DPP9
entrez
91039
canonical
uniprot
Q86TI2
canonical
ensembl
ENSG00000142002
resolver
ensp
ENSP00000262960
resolver
ensp
ENSP00000469603
resolver
ensp
ENSP00000471629
resolver
ensp
ENSP00000472224
resolver
ensp
ENSP00000472430
resolver
ensp
ENSP00000496196
resolver
ensp
ENSP00000515244
resolver
ensp
ENSP00000515514
resolver
ensp
ENSP00000525591
resolver
ensp
ENSP00000525592
resolver
ensp
ENSP00000642935
resolver
ensp
ENSP00000642936
resolver
ensp
ENSP00000672557
resolver
ensp
ENSP00000672558
resolver
ensp
ENSP00000680021
resolver
ensp
ENSP00000680023
resolver
enst
ENST00000597849
resolver
genesymbol
DPP9
resolver
genesymbol_syn
DPRP2
resolver
hgnc
HGNC:18648
resolver
uniprot
M0R2A8
resolver
uniprot
O75273
resolver
uniprot
O75868
resolver
uniprot
Q1ZZB8
resolver
uniprot
Q6AI37
resolver
uniprot
Q6UAL0
resolver
uniprot
Q6ZMT2
resolver
uniprot
Q6ZNJ5
resolver
uniprot
Q8N2J7
resolver
uniprot
Q8N3F5
resolver
uniprot
Q8WXD8
resolver
uniprot
Q96NT8
resolver
uniprot
Q9BVR3
resolver
uniprot_entry
DPP9_HUMAN
resolver
uniprot_entry
M0R2A8_HUMAN
resolver
uniprot_sec
O75273
resolver
uniprot_sec
O75868
resolver
uniprot_sec
Q1ZZB8
resolver
uniprot_sec
Q6AI37
resolver
uniprot_sec
Q6UAL0
resolver
uniprot_sec
Q6ZMT2
resolver
uniprot_sec
Q6ZNJ5
resolver
uniprot_sec
Q8N2J7
resolver
uniprot_sec
Q8N3F5
resolver
uniprot_sec
Q8WXD8
resolver
uniprot_sec
Q96NT8
resolver
uniprot_sec
Q9BVR3
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfluorophosphate (PubMed:12662155). Inhibited by Val-boroPro (Talabostat, PT-100), a non-selective inhibitor, which triggers pyroptosis in monocytes and macrophages (PubMed:27820798, PubMed:29967349, PubMed:32796818, PubMed:33731932, PubMed:36357533). 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 (PubMed:33731932, PubMed:34019797, PubMed:36357533). 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 (PubMed:34019797). Chemical inhibition of DPP9 by Val-boroPro in HIV-1-infected cells activates the CARD8 inflammasome, triggering cell death, offering a promising strategy for the elimination of HIV-1 reservoirs in people living with HIV-1 (PubMed:36357533). {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29967349, ECO:0000269|PubMed:32796818, ECO:0000269|PubMed:33731932, ECO:0000269|PubMed:34019797, ECO:0000269|PubMed:36357533}.
uniprot
proteins
amino_acid_sequence
MATTGTPTADRGDAAATDDPAARFQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLLSWKQMLDHFQATPHHGVYSREEELLRERKRLGVFGITSYDFHSESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCSGPRMDPKICPADPAFFSFINNSDLWVANIETGEERRLTFCHQGLSNVLDDPKSAGVATFVIQEEFDRFTGYWWCPTASWEGSEGLKTLRILYEEVDESEVEVIHVPSPALEERKTDSYRYPRTGSKNPKIALKLAEFQTDSQGKIVSTQEKELVQPFSSLFPKVEYIARAGWTRDGKYAWAMFLDRPQQWLQLVLLPPALFIPSTENEEQRLASARAVPRNVQPYVVYEEVTNVWINVHDIFYPFPQSEGEDELCFLRANECKTGFCHLYKVTAVLKSQGYDWSEPFSPGEDEFKCPIKEEIALTSGEWEVLARHGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVRLTTPGFSHSCSMSQNFDMFVSHYSSVSTPPCVHVYKLSGPDDDPLHKQPRFWASMMEAASCPPDYVPPEIFHFHTRSDVRLYGMIYKPHALQPGKKHPTVLFVYGGPQVQLVNNSFKGIKYLRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQHGYEAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL
uniprot
proteins
disease_involvement
DISEASE: Hatipoglu immunodeficiency syndrome (HATIS) [MIM:620331]: An autosomal recessive immunologic disorder manifesting in infancy or early childhood, and characterized by failure to thrive, short stature, skin pigmentation abnormalities, pancytopenia, and susceptibility to recurrent infections. {ECO:0000269|PubMed:36112693}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:12662155, PubMed:16475979, PubMed:19667070, PubMed:29382749, PubMed:30291141, PubMed:33731929, PubMed:36112693). 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:29967349, PubMed:30291141, PubMed:31525884, PubMed:32796818, PubMed:36112693, PubMed:36357533). 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 (PubMed:33731929, PubMed:33731932, PubMed:34019797). 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 (PubMed:33731929). {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:16475979, ECO:0000269|PubMed:19667070, ECO:0000269|PubMed:27820798, ECO:0000269|PubMed:29382749, ECO:0000269|PubMed:29967349, ECO:0000269|PubMed:30291141, ECO:0000269|PubMed:31525884, ECO:0000269|PubMed:32796818, ECO:0000269|PubMed:33731929, ECO:0000269|PubMed:33731932, ECO:0000269|PubMed:34019797, ECO:0000269|PubMed:36112693, ECO:0000269|PubMed:36357533}.
uniprot
proteins
mass_dalton
98263
uniprot
proteins
mutagenesis
MUTAGEN 96..97; /note="RK->EE: Reduced interaction with CARD8 without affecting the peptidase activity."; /evidence="ECO:0000269|PubMed:34019797"; MUTAGEN 100..101; /note="LL->EE: Reduced interaction with NLRP1 and CARD8 without affecting the peptidase activity."; /evidence="ECO:0000269|PubMed:33731932, ECO:0000269|PubMed:34019797"; MUTAGEN 102..103; /note="LL->EE: Reduced interaction with CARD8 without affecting the peptidase activity."; /evidence="ECO:0000269|PubMed:34019797"; MUTAGEN 102; /note="L->E: Reduced interaction with NLRP1 without affecting the peptidase activity."; /evidence="ECO:0000269|PubMed:33731929"; MUTAGEN 597; /note="E->R: Reduced interaction with NLRP1 without affecting the peptidase activity."; /evidence="ECO:0000269|PubMed:33731932"; MUTAGEN 730; /note="S->A: Abolished dipeptidyl peptidase activity and ability to sequester NLRP1 and inhibit pyroptosis."; /evidence="ECO:0000269|PubMed:30291141, ECO:0000269|PubMed:33731929
uniprot
proteins
protein_family
DPPIV subfamily
uniprot
proteins
protein_family
Peptidase S9B family
uniprot
proteins
pubmed
12459266
uniprot
proteins
pubmed
12662155
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15245913
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16475979
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19667070
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24562348
uniprot
proteins
pubmed
27820798
uniprot
proteins
pubmed
29382749
uniprot
proteins
pubmed
29967349
uniprot
proteins
pubmed
30291141
uniprot
proteins
pubmed
31525884
uniprot
proteins
pubmed
32796818
uniprot
proteins
pubmed
33731929
uniprot
proteins
pubmed
33731932
uniprot
proteins
pubmed
34019797
uniprot
proteins
pubmed
36112693
uniprot
proteins
pubmed
36357533
uniprot
proteins
sequence_length
863
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15245913}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:24562348}.
uniprot
proteins