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Identification
HMDB Protein ID HMDBP08856
Secondary Accession Numbers
  • 14583
Name Xaa-Pro aminopeptidase 1
Synonyms
  1. Aminoacylproline aminopeptidase
  2. Cytosolic aminopeptidase P
  3. Soluble aminopeptidase P
  4. X-Pro aminopeptidase 1
  5. X-prolyl aminopeptidase 1, soluble
  6. sAmp
Gene Name XPNPEP1
Protein Type Unknown
Biological Properties
General Function Involved in hydrolase activity
Specific Function Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro
Pathways Not Available
Reactions Not Available
GO Classification
Function
metalloexopeptidase activity
catalytic activity
hydrolase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
metallopeptidase activity
Process
metabolic process
macromolecule metabolic process
cellular process
protein metabolic process
proteolysis
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location Chromosome:1
Locus 10q25.3
SNPs XPNPEP1
Gene Sequence
>1872 bp
ATGCCTCCAAAGGTGACTTCAGAGCTGCTTCGGCAGCTGAGACAAGCCATGAGGAACTCT
GAGTATGTGACCGAACCGATCCAGGCCTACATCATCCCATCGGGAGATGCTCATCAGAGT
GAGTATATTGCTCCATGTGACTGTCGGCGGGCTTTTGTCTCTGGATTCGATGGCTCTGCG
GGCACAGCCATCATCACAGAAGAGCATGCAGCCATGTGGACTGACGGGCGCTACTTTCTC
CAGGCTGCCAAGCAAATGGACAGCAACTGGACACTTATGAAGATGGGTCTGAAGGACACA
CCAACTCAGGAAGACTGGCTGGTGAGTGTGCTTCCTGAAGGATCCAGGGTTGGTGTGGAC
CCCTTGATCATTCCTACAGATTATTGGAAGAAAATGGCCAAAGTTCTGAGAAGTGCCGGC
CATCACCTCATTCCTGTCAAGGAGAACCTCGTTGACAAAATCTGGACAGACCGTCCTGAG
CGCCCTTGCAAGCCTCTCCTCACACTGGGCCTGGATTACACAGGCATCTCCTGGAAGGAC
AAGGTTGCAGACCTTCGGTTGAAAATGGCTGAGAGGAACGTCATGTGGTTTGTGGTCACT
GCCTTGGATGAGATTGCGTGGCTATTTAATCTCCGAGGATCAGATGTGGAGCACAATCCA
GTATTTTTCTCCTACGCAATCATAGGACTAGAGACGATCATGCTCTTCATTGATGGTGAC
CGCATAGACGCCCCCAGTGTGAAGGAGCACCTGCTTCTTGACTTGGGTCTGGAAGCCGAA
TACAGGATCCAGGTGCATCCCTACAAGTCCATCCTGAGCGAGCTCAAGGCCCTGTGTGCT
GACCTCTCCCCAAGGGAGAAGGTGTGGGTCAGTGACAAGGCCAGCTATGCTGTGAGCGAG
ACCATCCCCAAGGACCACCGCTGCTGTATGCCTTACACCCCCATCTGCATCGCCAAAGCT
GTGAAGAATTCAGCTGAGTCAGAAGGCATGAGGCCGGCTCACATTAAAGATGCTGTTGCT
CTCTGTGAACTCTTTAACTGGCTGGAGAAAGAGGTTCCCAAAGGTGGTGTGACAGAGATC
TCAGCTGCTGACAAAGCTGAGGAGTTTCGCAGGCAACAGGCAGACTTTGTGGACCTGAGC
TTCCCAACAATTTCCAGTACGGGACCCAACGGCGCCATCATTCACTACGCGCCAGTCCCT
GAGACGAATAGGACCTTGTCCCTGGATGAGGTGTACCTTATTGACTCGGGTGCTCAATAC
AAGGATGGCACCACAGATGTGACGCGGACAATGCATTTTGGGACCCCTACAGCCTACGAG
AAGGAATGCTTCACATATGTCCTCAAGGGCCACATAGCTGTGAGTGCAGCCGTTTTCCCG
ACTGGAACCAAAGGTCACCTTCTTGACTCCTTTGCCCGTTCAGCTTTATGGGATTCAGGC
CTAGATTACTTGCACGGGACTGGACATGGTGTTGGGTCTTTTTTGAATGTCCATGAGGGT
CCTTGCGGCATCAGTTACAAAACATTCTCTGATGAGCCCTTGGAGGCAGGCATGATTGTC
ACTGATGAGCCCGGGTACTATGAAGATGGGGCTTTTGGAATTCGCATTGAGAATGTTGTC
CTTGTGGTTCCTGTGAAGACCAAGTATAATTTTAATAACCGGGGAAGCCTGACCTTTGAA
CCTCTAACATTGGTTCCAATTCAGACCAAAATGATAGATGTGGATTCTCTTACAGACAAA
GAGTGCGACTGGCTCAACAATTACCACCTGACCTGCAGGGATGTGATTGGGAAGGAATTG
CAGAAACAGGGCCGCCAGGAAGCTCTCGAGTGGCTCATCAGAGAGACGCAACCCATCTCC
AAACAGCATTAA
Protein Properties
Number of Residues 623
Molecular Weight 69917.2
Theoretical pI 5.41
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Xaa-Pro aminopeptidase 1
MPPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSA
GTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVD
PLIIPTDYWKKMAKVLRSAGHHLIPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKD
KVADLRLKMAERNVMWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGD
RIDAPSVKEHLLLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSE
TIPKDHRCCMPYTPICIAKAVKNSAESEGMRRAHIKDAVALCELFNWLEKEVPKGGVTEI
SAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPVPETNRTLSLDEVYLIDSGAQY
KDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSG
LDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVV
LVVPVKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDSLTDKECDWLNNYHLTCRDVIGKEL
QKQGRQEALEWLIRETQPISKQH
GenBank ID Protein 9739017
UniProtKB/Swiss-Prot ID Q9NQW7
UniProtKB/Swiss-Prot Entry Name XPP1_HUMAN
PDB IDs Not Available
GenBank Gene ID AF195530
GeneCard ID XPNPEP1
GenAtlas ID XPNPEP1
HGNC ID HGNC:12822
References
General References
  1. 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. [PubMed:15489334 ]
  2. 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. [PubMed:19608861 ]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed:15164054 ]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
  6. Vanhoof G, Goossens F, Juliano MA, Juliano L, Hendriks D, Schatteman K, Lin AH, Scharpe S: Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P). Cytogenet Cell Genet. 1997;78(3-4):275-80. [PubMed:9465902 ]
  7. Sprinkle TJ, Caldwell C, Ryan JW: 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. 2000 Jun 1;378(1):51-6. [PubMed:10871044 ]
  8. Cottrell GS, Hooper NM, Turner AJ: Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme. Biochemistry. 2000 Dec 12;39(49):15121-8. [PubMed:11106490 ]
  9. Li X, Lou Z, Li X, Zhou W, Ma M, Cao Y, Geng Y, Bartlam M, Zhang XC, Rao Z: Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit. J Biol Chem. 2008 Aug 15;283(33):22858-66. doi: 10.1074/jbc.M710274200. Epub 2008 May 30. [PubMed:18515364 ]