QPCT

Glutaminyl-peptide cyclotransferase is an enzyme that in humans is encoded by the QPCT gene.[5][6]

QPCT
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2ZEE, 2ZEF, 2AFU, 2AFM, 2AFX, 4YU9, 2ZEL, 2ZEG, 2ZEM, 4YWY, 2AFZ, 3PBB, 2ZEH, 2AFS, 3SI0, 2ZEP, 3PBE, 2ZEO, 2ZED, 2AFO, 2ZEN, 2AFW
Identifiers
Aliases	QPCT, GCT, QC, sQC, glutaminyl-peptide cyclotransferase
External IDs	OMIM: 607065 MGI: 1917786 HomoloGene: 8238 GeneCards: QPCT
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p22.2 Start 37,342,827 bp[1] End 37,373,322 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 E3 Start 79,051,906 bp[2] End 79,090,378 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • zinc ion binding • glutaminyl-peptide cyclotransferase activity • transferase activity, transferring acyl groups • metal ion binding Cellular component • extracellular exosome • extracellular region • specific granule lumen • tertiary granule lumen • ficolin-1-rich granule lumen Biological process • peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase • cellular protein modification process • neutrophil degranulation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	25797	70536
Ensembl	ENSG00000115828	ENSMUSG00000024084
UniProt	Q16769	Q9CYK2
RefSeq (mRNA)	NM_012413	NM_027455 NM_001316729
RefSeq (protein)	NP_036545	NP_001303658 NP_081731
Location (UCSC)	Chr 2: 37.34 – 37.37 Mb	Chr 17: 79.05 – 79.09 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes human pituitary glutaminyl cyclase, which is responsible for the presence of pyroglutamyl residues in many neuroendocrine peptides. The amino acid sequence of this enzyme is 86% identical to that of bovine glutaminyl cyclase.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000115828 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024084 - 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. Song I, Chuang CZ, Bateman RC Jr (Jan 1995). "Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase". J Mol Endocrinol. 13 (1): 77–86. doi:10.1677/jme.0.0130077. PMID 7999256.
6. "Entrez Gene: QPCT glutaminyl-peptide cyclotransferase (glutaminyl cyclase)".

Further reading

• Busby WH, Quackenbush GE, Humm J, et al. (1987). "An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes". J. Biol. Chem. 262 (18): 8532–6. PMID 3597387.
• Bateman RC, Temple JS, Misquitta SA, Booth RE (2001). "Evidence for essential histidines in human pituitary glutaminyl cyclase". Biochemistry. 40 (37): 11246–50. doi:10.1021/bi011177o. PMID 11551224.
• Schilling S, Hoffmann T, Rosche F, et al. (2002). "Heterologous expression and characterization of human glutaminyl cyclase: evidence for a disulfide bond with importance for catalytic activity". Biochemistry. 41 (35): 10849–57. doi:10.1021/bi0260381. PMID 12196024.
• 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.
• Schilling S, Niestroj AJ, Rahfeld JU, et al. (2004). "Identification of human glutaminyl cyclase as a metalloenzyme. Potent inhibition by imidazole derivatives and heterocyclic chelators". J. Biol. Chem. 278 (50): 49773–9. doi:10.1074/jbc.M309077200. PMID 14522962.
• Booth RE, Misquitta SA, Bateman RC (2004). "Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification". Protein Expr. Purif. 32 (1): 141–6. doi:10.1016/S1046-5928(03)00226-2. PMID 14680951.
• Ezura Y, Kajita M, Ishida R, et al. (2005). "Association of multiple nucleotide variations in the pituitary glutaminyl cyclase gene (QPCT) with low radial BMD in adult women". J. Bone Miner. Res. 19 (8): 1296–301. doi:10.1359/JBMR.040324. PMID 15231017.
• 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.
• Huang KF, Liu YL, Cheng WJ, et al. (2005). "Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation". Proc. Natl. Acad. Sci. U.S.A. 102 (37): 13117–22. doi:10.1073/pnas.0504184102. PMC 1201592. PMID 16135565.
• Huang QY, Kung AW (2007). "The association of common polymorphisms in the QPCT gene with bone mineral density in the Chinese population". Journal of Human Genetics. 52 (9): 757–62. doi:10.1007/s10038-007-0178-6. PMID 17687619.