| IED ID | IndEnz0002014052 |
| Enzyme Type ID | protease014052 |
| Protein Name |
Carboxypeptidase B2 EC 3.4.17.20 Carboxypeptidase R CPR Carboxypeptidase U CPU Thrombin-activable fibrinolysis inhibitor TAFI |
| Gene Name | Cpb2 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MKLYGLGVLVAIILYEKHGLAFQSGHVLSALPRTSRQVQLLQNLTTTYEVVLWQPVTAEFIEKKKEVHFFVNASDVNSVKAYLNASRIPFNVLMNNVEDLIQQQTSNDTVSPRASSSYYEQYHSLNEIYSWIEVITEQHPDMLQKIYIGSSYEKYPLYVLKVSGKEHRVKNAIWIDCGIHAREWISPAFCLWFIGYVTQFHGKENTYTRLLRHVDFYIMPVMNVDGYDYTWKKNRMWRKNRSVHMNNRCVGTDLNRNFASKHWCEKGASSFSCSETYCGLYPESEPEVKAVADFLRRNINHIKAYISMHSYSQQILFPYSYNRSKSKDHEELSLVASEAVRAIESINKNTRYTHGSGSESLYLAPGGSDDWIYDLGIKYSFTIELRDTGRYGFLLPERFIKPTCAEALAAVSKIAWHVIRNS |
| Enzyme Length | 422 |
| Uniprot Accession Number | Q9EQV9 |
| Absorption | |
| Active Site | ACT_SITE 384; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
| Activity Regulation | ACTIVITY REGULATION: TAFI/CPB2 is unique among carboxypeptidases in that it spontaneously inactivates with a short half-life, a property that is crucial for its role in controlling blood clot lysis. The zymogen is stabilized by interactions with the activation peptide. Release of the activation peptide increases a dynamic flap mobility and in time this leads to conformational changes that disrupt the catalytic site and expose a cryptic thrombin-cleavage site present at Arg-323 (By similarity). {ECO:0000250}. |
| Binding Site | BINDING 238; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730; BINDING 362; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of C-terminal Arg and Lys from a polypeptide.; EC=3.4.17.20; |
| DNA Binding | |
| EC Number | 3.4.17.20 |
| Enzyme Function | FUNCTION: Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. {ECO:0000269|PubMed:11021404}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (1); Disulfide bond (3); Glycosylation (6); Metal binding (3); Propeptide (1); Region (3); Signal peptide (1); Site (1) |
| Keywords | Blood coagulation;Carboxypeptidase;Disulfide bond;Fibrinolysis;Glycoprotein;Hemostasis;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..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11848438; 12958609; 15497025; 17002650; 17911187; 18513211; 19325462; 19386599; 22768796; 23369837; 24188431; 28289017; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,827 |
| Kinetics | |
| Metal Binding | METAL 180; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 183; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 309; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.20; |