| IED ID | IndEnz0002014039 |
| Enzyme Type ID | protease014039 |
| Protein Name |
Carboxypeptidase B EC 3.4.17.2 |
| Gene Name | CPB1 CPB |
| Organism | Sus scrofa (Pig) |
| 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 Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MLAFLILVTVTLASAHHSGEHFEGEKVFRVNVEDENDISLLHELASTRQIDFWKPDSVTQIKPHSTVDFRVKAEDILAVEDFLEQNELQYEVLINNLRSVLEAQFDSRVRTTGHSYEKYNNWETIEAWTKQVTSENPDLISRTAIGTTFLGNNIYLLKVGKPGPNKPAIFMDCGFHAREWISHAFCQWFVREAVLTYGYESHMTEFLNKLDFYVLPVLNIDGYIYTWTKNRMWRKTRSTNAGTTCIGTDPNRNFDAGWCTTGASTDPCDETYCGSAAESEKETKALADFIRNNLSSIKAYLTIHSYSQMILYPYSYDYKLPENNAELNNLAKAAVKELATLYGTKYTYGPGATTIYPAAGGSDDWAYDQGIKYSFTFELRDKGRYGFILPESQIQATCEETMLAIKYVTNYVLGHL |
| Enzyme Length | 416 |
| Uniprot Accession Number | P09955 |
| Absorption | |
| Active Site | ACT_SITE 378; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P00732 |
| Activity Regulation | |
| Binding Site | BINDING 234; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730; BINDING 356; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00730 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal lysine or arginine amino acid.; EC=3.4.17.2; Evidence={ECO:0000250|UniProtKB:P00732}; |
| DNA Binding | |
| EC Number | 3.4.17.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (20); Binding site (2); Chain (1); Disulfide bond (3); Helix (17); Metal binding (3); Propeptide (1); Region (3); Sequence conflict (2); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Carboxypeptidase;Cytoplasmic vesicle;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00732}. Zymogen granule lumen {ECO:0000250|UniProtKB:P55261}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence="ECO:0000269|PubMed:2018774, ECO:0000269|PubMed:2223783" |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (39) |
| Cross Reference PDB | 1NSA; 1PBA; 1Z5R; 1ZG7; 1ZG8; 1ZG9; 2JEW; 2PIY; 2PIZ; 2PJ0; 2PJ1; 2PJ2; 2PJ3; 2PJ4; 2PJ5; 2PJ6; 2PJ7; 2PJ8; 2PJ9; 2PJA; 2PJB; 2PJC; 3GLJ; 3WAB; 3WC5; 3WC6; 3WC7; 4UIA; 4UIB; 4Z65; 5J1Q; 5JC6; 5LRG; 5LRJ; 5LRK; 5LYD; 5LYF; 5LYI; 5LYL; 5ZEQ; |
| Mapped Pubmed ID | 15982000; 17990866; 18219114; 19802820; 24010887; 25990761; 26457527; 27604544; 27749053; 28274181; 29859906; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,381 |
| Kinetics | |
| Metal Binding | METAL 176; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15086; METAL 179; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15086; METAL 304; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15086 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.2; |