Search by BoMiProt ID - Bomi387


Primary Information

BoMiProt ID Bomi387
Protein Name Xaa-Pro aminopeptidase 1
Organism Bos taurus
Uniprot IDQ1JPJ2
Milk FractionExosome
Ref Sequence ID NP_001069070.1
Aminoacid Length 623
Molecular Weight 69790
FASTA Sequence Download
Gene Name XPNPEP1
Gene ID 513156
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Protein Function metallopeptidases;enzyme cleaves Tyr-Ser, Ser-Pro and Pro-Pro bond and not Pro-Ala bond of the peptide substrates; human aminopeptidase XPNPEP3 is associated with cystic-kidney disease and TNF-TNFR2 cellular signaling; act as an adaptor molecule in TNF-TNFR2 signaling pathway; regulate phosphorylation of JNK kinases and exert anti-apoptotic functions;
Biochemical Properties has two isoforms resulting from alternative splicing, one located in mitochondrial matrix (XPNPEP3) and the other in cytosol (XPNPEP3c); The active site with a binuclear metal centre is located in an oval depression at the centre of C-domain; presence of two manganese ions in the active site; apstatin is an active site inhibitor; XPNPEP3 and Intermediate cleavage peptide 55 exist as dimer; Both N- and C-domains from each subunit are involved in dimerization employing both electrostatic and van der Waals contacts
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography 1. Singh, R. et al. (2017) ‘Structure of the human aminopeptidase XPNPEP3 and comparison of its in vitro activity with Icp55 orthologs: Insights into diverse cellular processes’, Journal of Biological Chemistry, 292(24), pp. 10035–10047. doi: 10.1074/jbc.M117.783357.
2. Inoue, M. et al. (2015) ‘Aminopeptidase P3, a new member of the TNF-TNFR2 signaling complex, induces phosphorylation of JNK1 and JNK2.’, Journal of cell science, 128(4), pp. 656–69. doi: 10.1242/jcs.149385.
3. Erşahin, Ç. et al. (2005) ‘Aminopeptidase P isozyme expression in human tissues and peripheral blood mononuclear cell fractions’, Archives of Biochemistry and Biophysics, 435(2), pp. 303–310. doi: 10.1016/j.abb.2004.12.023.