XPNPEP1

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
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 stromal cell of endometrium duodenum monocyte rectum skin of abdomen tibia gastric mucosa gallbladder Top expressed in jejunum ileum internal carotid artery yolk sac external carotid artery stria vascularis spermatid duodenum Paneth cell kidney 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
View/Edit Human View/Edit Mouse

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

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]

References

1. GRCh38: Ensembl release 89: ENSG00000108039 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025027 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: XPNPEP1 X-prolyl aminopeptidase (aminopeptidase P) 1, soluble".

Further reading

• Vanhoof G, De Meester I, Goossens F, Hendriks D, Scharpé S, Yaron A (Aug 1992). "Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P". Biochemical Pharmacology. 44 (3): 479–87. doi:10.1016/0006-2952(92)90439-P. PMID   1510698.
• Blau N, Niederwieser A, Shmerling DH (1988). "Peptiduria presumably caused by aminopeptidase-P deficiency. A new inborn error of metabolism". Journal of Inherited Metabolic Disease. 11 Suppl 2: 240–2. doi:10.1007/BF01804246. PMID   3141711. S2CID   32596444.
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Vanhoof G, Goossens F, Juliano MA, Juliano L, Hendriks D, Schatteman K, Lin AH, Scharpé S (1998). "Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)". Cytogenetics and Cell Genetics. 78 (3–4): 275–80. doi:10.1159/000134671. PMID   9465902.
• Sprinkle TJ, Caldwell C, Ryan JW (Jun 2000). "Cloning, chromosomal sublocalization of the human soluble aminopeptidase P gene (XPNPEP1) to 10q25.3 and conservation of the putative proton shuttle and metal ligand binding sites with XPNPEP2". Archives of Biochemistry and Biophysics. 378 (1): 51–6. doi:10.1006/abbi.2000.1792. PMID   10871044.
• Cottrell GS, Hooper NM, Turner AJ (Dec 2000). "Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme". Biochemistry. 39 (49): 15121–8. doi:10.1021/bi001585c. PMID   11106490.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID   12665801. S2CID   23783563.