| IED ID | IndEnz0002018836 | 
| Enzyme Type ID | protease018836 | 
| Protein Name | 
                        
                            
                                Serine carboxypeptidase II-2  EC 3.4.16.6 CP-MII.2 Cleaved into: Serine carboxypeptidase II-2 chain A; Serine carboxypeptidase II-2 chain B Fragment  | 
                    
| Gene Name | CXP;2-2 | 
| Organism | Hordeum vulgare (Barley) | 
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Hordeinae Hordeum Hordeum vulgare (Barley) | 
| Enzyme Sequence | VPRVPGQAFDASFAHYAGYVTVSEDRGAALFYWFFEAAHDPASKPLLLWLNGGPGCSSIAFGVGEEVGPFHVNADGKGVHMNPYSWNQVANILFLDSPVGVGYSYSNTSADILSNGDERTAKDSLVFLTKWLERFPQYKEREFYLTGESYAGHYVPQLAQAIKRHHEATGDKSINLKGYMVGNALTDDFHDHYGIFQYMWTTGLISDQTYKLLNIFCDFESFVHTSPQCDKILDIASTEAGNIDSYSIFTPTCHSSFASSRNKVVKRLRSVGKMGEQYDPCTEKHSIVYFNLHEVQKALHVNPVIGKSKWETCSEVINTNWKDCERSVLHIYHELIQYGLRIWMFSGDTDAVIPVTSTRYSIDALKLPTVTPWHAWYDDDGEVGGWTQGYKGLNFVTVRGAGHEVPLHRPKQALTLIKSFLAGRPMPVLSDLRSDM | 
| Enzyme Length | 436 | 
| Uniprot Accession Number | P55748 | 
| Absorption | |
| Active Site | ACT_SITE 149; /evidence=ECO:0000250; ACT_SITE 350; /evidence=ECO:0000250; ACT_SITE 403; /evidence=ECO:0000250 | 
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal arginine or lysine residue.; EC=3.4.16.6; | 
| DNA Binding | |
| EC Number | 3.4.16.6 | 
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (3); Glycosylation (1); Non-terminal residue (1); Propeptide (1) | 
| Keywords | Carboxypeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Zymogen | 
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The linker peptide is endoproteolytically excised during enzyme maturation. {ECO:0000250}. | 
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 48,952 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |