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Details on Person UniProt:P12955-2 PEPD
| Class:Id | ReferenceIsoform:8969799 |
|---|---|
| _chainChangeLog | initiator methionine:1 added on Fri February 17 2017;chain:2-493 added on Fri February 17 2017;initiator methionine:1 for 8969799 removed on Fri Nov 03 2023;initiator methionine: for 8969799 added on Fri Nov 03 2023;initiator methionine: for 8969799 removed on Fri Aug 15 2025;initiator methionine:1 for 8969799 added on Fri Aug 15 2025 |
| _displayName | UniProt:P12955-2 PEPD |
| _timestamp | 2025-08-15 21:47:41 |
| chain | initiator methionine:1 chain:2-493 |
| checksum | E8C4A2497E44BA22 |
| comment | 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).CATALYTIC ACTIVITY Xaa-L-Pro dipeptide + H2O = an L-alpha-amino acid + L-prolineCOFACTOR Binds 2 manganese ions per subunit.ACTIVITY REGULATION Specifically inhibited by the pseudodipeptide CQ31 (PubMed:35165443). Inhibition by CQ31 indirectly activates the CARD8 inflammasome: dipeptide accumulation following PEPD inactivation weaky inhibit dipeptidyl peptidases DDP8 and DPP9, relieving DPP8- and/or DPP9-mediated inhibition of CARD8 (PubMed:35165443).SUBUNIT Homodimer.INTERACTION The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily. |
| created | [InstanceEdit:8964659] Weiser, JD |
| description | recommendedName: Xaa-Pro dipeptidase shortName: X-Pro dipeptidase ecNumber evidence="5 9"3.4.13.9 alternativeName: Imidodipeptidase alternativeName: Peptidase D alternativeName: fullName evidence="14"Proline dipeptidase shortName evidence="14"Prolidase |
| geneName | PEPD PRD |
| identifier | P12955 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Alternative splicing Collagen degradation Dipeptidase Direct protein sequencing Disease variant Hydrolase Manganese Metal-binding Metalloprotease Phosphoprotein Protease Proteomics identification Reference proteome |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | PEPD |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8958615] ENSEMBL:ENSG00000124299 PEPD [Homo sapiens] |
| secondaryIdentifier | PEPD_HUMAN A8K3Z1 A8K416 A8K696 A8MX47 B4DDB7 B4DGJ1 E9PCE8 Q8TBN9 Q9BT75 |
| sequenceLength | 493 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | P12955-2 |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:P12955-2 PEPD (8969799)
