| IED ID | IndEnz0002000196 |
| Enzyme Type ID | protease000196 |
| Protein Name |
Xaa-Pro dipeptidase X-Pro dipeptidase EC 3.4.13.9 Imidodipeptidase Peptidase D Proline dipeptidase Prolidase |
| Gene Name | PEPD PRD |
| 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 | MAAATGPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGGEETQRYCTDTGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLPASHATWMGKIHSKEHFKEKYAVDDVQYVDEIASVLTSQKPSVLLTLRGVNTDSGSVCREASFDGISKFEVNNTILHPEIVECRVFKTDMELEVLRYTNKISSEAHREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSSYTCICGSGENSAVLHYGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTADQKAVYEAVLRSSRAVMGAMKPGVWWPDMHRLADRIHLEELAHMGILSGSVDAMVQAHLGAVFMPHGLGHFLGIDVHDVGGYPEGVERIDEPGLRSLRTARHLQPGMVLTVEPGIYFIDHLLDEALADPARASFLNREVLQRFRGFGGVRIEEDVVVTDSGIELLTCVPRTVEEIEACMAGCDKAFTPFSGPK |
| Enzyme Length | 493 |
| Uniprot Accession Number | P12955 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.; EC=3.4.13.9; |
| DNA Binding | |
| EC Number | 3.4.13.9 |
| Enzyme Function | FUNCTION: Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (18); Chain (1); Helix (21); Initiator methionine (1); Metal binding (7); Modified residue (2); Natural variant (7); Sequence conflict (14); Turn (4) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Collagen degradation;Dipeptidase;Direct protein sequencing;Disease variant;Hydrolase;Manganese;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome |
| Interact With | P54253; P54274 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"; MOD_RES 167; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (21) |
| Cross Reference PDB | 2IW2; 2OKN; 5M4G; 5M4J; 5M4L; 5M4Q; 5MBY; 5MBZ; 5MC0; 5MC1; 5MC2; 5MC3; 5MC4; 5MC5; 6H2P; 6H2Q; 6QSB; 6QSC; 6SRE; 6SRF; 6SRG; |
| Mapped Pubmed ID | 11820613; 15878628; 16713569; 16999949; 17096092; 17377743; 17570078; 17604013; 17999410; 18202846; 18387361; 18514097; 18550075; 18607169; 18989777; 19263194; 19401414; 19823062; 20087956; 20383038; 20437180; 20486204; 20626024; 20711500; 20868675; 21044950; 21722016; 21988832; 22185542; 22245250; 22258852; 22811354; 22999980; 23163753; 23171426; 23212918; 23242638; 23287645; 23457135; 23516557; 23549681; 23553128; 24065222; 24225260; 24484408; 24606918; 24612543; 24810047; 25031340; 25120796; 25842545; 25994092; 26078578; 26087900; 26509313; 26870880; 27320745; 27387023; 27443556; 28462712; 28534076; 28677335; 28867357; 29233996; 29668362; 29873502; 30066404; 30796241; 32598484; 32734598; 33477820; 33477899; 34880421; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,548 |
| Kinetics | |
| Metal Binding | METAL 276; /note=Manganese 1; METAL 287; /note=Manganese 1; METAL 287; /note=Manganese 2; METAL 370; /note=Manganese 2; METAL 412; /note=Manganese 2; METAL 452; /note=Manganese 1; METAL 452; /note=Manganese 2 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.13.9; |