Dpp9
entrez
224897
canonical
uniprot
Q8BVG4
canonical
ensembl
ENSMUSG00000001229
resolver
ensp
ENSMUSP00000046604
resolver
ensp
ENSMUSP00000285260
resolver
ensp
ENSMUSP00000285302
resolver
genesymbol
Dpp9
resolver
uniprot
Q6KAM9
resolver
uniprot
Q8BWT9
resolver
uniprot_entry
DPP9_MOUSE
resolver
uniprot_sec
Q6KAM9
resolver
uniprot_sec
Q8BWT9
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfluorophosphate (By similarity). Inhibited by Val-boroPro (Talabostat, PT-100), a non-selective inhibitor, which triggers pyroptosis in monocytes and macrophages (PubMed:27820798, PubMed:29396289). Val-boroPro inhibits activity by binding to the active site, mimicking a substrate-bound state, thereby displacing the C-terminal fragment of NLRP1, leading to activation of the NLRP1 inflammasome. In contrast, Val-boroPro does not directly displaces CARD8: it acts by promoting degradation of the N-terminal part of CARD8, leading to indirect disruption of the ternary complex (By similarity). {ECO:0000250|UniProtKB:Q86TI2, ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29396289}.
uniprot
proteins
amino_acid_sequence
MCSGVSPVEQVAAGDMDDTAARFCVQKHSWDGLRSIIHGSRKSSGLIVSKAPHDFQFVQKPDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLLSWKQMLDHFQATPHHGVYSREEELLRERKRLGVFGITSYDFHSESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCSGPRMDPKICPADPAFFSFINNSDLWVANIETGEERRLTFCHQGSAGVLDNPKSAGVATFVIQEEFDRFTGCWWCPTASWEGSEGLKTLRILYEEVDESEVEVIHVPSPALEERKTDSYRYPRTGSKNPKIALKLAELQTDHQGKIVSSCEKELVQPFSSLFPKVEYIARAGWTRDGKYAWAMFLDRPQQRLQLVLLPPALFIPAVESEAQRQAAARAVPKNVQPFVIYEEVTNVWINVHDIFHPFPQAEGQQDFCFLRANECKTGFCHLYRVTVELKTKDYDWTEPLSPTEDEFKCPIKEEVALTSGEWEVLSRHGSKIWVNEQTKLVYFQGTKDTPLEHHLYVVSYESAGEIVRLTTLGFSHSCSMSQSFDMFVSHYSSVSTPPCVHVYKLSGPDDDPLHKQPRFWASMMEAANCPPDYVPPEIFHFHTRADVQLYGMIYKPHTLQPGRKHPTVLFVYGGPQVQLVNNSFKGIKYLRLNTLASLGYAVVVIDGRGSCQRGLHFEGALKNQMGQVEIEDQVEGLQYVAEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQQGYEAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRCRESGEHYEVTLLHFLQEHL
uniprot
proteins
ec_number
3.4.14.5
uniprot
proteins
function
FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:24223149). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed:27820798, PubMed:29396289). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (By similarity). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP9, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (By similarity). {ECO:0000250|UniProtKB:Q86TI2, ECO:0000269|PubMed:24223149, ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29396289}.
uniprot
proteins
mass_dalton
98001
uniprot
proteins
mutagenesis
MUTAGEN 729; /note="S->A: Decreased levels of global dipeptidyl peptidase activity. Homozygous pups are born at the expected Mendelian rate and display no obvious morphological defects, but none survive to weaning. Homozygous pups display suckling defects and survive only when fed manually. The suckling defects are probably due to increased apoptosis of migratory tongue muscle progenitor cells, leading to defects in the development of intrinsic muscles in the distal tongue and decreased tongue size."; /evidence="ECO:0000269|PubMed:24223149, ECO:0000269|PubMed:28887018, ECO:0000269|PubMed:36112693
uniprot
proteins
protein_family
DPPIV subfamily
uniprot
proteins
protein_family
Peptidase S9B family
uniprot
proteins
pubmed
15449545
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24223149
uniprot
proteins
pubmed
27820798
uniprot
proteins
pubmed
28887018
uniprot
proteins
pubmed
29396289
uniprot
proteins
pubmed
36112693
uniprot
proteins
sequence_length
862
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24223149}.
uniprot
proteins