Detail Information for IndEnz0002004461
IED ID IndEnz0002004461
Enzyme Type ID protease004461
Protein Name Serine carboxypeptidase 2
EC 3.4.16.6
CPDW-II
CP-WII
Carboxypeptidase D
Serine carboxypeptidase II

Cleaved into: Serine carboxypeptidase 2 chain A
Serine carboxypeptidase II chain A
; Serine carboxypeptidase 2 chain B
Serine carboxypeptidase II chain B
Gene Name CBP2
Organism Triticum aestivum (Wheat)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Triticinae Triticum Triticum aestivum (Wheat)
Enzyme Sequence VEPSGHAADRIARLPGQPAVDFDMYSGYITVDEGAGRSLFYLLQEAPEDAQPAPLVLWLNGGPGCSSVAYGASEELGAFRVKPRGAGLVLNEYRWNKVANVLFLDSPAGVGFSYTNTSSDIYTSGDNRTAHDSYAFLAKWFERFPHYKYRDFYIAGESYAGHYVPELSQLVHRSKNPVINLKGFMVGNGLIDDYHDYVGTFEFWWNHGIVSDDTYRRLKEACLHDSFIHPSPACDAATDVATAEQGNIDMYSLYTPVCNITSSSSSSSSSLSQQRRSRGRYPWLTGSYDPCTERYSTAYYNRRDVQMALHANVTGAMNYTWATCSDTINTHWHDAPRSMLPIYRELIAAGLRIWVFSGDTDAVVPLTATRYSIGALGLPTTTSWYPWYDDQEVGGWSQVYKGLTLVSVRGAGHEVPLHRPRQALVLFQYFLQGKPMPGQTKNAT
Enzyme Length 444
Uniprot Accession Number P08819
Absorption
Active Site ACT_SITE 158; ACT_SITE 361; ACT_SITE 413
Activity Regulation
Binding Site BINDING 251; /note=Substrate; BINDING 414; /note=Substrate
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); Beta strand (16); Binding site (2); Chain (2); Disulfide bond (3); Glycosylation (5); Helix (18); Natural variant (1); Propeptide (1); Region (2); Sequence conflict (7); Turn (5)
Keywords 3D-structure;Allergen;Carboxypeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Zymogen
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: N-glycosylated.
Signal Peptide
Structure 3D X-ray crystallography (5)
Cross Reference PDB 1BCR; 1BCS; 1WHS; 1WHT; 3SC2;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 49,506
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda