QPCT

QPCT

Identifiers

QPCT, GCT, QC, sQC, glutaminyl-peptide cyclotransferase

External IDs

OMIM: 607065; MGI: 1917786; GeneCards: QPCT

Available structures

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

Enzyme activity
EC #	BRENDA	ExPASy	KEGG	MetaCyc
2.3.2.5	↗	↗	↗	↗

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2p22.2	Start	37,342,827 bp^[1]
Band	2p22.2	End	37,373,322 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17\|17 E3	Start	79,359,335 bp^[2]
Band	17\|17 E3	End	79,397,807 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

right adrenal cortex

beta cell

left adrenal gland

left adrenal cortex

blood

bone marrow cell

monocyte

skin of arm

trabecular bone

corpus epididymis

Top expressed in

spermatocyte

lens

lumbar subsegment of spinal cord

iris

neural layer of retina

arcuate nucleus

paraventricular nucleus of hypothalamus

spermatid

seminiferous tubule

median eminence

More reference expression data


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

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


25797


70536


ENSG00000115828


ENSMUSG00000024084


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]

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000115828 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000024084 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "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.

PDB gallery

2afm: Crystal structure of human glutaminyl cyclase at pH 6.5
2afo: Crystal structure of human glutaminyl cyclase at pH 8.0
2afs: Crystal structure of the genetic mutant R54W of human glutaminyl cyclase
2afu: Crystal structure of human glutaminyl cyclase in complex with glutamine t-butyl ester
2afw: Crystal structure of human glutaminyl cyclase in complex with N-acetylhistamine
2afx: Crystal structure of human glutaminyl cyclase in complex with 1-benzylimidazole
2afz: Crystal structure of human glutaminyl cyclase in complex with 1-vinylimidazole

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