKYATIPNFSCVEFAAHKAVKALRSVHGIRYRHGPASQTLYVSSGNSMDWAYKNGIPYAFAFELRDTGHFGFLLPEMLIKPTCTETMLAVKNITMHLLKKCP |
Enzyme Length | 438 |
Uniprot Accession Number | Q5U901 |
Absorption | |
Active Site | ACT_SITE 399; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
Activity Regulation | |
Binding Site | BINDING 255; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730; BINDING 377; /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. 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. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (1); Binding site (2); Chain (1); Disulfide bond (1); Glycosylation (4); Metal binding (3); Propeptide (1); Region (3); Signal peptide (1) |
Keywords | Alternative splicing;Carboxypeptidase;Cleavage on pair of basic residues;Disulfide bond;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:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 18178555; 21677750; |
Motif | |
Gene Encoded By | |
Mass | 51,143 |
Kinetics | |
Metal Binding | METAL 197; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 200; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 325; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
Rhea ID | |
Cross Reference Brenda | 3.4.17.1; |