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PREP prolyl endopeptidase [ Sus scrofa (pig) ]

Gene ID: 445540, updated on 26-Jun-2026
Official Symbol
PREPprovided by VGNC
Official Full Name
prolyl endopeptidaseprovided by VGNC
Primary source
VGNC:VGNC:103157
See related
Ensembl:ENSSSCG00000004368 RGD:14297949
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Sus scrofa
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus
Expression
Ubiquitous expression in ovary (RPKM 34.5), psoas major muscle (RPKM 13.5) and 8 other tissues See more
Orthologs
all
Try the new Gene page
Try the new Transcripts and proteins table
See PREP in Genome Data Viewer
Location:
chromosome: 1
Exon count:
22
Annotation release Status Assembly Chr Location
RS_2026_06 current Sscrofa_HxYL_maternal_Yorkshire_Landrace_v2.0 (GCF_054392235.1) 1 NC_139383.1 (71666108..72228546, complement)
106 previous assembly Sscrofa11.1 (GCF_000003025.6) 1 NC_010443.5 (71496299..72027308, complement)

Chromosome 1 - NC_139383.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC106508909 Neighboring gene popeye domain cAMP effector 3 Neighboring gene uncharacterized LOC146406140 Neighboring gene large ribosomal subunit protein eL6 pseudogene Neighboring gene uncharacterized LOC106507207

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Analyzing slowly exchanging protein conformations by ion mobility mass spectrometry: study of the dynamic equilibrium of prolyl oligopeptidase. López A, et al. J Mass Spectrom, 2016 Jul. PMID 27434808
  2. Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification. Stone SR, et al. Biochem J, 1991 Jun 15. PMID 2064618, Free PMC Article
  3. cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue. Rennex D, et al. Biochemistry, 1991 Feb 26. PMID 1900195
  4. Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Fülöp V, et al. Cell, 1998 Jul 24. PMID 9695945
  5. Structural analysis of prolyl oligopeptidases using molecular docking and dynamics: insights into conformational changes and ligand binding. Kaushik S, et al. PLoS One, 2011. PMID 22132071, Free PMC Article

See all (9) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Ion mobility mass spectrometry (IMMS) experiments detected two species of PREP that correlated well with the open and closed conformations in dynamic equilibrium. Therefore, these findings emphasize the value of IMMS for the study of multiple co-existing conformations of large proteins in slow equilibrium in solution.
    Title: Analyzing slowly exchanging protein conformations by ion mobility mass spectrometry: study of the dynamic equilibrium of prolyl oligopeptidase.
  2. Molecular modeling and docking based approaches were used to unravel questions like differences in ligand binding affinities in three POP species (porcine, human and A. thaliana).
    Title: Structural analysis of prolyl oligopeptidases using molecular docking and dynamics: insights into conformational changes and ligand binding.
Submit: New GeneRIF Correction

Markers

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables oligopeptidase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables serine-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytosol IEA
Inferred from Electronic Annotation
more info
 PubMed 
Preferred Names
prolyl endopeptidase
Names
PE
post-proline cleaving enzyme
NP_001004050.1
XP_020939260.1
XP_084867527.1
XP_084867531.1
XP_084867534.1
XP_084867545.1
XP_084867555.1
XP_084867558.1

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001004050.1 → NP_001004050.1  prolyl endopeptidase

    See identical proteins and their annotated locations for NP_001004050.1

    Status: PROVISIONAL

    Source sequence(s)
    M64227
    UniProtKB/Swiss-Prot
    P23687
    UniProtKB/TrEMBL
    A0A8D1QGF2, F1RYQ0
    Related
    ENSSSCP00000004715.4, ENSSSCT00000004829.5
    Conserved Domains (1) summary
    COG1505
    Location:26 → 704
    PreP; Prolyl oligopeptidase PreP, S9A serine peptidase family [Amino acid transport and metabolism]

RefSeqs of Annotated Genomes: GCF_054392235.1-RS_2026_06

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference Sscrofa_HxYL_maternal_Yorkshire_Landrace_v2.0

Genomic

  1. NC_139383.1 Reference Sscrofa_HxYL_maternal_Yorkshire_Landrace_v2.0

    Range
    71666108..72228546 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_085011432.1 → XP_084867558.1  prolyl endopeptidase isoform X1

  2. XM_021083601.2 → XP_020939260.1  prolyl endopeptidase isoform X1

    UniProtKB/TrEMBL
    A0A8D1QGF2, F1RYQ0
    Conserved Domains (1) summary
    COG1505
    Location:47 → 725
    PreP; Prolyl oligopeptidase PreP, S9A serine peptidase family [Amino acid transport and metabolism]

  3. XM_085011429.1 → XP_084867555.1  prolyl endopeptidase isoform X1

  4. XM_085011405.1 → XP_084867531.1  prolyl endopeptidase isoform X1

  5. XM_085011401.1 → XP_084867527.1  prolyl endopeptidase isoform X1

  6. XM_085011408.1 → XP_084867534.1  prolyl endopeptidase isoform X1

  7. XM_085011419.1 → XP_084867545.1  prolyl endopeptidase isoform X1

RNA

  1. XR_014837058.1 RNA Sequence

  2. XR_014837057.1 RNA Sequence

Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P23687.1 GenPept UniProtKB/Swiss-Prot:P23687

Gene LinkOut

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Molecular Biology Databases
Research Materials