CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004067
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Xaa-Pro dipeptidase 
Protein Synonyms/Alias
 X-Pro dipeptidase; Imidodipeptidase; Peptidase D; Proline dipeptidase; Prolidase 
Gene Name
 PEPD 
Gene Synonyms/Alias
 PRD 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36RLCERLRKNPAVQAGubiquitination[1]
303GKFTADQKAVYEAVLubiquitination[2]
484ACMAGCDKAFTPFSGubiquitination[3]
Reference
 [1] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 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. 
Sequence Annotation
 METAL 276 276 Manganese 1.
 METAL 287 287 Manganese 1.
 METAL 287 287 Manganese 2.
 METAL 370 370 Manganese 2.
 METAL 412 412 Manganese 2.
 METAL 452 452 Manganese 1.
 METAL 452 452 Manganese 2.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Collagen degradation; Complete proteome; Dipeptidase; Direct protein sequencing; Disease mutation; Hydrolase; Manganese; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 493 AA 
Protein Sequence
MAAATGPSFW LGNETLKVPL ALFALNRQRL CERLRKNPAV QAGSIVVLQG GEETQRYCTD 60
TGVLFRQESF FHWAFGVTEP GCYGVIDVDT GKSTLFVPRL PASHATWMGK IHSKEHFKEK 120
YAVDDVQYVD EIASVLTSQK PSVLLTLRGV NTDSGSVCRE ASFDGISKFE VNNTILHPEI 180
VECRVFKTDM ELEVLRYTNK ISSEAHREVM KAVKVGMKEY ELESLFEHYC YSRGGMRHSS 240
YTCICGSGEN SAVLHYGHAG APNDRTIQNG DMCLFDMGGE YYCFASDITC SFPANGKFTA 300
DQKAVYEAVL RSSRAVMGAM KPGVWWPDMH RLADRIHLEE LAHMGILSGS VDAMVQAHLG 360
AVFMPHGLGH FLGIDVHDVG GYPEGVERID EPGLRSLRTA RHLQPGMVLT VEPGIYFIDH 420
LLDEALADPA RASFLNREVL QRFRGFGGVR IEEDVVVTDS GIELLTCVPR TVEEIEACMA 480
GCDKAFTPFS GPK 493 
Gene Ontology
 GO:0004177; F:aminopeptidase activity; IEA:InterPro.
 GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
 GO:0030145; F:manganese ion binding; IEA:InterPro.
 GO:0004181; F:metallocarboxypeptidase activity; TAS:ProtInc.
 GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
 GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
 GO:0006508; P:proteolysis; TAS:ProtInc. 
Interpro
 IPR007865; Aminopep_P_N.
 IPR000994; Pept_M24_structural-domain.
 IPR001131; Peptidase_M24B_aminopep-P_CS. 
Pfam
 PF05195; AMP_N
 PF00557; Peptidase_M24 
SMART
 SM01011; AMP_N 
PROSITE
 PS00491; PROLINE_PEPTIDASE 
PRINTS