You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP00692
Secondary Accession Numbers
  • 5965
Name Glutaminyl-peptide cyclotransferase
Synonyms
  1. EC
  2. Glutaminyl cyclase
  3. Glutaminyl-tRNA cyclotransferase
  4. Glutamyl cyclase
  5. QC
  6. sQC
Gene Name QPCT
Protein Type Unknown
Biological Properties
General Function Involved in peptidase activity
Specific Function Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.
Pathways Not Available
Reactions
L-glutaminyl-peptide → 5-oxoprolyl-peptide + Ammonia details
GO Classification
Biological Process
proteolysis
peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
Cellular Component
extracellular region
Function
catalytic activity
hydrolase activity
peptidase activity
Molecular Function
metal ion binding
peptidase activity
zinc ion binding
glutaminyl-peptide cyclotransferase activity
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Cellular Location
  1. Cytoplasmic
Gene Properties
Chromosome Location 2
Locus 2p22.2
SNPs QPCT
Gene Sequence
>1086 bp
ATGGCAGGCGGAAGACACCGGCGCGTCGTGGGCACCCTCCACCTGCTGCTGCTGGTGGCC
GCCCTGCCCTGGGCATCCAGGGGGGTCAGTCCGAGTGCCTCAGCCTGGCCAGAGGAGAAG
AATTACCACCAGCCAGCCATTTTGAATTCATCGGCTCTTCGGCAAATTGCAGAAGGCACC
AGTATCTCTGAAATGTGGCAAAATGACTTACAGCCATTGCTGATAGAGCGATACCCGGGA
TCCCCTGGAAGCTATGCTGCTCGTCAGCACATCATGCAGCGAATTCAGAGGCTTCAGGCT
GACTGGGTCTTGGAAATAGACACCTTCTTGAGTCAGACACCCTATGGGTACCGGTCTTTC
TCAAATATCATCAGCACCCTCAATCCCACTGCTAAACGACATTTGGTCCTCGCCTGCCAC
TATGACTCCAAGTATTTTTCCCACTGGAACAACAGAGTGTTTGTAGGAGCCACTGATTCA
GCCGTGCCATGTGCAATGATGTTGGAACTTGCTCGTGCCTTAGACAAGAAACTCCTTTCC
TTAAAGACTGTTTCAGACTCCAAGCCAGATTTGTCACTCCAGCTGATCTTCTTTGATGGT
GAAGAGGCTTTTCTTCACTGGTCTCCTCAAGATTCTCTCTATGGGTCTCGACACTTAGCT
GCAAAGATGGCATCGACCCCGCACCCACCTGGAGCGAGAGGCACCAGCCAACTGCATGGC
ATGGATTTATTGGTCTTATTGGATTTGATTGGAGCTCCAAACCCAACGTTTCCCAATTTT
TTTCCAAACTCAGCCAGGTGGTTCGAAAGACTTCAAGCAATTGAACATGAACTTCATGAA
TTGGGTTTGCTCAAGGATCACTCTTTGGAGGGGCGGTATTTCCAGAATTACAGTTATGGA
GGTGTGATTCAGGATGACCATATTCCATTTTTAAGAAGAGGTGTTCCAGTTCTGCATCTG
ATACCGTCTCCTTTCCCTGAAGTCTGGCACACCATGGATGACAATGAAGAAAATTTGGAT
GAATCAACCATTGACAATCTAAACAAAATCCTACAAGTCTTTGTGTTGGAATATCTTCAT
TTGTAA
Protein Properties
Number of Residues 361
Molecular Weight 40876.14
Theoretical pI 6.612
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Glutaminyl-peptide cyclotransferase
MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGT
SISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSF
SNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLS
LKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHG
MDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYG
GVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLH
L
GenBank ID Protein 296949
UniProtKB/Swiss-Prot ID Q16769
UniProtKB/Swiss-Prot Entry Name QPCT_HUMAN
PDB IDs
GenBank Gene ID X71125
GeneCard ID QPCT
GenAtlas ID QPCT
HGNC ID HGNC:9753
References
General References
  1. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed:15815621 ]
  2. 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 ]
  3. Song I, Chuang CZ, Bateman RC Jr: Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase. J Mol Endocrinol. 1994 Aug;13(1):77-86. [PubMed:7999256 ]
  4. Schilling S, Hoffmann T, Manhart S, Hoffmann M, Demuth HU: Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions. FEBS Lett. 2004 Apr 9;563(1-3):191-6. [PubMed:15063747 ]
  5. Huang KF, Liu YL, Cheng WJ, Ko TP, Wang AH: Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13117-22. Epub 2005 Aug 31. [PubMed:16135565 ]