| IED ID | IndEnz0002014047 |
| Enzyme Type ID | protease014047 |
| Protein Name |
Carboxypeptidase B2 EC 3.4.17.20 Carboxypeptidase U CPU Plasma carboxypeptidase B pCPB Thrombin-activable fibrinolysis inhibitor TAFI |
| Gene Name | CPB2 |
| 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 | MKLCSLAVLVPIVLFCEQHVFAFQSGQVLAALPRTSRQVQVLQNLTTTYEIVLWQPVTADLIVKKKQVHFFVNASDVDNVKAHLNVSGIPCSVLLADVEDLIQQQISNDTVSPRASASYYEQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQAAKNAIWIDCGIHAREWISPAFCLWFIGHITQFYGIIGQYTNLLRLVDFYVMPVVNVDGYDYSWKKNRMWRKNRSFYANNHCIGTDLNRNFASKHWCEEGASSSSCSETYCGLYPESEPEVKAVASFLRRNINQIKAYISMHSYSQHIVFPYSYTRSKSKDHEELSLVASEAVRAIEKISKNTRYTHGHGSETLYLAPGGGDDWIYDLGIKYSFTIELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVIRNV |
| Enzyme Length | 423 |
| Uniprot Accession Number | Q96IY4 |
| Absorption | |
| Active Site | ACT_SITE 385; /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-324. {ECO:0000269|PubMed:18559974}. |
| Binding Site | BINDING 239; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730; BINDING 363; /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; Evidence={ECO:0000269|PubMed:10574983}; |
| 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:10574983}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Beta strand (14); Binding site (2); Chain (1); Disulfide bond (3); Glycosylation (5); Helix (17); Metal binding (3); Natural variant (2); Propeptide (1); Region (3); Sequence conflict (1); Signal peptide (1); Site (1); Turn (7) |
| Keywords | 3D-structure;Alternative splicing;Blood coagulation;Carboxypeptidase;Direct protein sequencing;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 | PTM: N-glycosylated. N-glycan at Asn-108: Hex5HexNAc4. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16445295, ECO:0000269|PubMed:18559974, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (10) |
| Cross Reference PDB | 3D66; 3D67; 3D68; 3LMS; 4P10; 5HVF; 5HVG; 5HVH; 7NEE; 7NEU; |
| Mapped Pubmed ID | 11565542; 11903334; 11939578; 12624641; 14525995; 15521922; 17107352; 17138567; 21988832; 2443571; 24588961; 2708524; 27279497; 33764059; 4098172; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,424 |
| Kinetics | |
| Metal Binding | METAL 181; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:18559974, ECO:0000269|PubMed:20088943"; METAL 184; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:18559974, ECO:0000269|PubMed:20088943"; METAL 310; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:18559974, ECO:0000269|PubMed:20088943" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.20; |