UniProtKB - Q16769 (QPCT_HUMAN)
Protein
Glutaminyl-peptide cyclotransferase
Gene
QPCT
Organism
Homo sapiens (Human)
Status
Functioni
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]-amyloid-beta. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.3 Publications
Caution
It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn2+-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn2+ ions, typically in a 1:1 stoichiometry (PubMed:18072935, PubMed:21288892). However, a recent study suggests a Zn2+-independent catalytic mechanism (By similarity).By similarityCurated2 Publications
Catalytic activityi
- EC:2.3.2.54 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 159 | ZincCombined sources4 Publications | 1 | |
Active sitei | 201 | Proton acceptor1 Publication | 1 | |
Metal bindingi | 202 | ZincCombined sources4 Publications | 1 | |
Active sitei | 248 | Proton acceptor1 Publication | 1 | |
Metal bindingi | 330 | ZincCombined sources4 Publications | 1 |
GO - Molecular functioni
- glutaminyl-peptide cyclotransferase activity Source: UniProtKB
- zinc ion binding Source: UniProtKB
GO - Biological processi
- cellular protein modification process Source: ProtInc
- neutrophil degranulation Source: Reactome
- peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase Source: UniProtKB
Keywordsi
Molecular function | Acyltransferase, Transferase |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | MetaCyc:HS03941-MONOMER |
BRENDAi | 2.3.2.5, 2681 |
PathwayCommonsi | Q16769 |
Reactomei | R-HSA-6798695, Neutrophil degranulation |
Protein family/group databases
MEROPSi | M28.974 |
Names & Taxonomyi
Protein namesi | Recommended name: Glutaminyl-peptide cyclotransferase (EC:2.3.2.5)Alternative name(s): Glutaminyl cyclase Short name: QC Short name: sQC Glutaminyl-tRNA cyclotransferase Glutamyl cyclase Short name: EC |
Gene namesi | Name:QPCT |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:9753, QPCT |
MIMi | 607065, gene |
neXtProti | NX_Q16769 |
VEuPathDBi | HostDB:ENSG00000115828.15 |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
- extracellular region Source: Reactome
Other locations
- ficolin-1-rich granule lumen Source: Reactome
- specific granule lumen Source: Reactome
- tertiary granule lumen Source: Reactome
Keywords - Cellular componenti
SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 144 | K → A: Lowers activity by approximately 40%. 1 Publication | 1 | |
Mutagenesisi | 146 | F → A: Lowers activity by approximately 30%. 1 Publication | 1 | |
Mutagenesisi | 160 | S → A: Reduces activity by about 50%. 1 Publication | 1 | |
Mutagenesisi | 160 | S → G: Reduces activity by 96%. 1 Publication | 1 | |
Mutagenesisi | 201 | E → D: Reduces activity by about 98%. 2 Publications | 1 | |
Mutagenesisi | 201 | E → L or Q: Abolishes activity. 2 Publications | 1 | |
Mutagenesisi | 207 | W → L: Greatly lowers activity. 1 Publication | 1 | |
Mutagenesisi | 248 | D → A: Reduces activity by 99%. 2 Publications | 1 | |
Mutagenesisi | 248 | D → Q: Abolishes activity. 2 Publications | 1 | |
Mutagenesisi | 304 | Q → L: Lowers activity by approximately 35%. 1 Publication | 1 | |
Mutagenesisi | 305 | D → A, E or L: Abolishes activity. 2 Publications | 1 | |
Mutagenesisi | 305 | D → N: Reduces activity by 99%. 2 Publications | 1 | |
Mutagenesisi | 319 | H → L: Reduces activity by 87%. 1 Publication | 1 | |
Mutagenesisi | 325 | F → A: Greatly lowers activity. 1 Publication | 1 | |
Mutagenesisi | 329 | W → A: Abolishes activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 25797 |
OpenTargetsi | ENSG00000115828 |
PharmGKBi | PA34095 |
Miscellaneous databases
Pharosi | Q16769, Tchem |
Chemistry databases
ChEMBLi | CHEMBL4508 |
DrugBanki | DB04581, 1-benzylimidazole DB04636, Glutamine t-butyl ester DB04622, N-acetylhistamine |
GuidetoPHARMACOLOGYi | 2411 |
Genetic variation databases
BioMutai | QPCT |
DMDMi | 2498824 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 28 | Sequence analysisAdd BLAST | 28 | |
ChainiPRO_0000022195 | 29 – 361 | Glutaminyl-peptide cyclotransferaseAdd BLAST | 333 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 49 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 139 ↔ 164 | 1 Publication | ||
Glycosylationi | 296 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
CPTACi | CPTAC-1301 |
jPOSTi | Q16769 |
MassIVEi | Q16769 |
PaxDbi | Q16769 |
PeptideAtlasi | Q16769 |
PRIDEi | Q16769 |
ProteomicsDBi | 61056 [Q16769-1] 61057 [Q16769-2] |
TopDownProteomicsi | Q16769-2 [Q16769-2] |
PTM databases
GlyGeni | Q16769, 2 sites |
iPTMneti | Q16769 |
PhosphoSitePlusi | Q16769 |
Expressioni
Gene expression databases
Bgeei | ENSG00000115828, Expressed in bone marrow and 216 other tissues |
ExpressionAtlasi | Q16769, baseline and differential |
Genevisiblei | Q16769, HS |
Organism-specific databases
HPAi | ENSG00000115828, Tissue enhanced (adrenal gland, blood) |
Interactioni
Binary interactionsi
Q16769
With | #Exp. | IntAct |
---|---|---|
UBQLN2 [Q9UHD9] | 3 | EBI-2856807,EBI-947187 |
Protein-protein interaction databases
BioGRIDi | 117329, 31 interactors |
IntActi | Q16769, 21 interactors |
MINTi | Q16769 |
STRINGi | 9606.ENSP00000344829 |
Chemistry databases
BindingDBi | Q16769 |
Miscellaneous databases
RNActi | Q16769, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q16769 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q16769 |
Family & Domainsi
Sequence similaritiesi
Belongs to the glutaminyl-peptide cyclotransferase family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG3946, Eukaryota |
GeneTreei | ENSGT00390000003107 |
HOGENOMi | CLU_045003_1_0_1 |
InParanoidi | Q16769 |
OMAi | HTFDDNE |
OrthoDBi | 1257754at2759 |
PhylomeDBi | Q16769 |
TreeFami | TF315071 |
Family and domain databases
CDDi | cd03880, M28_QC_like, 1 hit |
InterProi | View protein in InterPro IPR037457, M28_QC IPR007484, Peptidase_M28 IPR040234, QC/QCL |
PANTHERi | PTHR12283, PTHR12283, 1 hit |
Pfami | View protein in Pfam PF04389, Peptidase_M28, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: Q16769-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MAGGRHRRVV GTLHLLLLVA ALPWASRGVS PSASAWPEEK NYHQPAILNS
60 70 80 90 100
SALRQIAEGT SISEMWQNDL QPLLIERYPG SPGSYAARQH IMQRIQRLQA
110 120 130 140 150
DWVLEIDTFL SQTPYGYRSF SNIISTLNPT AKRHLVLACH YDSKYFSHWN
160 170 180 190 200
NRVFVGATDS AVPCAMMLEL ARALDKKLLS LKTVSDSKPD LSLQLIFFDG
210 220 230 240 250
EEAFLHWSPQ DSLYGSRHLA AKMASTPHPP GARGTSQLHG MDLLVLLDLI
260 270 280 290 300
GAPNPTFPNF FPNSARWFER LQAIEHELHE LGLLKDHSLE GRYFQNYSYG
310 320 330 340 350
GVIQDDHIPF LRRGVPVLHL IPSPFPEVWH TMDDNEENLD ESTIDNLNKI
360
LQVFVLEYLH L
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketB5MCZ9 | B5MCZ9_HUMAN | Glutaminyl-peptide cyclotransferase | QPCT | 284 | Annotation score: | ||
C9JS14 | C9JS14_HUMAN | Glutaminyl-peptide cyclotransferase | QPCT | 117 | Annotation score: | ||
A0A3B3IUD5 | A0A3B3IUD5_HUMAN | Glutaminyl-peptide cyclotransferase | QPCT | 137 | Annotation score: |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_053956 | 54 | R → W Lowers activity by approximately 30%. 1 PublicationCorresponds to variant dbSNP:rs2255991Ensembl. | 1 | |
Natural variantiVAR_005569 | 71 | Q → R. Corresponds to variant dbSNP:rs895245310Ensembl. | 1 | |
Natural variantiVAR_053957 | 360 | H → P1 PublicationCorresponds to variant dbSNP:rs4670696Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_038487 | 41 – 89 | Missing in isoform 2. CuratedAdd BLAST | 49 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X71125 mRNA Translation: CAA50438.1 X67731 mRNA Translation: CAA47961.1 AK290605 mRNA Translation: BAF83294.1 AC007391 Genomic DNA Translation: AAY14804.1 CH471053 Genomic DNA Translation: EAX00392.1 CH471053 Genomic DNA Translation: EAX00394.1 CH471053 Genomic DNA Translation: EAX00396.1 BC036721 mRNA Translation: AAH36721.1 BC047756 mRNA Translation: AAH47756.1 |
CCDSi | CCDS1790.1 [Q16769-1] |
PIRi | I37421 |
RefSeqi | NP_036545.1, NM_012413.3 [Q16769-1] |
Genome annotation databases
Ensembli | ENST00000338415; ENSP00000344829; ENSG00000115828 [Q16769-1] |
GeneIDi | 25797 |
KEGGi | hsa:25797 |
UCSCi | uc002rqg.4, human [Q16769-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X71125 mRNA Translation: CAA50438.1 X67731 mRNA Translation: CAA47961.1 AK290605 mRNA Translation: BAF83294.1 AC007391 Genomic DNA Translation: AAY14804.1 CH471053 Genomic DNA Translation: EAX00392.1 CH471053 Genomic DNA Translation: EAX00394.1 CH471053 Genomic DNA Translation: EAX00396.1 BC036721 mRNA Translation: AAH36721.1 BC047756 mRNA Translation: AAH47756.1 |
CCDSi | CCDS1790.1 [Q16769-1] |
PIRi | I37421 |
RefSeqi | NP_036545.1, NM_012413.3 [Q16769-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1MOI | model | - | A | 1-361 | [»] | |
2AFM | X-ray | 1.66 | A/B | 33-361 | [»] | |
2AFO | X-ray | 2.35 | A/B | 33-361 | [»] | |
2AFS | X-ray | 2.22 | A/B | 33-361 | [»] | |
2AFU | X-ray | 2.22 | A/B | 33-361 | [»] | |
2AFW | X-ray | 1.56 | A/B | 33-361 | [»] | |
2AFX | X-ray | 1.64 | A/B | 33-361 | [»] | |
2AFZ | X-ray | 1.68 | A/B | 33-361 | [»] | |
2ZED | X-ray | 1.70 | A/B | 33-361 | [»] | |
2ZEE | X-ray | 1.99 | A/B | 33-361 | [»] | |
2ZEF | X-ray | 1.67 | A/B | 33-361 | [»] | |
2ZEG | X-ray | 2.08 | A/B | 33-361 | [»] | |
2ZEH | X-ray | 1.80 | A/B | 33-361 | [»] | |
2ZEL | X-ray | 1.97 | A/B | 33-361 | [»] | |
2ZEM | X-ray | 2.18 | A/B | 33-361 | [»] | |
2ZEN | X-ray | 1.78 | A/B | 33-361 | [»] | |
2ZEO | X-ray | 1.66 | A/B | 33-361 | [»] | |
2ZEP | X-ray | 2.10 | A/B | 33-361 | [»] | |
3PBB | X-ray | 1.95 | A/B | 33-361 | [»] | |
3PBE | X-ray | 1.95 | A/B | 33-361 | [»] | |
3SI0 | X-ray | 2.10 | A | 38-361 | [»] | |
4YU9 | X-ray | 2.10 | A/B/C | 33-361 | [»] | |
4YWY | X-ray | 1.95 | A/B/C | 1-361 | [»] | |
6GBX | X-ray | 1.72 | A/B/C | 33-361 | [»] | |
6YI1 | X-ray | 1.92 | A/B | 35-361 | [»] | |
6YJY | X-ray | 1.67 | A/B | 35-361 | [»] | |
7COZ | X-ray | 1.85 | A/B/C | 35-361 | [»] | |
7CP0 | X-ray | 1.70 | A/B/C | 35-361 | [»] | |
SMRi | Q16769 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 117329, 31 interactors |
IntActi | Q16769, 21 interactors |
MINTi | Q16769 |
STRINGi | 9606.ENSP00000344829 |
Chemistry databases
BindingDBi | Q16769 |
ChEMBLi | CHEMBL4508 |
DrugBanki | DB04581, 1-benzylimidazole DB04636, Glutamine t-butyl ester DB04622, N-acetylhistamine |
GuidetoPHARMACOLOGYi | 2411 |
Protein family/group databases
MEROPSi | M28.974 |
PTM databases
GlyGeni | Q16769, 2 sites |
iPTMneti | Q16769 |
PhosphoSitePlusi | Q16769 |
Genetic variation databases
BioMutai | QPCT |
DMDMi | 2498824 |
Proteomic databases
CPTACi | CPTAC-1301 |
jPOSTi | Q16769 |
MassIVEi | Q16769 |
PaxDbi | Q16769 |
PeptideAtlasi | Q16769 |
PRIDEi | Q16769 |
ProteomicsDBi | 61056 [Q16769-1] 61057 [Q16769-2] |
TopDownProteomicsi | Q16769-2 [Q16769-2] |
Protocols and materials databases
Antibodypediai | 1981, 219 antibodies |
DNASUi | 25797 |
Genome annotation databases
Ensembli | ENST00000338415; ENSP00000344829; ENSG00000115828 [Q16769-1] |
GeneIDi | 25797 |
KEGGi | hsa:25797 |
UCSCi | uc002rqg.4, human [Q16769-1] |
Organism-specific databases
CTDi | 25797 |
DisGeNETi | 25797 |
GeneCardsi | QPCT |
HGNCi | HGNC:9753, QPCT |
HPAi | ENSG00000115828, Tissue enhanced (adrenal gland, blood) |
MIMi | 607065, gene |
neXtProti | NX_Q16769 |
OpenTargetsi | ENSG00000115828 |
PharmGKBi | PA34095 |
VEuPathDBi | HostDB:ENSG00000115828.15 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3946, Eukaryota |
GeneTreei | ENSGT00390000003107 |
HOGENOMi | CLU_045003_1_0_1 |
InParanoidi | Q16769 |
OMAi | HTFDDNE |
OrthoDBi | 1257754at2759 |
PhylomeDBi | Q16769 |
TreeFami | TF315071 |
Enzyme and pathway databases
BioCyci | MetaCyc:HS03941-MONOMER |
BRENDAi | 2.3.2.5, 2681 |
PathwayCommonsi | Q16769 |
Reactomei | R-HSA-6798695, Neutrophil degranulation |
Miscellaneous databases
BioGRID-ORCSi | 25797, 7 hits in 987 CRISPR screens |
ChiTaRSi | QPCT, human |
EvolutionaryTracei | Q16769 |
GeneWikii | QPCT |
GenomeRNAii | 25797 |
Pharosi | Q16769, Tchem |
PROi | PR:Q16769 |
RNActi | Q16769, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000115828, Expressed in bone marrow and 216 other tissues |
ExpressionAtlasi | Q16769, baseline and differential |
Genevisiblei | Q16769, HS |
Family and domain databases
CDDi | cd03880, M28_QC_like, 1 hit |
InterProi | View protein in InterPro IPR037457, M28_QC IPR007484, Peptidase_M28 IPR040234, QC/QCL |
PANTHERi | PTHR12283, PTHR12283, 1 hit |
Pfami | View protein in Pfam PF04389, Peptidase_M28, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | QPCT_HUMAN | |
Accessioni | Q16769Primary (citable) accession number: Q16769 Secondary accession number(s): Q16770, Q3KRG6, Q53TR4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | November 1, 1997 | |
Last modified: | April 7, 2021 | |
This is version 169 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - 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