XPNPEP1

X-prolyl aminopeptidase (aminopeptidase P) 1, soluble
Identifiers
Symbols	XPNPEP1; APP1; SAMP; XPNPEP; XPNPEPL; XPNPEPL1
External IDs	OMIM: 602443 MGI: 2180003 HomoloGene: 6424 GeneCards: XPNPEP1 Gene
EC number	3.4.11.9
Gene Ontology Molecular function • aminopeptidase activity • peptidase activity • manganese ion binding • protein homodimerization activity • metal ion binding • metalloaminopeptidase activity Cellular component • cytoplasm • cytosol Biological process • proteolysis • cellular process • bradykinin catabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7511	170750
Ensembl	ENSG00000108039	ENSMUSG00000025027
UniProt	Q9NQW7	Q3TL27
RefSeq (mRNA)	NM_001167604.1	NM_133216.2
RefSeq (protein)	NP_001161076.1	NP_573479.2
Location (UCSC)	Chr 10: 111.62 – 111.68 Mb	Chr 19: 53.02 – 53.11 Mb
PubMed search	[1]	[2]

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

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]

Further reading

• Vanhoof G, De Meester I, Goossens F, et al. (1992). "Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P.". Biochem. Pharmacol. 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.". J. Inherit. Metab. Dis. 11 Suppl 2: 240–2. doi:10.1007/BF01804246. PMID 3141711. 
• Maruyama K, Sugano S (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, et al. (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, et al. (1998). "Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)". Cytogenet. Cell Genet. 78 (3–4): 275–80. doi:10.1159/000134671. PMID 9465902. 
• Sprinkle TJ, Caldwell C, Ryan JW (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". Arch. Biochem. Biophys. 378 (1): 51–6. doi:10.1006/abbi.2000.1792. PMID 10871044. 
• Cottrell GS, Hooper NM, Turner AJ (2001). "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. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10". Nature 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.