Prolyl endopeptidase
Details
- Name
- Prolyl endopeptidase
- Synonyms
- 3.4.21.26
- PE
- PEP
- Post-proline cleaving enzyme
- Gene Name
- PREP
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0011558|Prolyl endopeptidase MLSLQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILS DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTH DGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAEL SDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVF TFKTNRQSPNYRVINIDFRDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNI LQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPR VFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI TPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE GYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG CSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV GRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP
- Number of residues
- 710
- Molecular Weight
- 80698.945
- Theoretical pI
- 5.58
- GO Classification
- Functionsserine-type endopeptidase activity / serine-type exopeptidase activity / serine-type peptidase activityProcessesproteolysisComponentscytoplasm / membrane / nucleus
- General Function
- Serine-type peptidase activity
- Specific Function
- Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011559|Prolyl endopeptidase (PREP) ATGCTGTCCCTTCAGTACCCCGACGTGTACCGCGACGAGACCGCCGTACAGGATTATCAT GGTCATAAAATTTGTGACCCTTACGCCTGGCTTGAAGACCCCGACAGTGAACAGACTAAG GCCTTTGTGGAGGCCCAGAATAAGATTACTGTGCCATTTCTTGAGCAGTGTCCCATCAGA GGTTTATACAAAGAGAGAATGACTGAACTATATGATTATCCCAAGTATAGTTGCCACTTC AAGAAAGGAAAACGGTATTTTTATTTTTACAATACAGGTTTGCAGAACCAGCGAGTATTA TATGTACAGGATTCCTTAGAGGGTGAGGCCAGAGTGTTCCTGGACCCCAACATACTGTCT GACGATGGCACAGTGGCACTCCGAGGTTATGCGTTCAGCGAAGATGGTGAATATTTTGCC TATGGTCTGAGTGCCAGTGGCTCAGACTGGGTGACAATCAAGTTCATGAAAGTTGATGGT GCCAAAGAGCTTCCAGATGTGCTTGAAAGAGTCAAGTTCAGCTGTATGGCCTGGACCCAT GATGGGAAGGGAATGTTCTACAACTCATACCCTCAACAGGATGGAAAAAGTGATGGCACA GAGACATCTACCAATCTCCACCAAAAGCTCTACTACCATGTCTTGGGAACCGATCAGTCA GAAGATATTTTGTGTGCTGAGTTTCCTGATGAACCTAAATGGATGGGTGGAGCTGAGTTA TCTGATGATGGCCGCTATGTCTTGTTATCAATAAGGGAAGGATGTGATCCAGTAAACCGA CTCTGGTACTGTGACCTACAGCAGGAATCCAGTGGCATCGCGGGAATCCTGAAGTGGGTA AAACTGATTGACAACTTTGAAGGGGAATATGACTACGTGACCAATGAGGGGACGGTGTTC ACATTCAAGACGAATCGCCAGTCTCCCAACTATCGCGTGATCAACATTGACTTCAGGGAT CCTGAAGAGTCTAAGTGGAAAGTACTTGTTCCTGAGCATGAGAAAGATGTCTTAGAATGG ATAGCTTGTGTCAGGTCCAACTTCTTGGTCTTATGCTACCTCCATGACGTCAAGAACATT CTGCAGCTCCATGACCTGACTACTGGTGCTCTCCTTAAGACCTTCCCGCTCGATGTCGGC AGCATTGTAGGGTACAGCGGTCAGAAGAAGGACACTGAAATCTTCTATCAGTTTACTTCC TTTTTATCTCCAGGTATCATTTATCACTGTGATCTTACCAAAGAGGAGCTGGAGCCAAGA GTTTTCCGAGAGGTGACCGTAAAAGGAATTGATGCTTCTGATTACCAGACAGTCCAGATT TTCTACCCTAGCAAGGATGGTACGAAGATTCCAATGTTCATTGTGCATAAAAAAGGCATA AAATTGGATGGCTCTCATCCAGCTTTCTTATATGGCTATGGCGGCTTCAACATATCCATC ACACCCAACTACAGTGTTTCCAGGCTTATTTTTGTGAGACACATGGGTGGTATCCTGGCA GTGGCCAACATCAGAGGAGGTGGCGAATATGGAGAGACGTGGCATAAAGGTGGTATCTTG GCCAACAAACAAAACTGCTTTGATGACTTTCAGTGTGCTGCTGAGTATCTGATCAAGGAA GGTTACACATCTCCCAAGAGGCTGACTATTAATGGAGGTTCAAATGGAGGCCTCTTAGTG GCTGCTTGTGCAAATCAGAGACCTGACCTCTTTGGTTGTGTTATTGCCCAAGTTGGAGTA ATGGACATGCTGAAGTTTCATAAATATACCATCGGCCATGCTTGGACCACTGATTATGGG TGCTCGGACAGCAAACAACACTTTGAATGGCTTGTCAAATACTCTCCATTGCATAATGTG AAGTTACCAGAAGCAGATGACATCCAGTACCCGTCCATGCTGCTCCTCACTGCTGACCAT GATGACCGCGTGGTCCCGCTTCACTCCCTGAAGTTCATTGCCACCCTTCAGTACATCGTG GGCCGCAGCAGGAAGCAAAGCAACCCCCTGCTTATCCACGTGGACACCAAGGCGGGCCAC GGGGCGGGGAAGCCCACAGCCAAAGTGATAGAGGAAGTCTCAGACATGTTTGCGTTCATC GCGCGGTGCCTGAACGTCGACTGGATTCCATAA
- Chromosome Location
- 6
- Locus
- 6q22
- External Identifiers
Resource Link UniProtKB ID P48147 UniProtKB Entry Name PPCE_HUMAN GenBank Protein ID 558596 GenBank Gene ID X74496 GenAtlas ID PREP HGNC ID HGNC:9358 - General References
- Vanhoof G, Goossens F, Hendriks L, De Meester I, Hendriks D, Vriend G, Van Broeckhoven C, Scharpe S: Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase. Gene. 1994 Nov 18;149(2):363-6. [Article]
- Shirasawa Y, Osawa T, Hirashima A: Molecular cloning and characterization of prolyl endopeptidase from human T cells. J Biochem. 1994 Apr;115(4):724-9. [Article]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Goossens F, De Meester I, Vanhoof G, Hendriks D, Vriend G, Scharpe S: The purification, characterization and analysis of primary and secondary-structure of prolyl oligopeptidase from human lymphocytes. Evidence that the enzyme belongs to the alpha/beta hydrolase fold family. Eur J Biochem. 1995 Oct 15;233(2):432-41. [Article]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
- Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
- Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
- Haffner CD, Diaz CJ, Miller AB, Reid RA, Madauss KP, Hassell A, Hanlon MH, Porter DJ, Becherer JD, Carter LH: Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP). Bioorg Med Chem Lett. 2008 Aug 1;18(15):4360-3. doi: 10.1016/j.bmcl.2008.06.067. Epub 2008 Jun 24. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01684 1-Hydroxy-1-Thio-Glycerol experimental unknown Details DB03382 S-oxy-L-cysteine experimental unknown Details DB03864 Monothioglycerol experimental unknown Details DB07148 (6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)pyrrolo[1,2-a]pyrazin-4(6H)-one experimental unknown Details DB08738 1-{3-oxo-3-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]propyl}-3-phenylquinoxalin-2(1H)-one experimental unknown Details DB08739 2-{3-[(2S)-4,4-difluoro-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-3-oxopropyl}-isoindole-1,3(2H)-dione experimental unknown Details DB03535 Z-Pro-Prolinal experimental unknown Details DB00107 Oxytocin approved, vet_approved unknown substrate Details