XPNPEP1

Xaa-Pro aminopeptidase 1 is an enzyme that in humans is encoded by the XPNPEP1 gene.^[5]

XPNPEP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3CTZ
Identifiers
Aliases	XPNPEP1, APP1, SAMP, XPNPEP, XPNPEPL, XPNPEPL1, X-prolyl aminopeptidase (aminopeptidase P) 1, soluble, X-prolyl aminopeptidase 1
External IDs	OMIM: 602443; MGI: 2180003; HomoloGene: 6424; GeneCards: XPNPEP1; OMA:XPNPEP1 - orthologs
Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10q25.1 Start 109,864,766 bp[1] End 109,923,553 bp[1]
Gene location (Mouse) Chr. Chromosome 19 (mouse)[2] Band 19|19 D2 Start 52,920,357 bp[2] End 53,028,645 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas jejunal mucosa epithelium of nasopharynx stromal cell of endometrium duodenum skin of leg monocyte rectum skin of abdomen tibia Top expressed in gastrula jejunum ileum internal carotid artery yolk sac external carotid artery right kidney stria vascularis spermatid duodenum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activity aminopeptidase activity hydrolase activity metallopeptidase activity protein homodimerization activity manganese ion binding metal ion binding metalloaminopeptidase activity Cellular component extracellular exosome cytoplasm cytosol Biological process bradykinin catabolic process proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7511 170750 Ensembl ENSG00000108039 ENSMUSG00000025027 UniProt Q9NQW7 Q6P1B1 RefSeq (mRNA) NM_001167604 NM_020383 NM_001324128 NM_001324131 NM_001324132 NM_001324133 NM_001324134 NM_001324135 NM_001324136 NM_133216 NM_001374834 RefSeq (protein) NP_001161076 NP_001311057 NP_001311060 NP_001311061 NP_001311062 NP_001311063 NP_001311064 NP_001311065 NP_065116 NP_573479 Location (UCSC) Chr 10: 109.86 – 109.92 Mb Chr 19: 52.92 – 53.03 Mb PubMed search [3] [4]
Wikidata
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Function

X-prolyl aminopeptidase (EC 3.4.11.9) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-prolyl aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. Deficiency of X-prolyl aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine (Blau et al., 1988).[supplied by OMIM]^[5]