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Reviewed, UniProtKB/Swiss-Prot Q16769 (QPCT_HUMAN)

Last modified November 3, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glutaminyl-peptide cyclotransferase
    EC=2.3.2.5
Alternative name(s):
    Glutaminyl-tRNA cyclotransferase
      Short name=Glutaminyl cyclase
    QC
    Glutamyl cyclase
    EC
Gene names
Name: QPCT
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

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. Ref.3

Catalytic activity

L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3. Ref.4

Cofactor

Binds 1 zinc ion per subunit.

Sequence similarities

Belongs to the glutaminyl-peptide cyclotransferase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 361333Glutaminyl-peptide cyclotransferase
PRO_0000022195

Sites

Active site2011Proton acceptor Probable
Metal binding1591Zinc
Metal binding2021Zinc
Metal binding3301Zinc

Amino acid modifications

Glycosylation491N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential

Natural variations

Natural variant541R → W: dbSNP rs2255991.
VAR_053956
Natural variant711Q → R
VAR_005569
Natural variant3601H → P: dbSNP rs4670696. Ref.2
VAR_053957

Experimental info

Mutagenesis541R → W: Lowers activity by approximately 30%. Ref.4
Mutagenesis1441K → A: Lowers activity by approximately 40%. Ref.4
Mutagenesis1461F → A: Lowers activity by approximately 30%. Ref.4
Mutagenesis2011E → D or Q: Abolishes activity. Ref.4
Mutagenesis2071W → L: Greatly lowers activity. Ref.4
Mutagenesis2481D → A: Abolishes activity. Ref.4
Mutagenesis3041Q → L: Lowers activity by approximately 35%. Ref.4
Mutagenesis3051D → L: Abolishes activity. Ref.4
Mutagenesis3251F → A: Greatly lowers activity. Ref.4
Mutagenesis3291W → A: Abolishes activity. Ref.4

Secondary structure

1 ........................................................ 361
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q16769-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 32C26041BCF5ED75

FASTA36140,877
        10         20         30         40         50         60 
MAGGRHRRVV GTLHLLLLVA ALPWASRGVS PSASAWPEEK NYHQPAILNS SALRQIAEGT 

        70         80         90        100        110        120 
SISEMWQNDL QPLLIERYPG SPGSYAARQH IMQRIQRLQA DWVLEIDTFL SQTPYGYRSF 

       130        140        150        160        170        180 
SNIISTLNPT AKRHLVLACH YDSKYFSHWN NRVFVGATDS AVPCAMMLEL ARALDKKLLS 

       190        200        210        220        230        240 
LKTVSDSKPD LSLQLIFFDG EEAFLHWSPQ DSLYGSRHLA AKMASTPHPP GARGTSQLHG 

       250        260        270        280        290        300 
MDLLVLLDLI GAPNPTFPNF FPNSARWFER LQAIEHELHE LGLLKDHSLE GRYFQNYSYG 

       310        320        330        340        350        360 
GVIQDDHIPF LRRGVPVLHL IPSPFPEVWH TMDDNEENLD ESTIDNLNKI LQVFVLEYLH 


L

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase."
Song I., Chuang C.Z., Bateman R.C. Jr.
J. Mol. Endocrinol. 13:77-86(1994) [PubMed: 7999256] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pituitary.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-360.
Tissue: Lung and Pancreas.
[3]"Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions."
Schilling S., Hoffmann T., Manhart S., Hoffmann M., Demuth H.U.
FEBS Lett. 563:191-196(2004) [PubMed: 15063747] [Abstract]
Cited for: FUNCTION AS GLUTAMYL CYCLASE.
[4]"Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation."
Huang K.-F., Liu Y.-L., Cheng W.-J., Ko T.-P., Wang A.H.-J.
Proc. Natl. Acad. Sci. U.S.A. 102:13117-13122(2005) [PubMed: 16135565] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 33-361, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-54; LYS-144; PHE-146; GLU-201; TRP-207; ASP-248; GLN-304; ASP-305; PHE-325 AND TRP-329.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X71125 mRNA. Translation: CAA50438.1.
X67731 mRNA. Translation: CAA47961.1.
BC036721 mRNA. Translation: AAH36721.1.
BC047756 mRNA. Translation: AAH47756.1.
IPIIPI00003919.
PIRI37421.
RefSeqNP_036545.1.
UniGeneHs.79033

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MOImodel-A1-361[»]
2AFMX-ray1.66A/B33-361[»]
2AFOX-ray2.35A/B33-361[»]
2AFSX-ray2.22A/B33-361[»]
2AFUX-ray2.22A/B33-361[»]
2AFWX-ray1.56A/B33-361[»]
2AFXX-ray1.64A/B33-361[»]
2AFZX-ray1.68A/B33-361[»]
2ZEDX-ray1.70A/B33-361[»]
2ZEEX-ray1.99A/B33-361[»]
2ZEFX-ray1.67A/B33-361[»]
2ZEGX-ray2.08A/B33-361[»]
2ZEHX-ray1.80A/B33-361[»]
2ZELX-ray1.97A/B33-361[»]
2ZEMX-ray2.18A/B33-361[»]
2ZENX-ray1.78A/B33-361[»]
2ZEOX-ray1.66A/B33-361[»]
2ZEPX-ray2.10A/B33-361[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ16769.

Protein family/group databases

MEROPSM28.974.

Proteomic databases

PeptideAtlasQ16769.
PRIDEQ16769.

Genome annotation databases

EnsemblENST00000338415; ENSP00000344829; ENSG00000115828; Homo sapiens. [Genome view]
ENST00000404976; ENSP00000385391; ENSG00000115828; Homo sapiens. [Genome view]
ENST00000427681; ENSP00000405728; ENSG00000115828; Homo sapiens. [Genome view]
ENST00000444022; ENSP00000389227; ENSG00000115828; Homo sapiens. [Genome view]
GeneID25797.
KEGGhsa:25797.
UCSCuc002rqg.1. human.

Organism-specific databases

CTD25797.
GeneCardsGC02P037483.
H-InvDBHIX0023907.
HGNCHGNC:9753. QPCT.
HPAHPA008406.
MIM607065. gene.
PharmGKBPA34095.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ16769.
HOVERGENQ16769.
OMAEMWQNDL.

Enzyme and pathway databases

BRENDA2.3.2.5. 247.

Gene expression databases

ArrayExpressQ16769.
BgeeQ16769.
CleanExHS_QPCT.
GenevestigatorQ16769.
GermOnlineENSG00000115828. Homo sapiens.

Family and domain databases

InterProIPR007484. Peptidase_M28.
[Graphical view]
PfamPF04389. Peptidase_M28. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio46985.
SOURCESearch...

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Entry information

Entry nameQPCT_HUMAN
AccessionPrimary (citable) accession number: Q16769
Secondary accession number(s): Q16770, Q3KRG6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 3, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Relevant documents

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Human chromosome 2: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents