PEPD
entrez
5184
canonical
uniprot
P12955
canonical
ensembl
ENSG00000124299
resolver
ensp
ENSP00000244137
resolver
ensp
ENSP00000380226
resolver
ensp
ENSP00000391890
resolver
genesymbol
PEPD
resolver
genesymbol_syn
PRD
resolver
hgnc
HGNC:8840
resolver
uniprot
A0A140VJR2
resolver
uniprot
A8K3Z1
resolver
uniprot
A8K416
resolver
uniprot
A8K696
resolver
uniprot
A8MX47
resolver
uniprot
B4DDB7
resolver
uniprot
B4DGJ1
resolver
uniprot
E9PCE8
resolver
uniprot
Q8TBN9
resolver
uniprot
Q9BT75
resolver
uniprot_entry
A0A140VJR2_HUMAN
resolver
uniprot_entry
PEPD_HUMAN
resolver
uniprot_sec
A8K3Z1
resolver
uniprot_sec
A8K416
resolver
uniprot_sec
A8K696
resolver
uniprot_sec
A8MX47
resolver
uniprot_sec
B4DDB7
resolver
uniprot_sec
B4DGJ1
resolver
uniprot_sec
E9PCE8
resolver
uniprot_sec
Q8TBN9
resolver
uniprot_sec
Q9BT75
resolver
activity_regulation
ACTIVITY REGULATION: Specifically inhibited by the pseudodipeptide CQ31 (PubMed:35165443). Inhibition by CQ31 indirectly activates the CARD8 inflammasome: dipeptide accumulation following PEPD inactivation weakly inhibits dipeptidyl peptidases DDP8 and DPP9, relieving DPP8- and/or DPP9-mediated inhibition of CARD8 (PubMed:35165443). {ECO:0000269|PubMed:35165443}.
uniprot
proteins
amino_acid_sequence
MAAATGPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGGEETQRYCTDTGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLPASHATWMGKIHSKEHFKEKYAVDDVQYVDEIASVLTSQKPSVLLTLRGVNTDSGSVCREASFDGISKFEVNNTILHPEIVECRVFKTDMELEVLRYTNKISSEAHREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSSYTCICGSGENSAVLHYGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTADQKAVYEAVLRSSRAVMGAMKPGVWWPDMHRLADRIHLEELAHMGILSGSVDAMVQAHLGAVFMPHGLGHFLGIDVHDVGGYPEGVERIDEPGLRSLRTARHLQPGMVLTVEPGIYFIDHLLDEALADPARASFLNREVLQRFRGFGGVRIEEDVVVTDSGIELLTCVPRTVEEIEACMAGCDKAFTPFSGPK
uniprot
proteins
disease_involvement
DISEASE: Prolidase deficiency (PD) [MIM:170100]: A multisystem disorder associated with massive iminodipeptiduria and lack of or reduced prolidase activity in erythrocytes, leukocytes, or cultured fibroblasts. Clinical features include skin ulcers, developmental delay, recurrent infections, and a characteristic facies. {ECO:0000269|PubMed:12384772, ECO:0000269|PubMed:2365824, ECO:0000269|PubMed:8198124, ECO:0000269|PubMed:8900231}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.13.9
uniprot
proteins
function
FUNCTION: Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position (PubMed:17081196, PubMed:35165443). The preferred dipeptide substrate is Gly-Pro, but other Xaa-Pro dipeptides, such as Ala-Pro, Met-Pro, Phe-Pro, Val-Pro and Leu-Pro, can be cleaved (PubMed:17081196). Plays an important role in collagen metabolism because the high level of iminoacids in collagen (PubMed:2925654). {ECO:0000269|PubMed:17081196, ECO:0000269|PubMed:2925654, ECO:0000269|PubMed:35165443}.
uniprot
proteins
mass_dalton
54548
uniprot
proteins
protein_family
Eukaryotic-type prolidase subfamily
uniprot
proteins
protein_family
Peptidase M24B family
uniprot
proteins
pubmed
11840567
uniprot
proteins
pubmed
12384772
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081196
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
2365824
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28677335
uniprot
proteins
pubmed
2925654
uniprot
proteins
pubmed
35165443
uniprot
proteins
pubmed
8198124
uniprot
proteins
pubmed
8900231
uniprot
proteins
sequence_length
493
uniprot
proteins