| IED ID | IndEnz0002004472 |
| Enzyme Type ID | protease004472 |
| Protein Name |
Carboxypeptidase O CPO EC 3.4.17.- |
| Gene Name | CPO |
| Organism | Bos taurus (Bovine) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MKPLLGTFYLLGMLVPGWLGYDRSLTQQRQEVVDKVVSPWSILETYSYNRYHPMGEIYQWMSEIREKYTEVVTQHFLGMTYESRPMYYLKISQPSSNPKKIIWMDCGIHAREWIAPAFCQWFVKEILQNYEDNSRIRRLLKNLDFYVLPVLNIDGYIYTWTTDRLWRKSRSSHNNGTCFGTDLNRNFDASWCSIGASHNCESLTFCGTGPMSEPETKAVSSFIESKKENIACFLTMHSYGQLILVPYGYTKNKSNNHEELIQVGQKAANALKAKHGTNYRVGSSADILYATSGSSRDWARDIGIPFSYTFELRDNGTYGFVLPETQIQATCEETMEAVLSVLDDVYEKYWYTNSARKAKSTALVLGLLMSFMSLL |
| Enzyme Length | 375 |
| Uniprot Accession Number | Q0II73 |
| Absorption | |
| Active Site | ACT_SITE 311; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00730 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Carboxypeptidase which preferentially cleaves C-terminal acidic residues from peptides and proteins. Can also cleave C-terminal hydrophobic amino acids, with a preference for small residues over large residues. {ECO:0000250|UniProtKB:Q8IVL8}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (3); Lipidation (1); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Carboxypeptidase;Cell membrane;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q8IVL8}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8IVL8}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000250|UniProtKB:Q8IVL8 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,175 |
| Kinetics | |
| Metal Binding | METAL 109; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 112; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 237; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda |