Detail Information for IndEnz0002019022
IED ID IndEnz0002019022
Enzyme Type ID protease019022
Protein Name Dipeptidyl peptidase 2
EC 3.4.14.2
Dipeptidyl aminopeptidase II
Dipeptidyl peptidase 7
Dipeptidyl peptidase II
DPP II
Quiescent cell proline dipeptidase
Gene Name DPP7 DPP2 QPP
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 MGSAPWAPVLLLALGLRGLQAGARRAPDPGFQERFFQQRLDHFNFERFGNKTFPQRFLVSDRFWVRGEGPIFFYTGNEGDVWAFANNSAFVAELAAERGALLVFAEHRYYGKSLPFGAQSTQRGHTELLTVEQALADFAELLRALRRDLGAQDAPAIAFGGSYGGMLSAYLRMKYPHLVAGALAASAPVLAVAGLGDSNQFFRDVTADFEGQSPKCTQGVREAFRQIKDLFLQGAYDTVRWEFGTCQPLSDEKDLTQLFMFARNAFTVLAMMDYPYPTDFLGPLPANPVKVGCDRLLSEAQRITGLRALAGLVYNASGSEHCYDIYRLYHSCADPTGCGTGPDARAWDYQACTEINLTFASNNVTDMFPDLPFTDELRQRYCLDTWGVWPRPDWLLTSFWGGDLRAASNIIFSNGNLDPWAGGGIRRNLSASVIAVTIQGGAHHLDLRASHPEDPASVVEARKLEATIIGEWVKAARREQQPALRGGPRLSL
Enzyme Length 492
Uniprot Accession Number Q9UHL4
Absorption
Active Site ACT_SITE 162; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 418; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 443; /note=Charge relay system; /evidence=ECO:0000255
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.; EC=3.4.14.2; Evidence={ECO:0000269|PubMed:15487984};
DNA Binding
EC Number 3.4.14.2
Enzyme Function FUNCTION: Plays an important role in the degradation of some oligopeptides. {ECO:0000269|PubMed:15487984}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. Has low activity at pH 7 and is inactive at pH 8.;
Pathway
nucleotide Binding
Features Active site (3); Beta strand (13); Chain (1); Glycosylation (6); Helix (19); Natural variant (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (4)
Keywords 3D-structure;Aminopeptidase;Cleavage on pair of basic residues;Cytoplasmic vesicle;Direct protein sequencing;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:15487984}. Cytoplasmic vesicle {ECO:0000269|PubMed:15487984}. Secreted {ECO:0000269|PubMed:15487984}.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000269|PubMed:15487984, ECO:0000269|PubMed:19159218}.
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D X-ray crystallography (3)
Cross Reference PDB 3JYH; 3N0T; 4EBB;
Mapped Pubmed ID 12529175; 15231747; 18823758; 18985028; 19556882; 20217867; 20534982; 20711500; 22952628; 24835590; 8692836;
Motif
Gene Encoded By
Mass 54,341
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.14.2;