QPCT

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 79,359,335 bp [2] End 79,397,807 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left adrenal gland blood bone marrow cells monocyte spongy bone corpus epididymis periodontal fiber human penis vulva pituitary gland Top expressed in spermatocyte lens iris arcuate nucleus paraventricular nucleus of hypothalamus spermatid seminiferous tubule median eminence aortic valve dorsomedial hypothalamic nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity zinc ion binding glutaminyl-peptide cyclotransferase activity acyltransferase activity 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 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: 79.36 – 79.4 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. doi: 10.1016/S0021-9258(18)47446-7 . 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. Bibcode:2002PNAS...9916899M. 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. S2CID   8470506.
• 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. Bibcode:2005PNAS..10213117H. 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.