Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutaminyl-peptide cyclotransferase

Gene

QPCT

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi159 – 1591Zinc; catalyticBy similarity
Active sitei201 – 2011Proton acceptorBy similarity
Metal bindingi202 – 2021Zinc; catalyticBy similarity
Active sitei248 – 2481Proton acceptorBy similarity
Metal bindingi330 – 3301Zinc; catalyticBy similarity

GO - Molecular functioni

  1. glutaminyl-peptide cyclotransferase activity Source: UniProtKB
  2. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM28.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaminyl-peptide cyclotransferase (EC:2.3.2.5)
Alternative name(s):
Glutaminyl cyclase
Short name:
QC
Glutaminyl-tRNA cyclotransferase
Gene namesi
Name:QPCT
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 361333Glutaminyl-peptide cyclotransferasePRO_0000022194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi139 ↔ 164By similarity
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ28120.

Expressioni

Tissue specificityi

Expressed mainly in brain tissue.

Structurei

3D structure databases

ProteinModelPortaliQ28120.
SMRiQ28120. Positions 33-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG298226.
HOGENOMiHOG000189291.
HOVERGENiHBG009812.
InParanoidiQ28120.
KOiK00683.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q28120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGCRDPRVV DTLHLLLLVA VLPLAVSGVR RGAVDWTQEK NYHQPALLNV
60 70 80 90 100
SSLRQVAEGT SISEMWQNDL RPLLIERYPG SPGSFAARQH IMQRIQRLQA
110 120 130 140 150
DWVLEVDTFL SQTPYGYRSF SNIISTLNPT AKRHLVLACH YDSKYFPHWD
160 170 180 190 200
DRVFVGATDS AVPCAMMLEL ARALDKQLFS LKNISDSRPD LSLQLIFFDG
210 220 230 240 250
EEAFHLWSPQ DSLYGSRHLA SKMASTPHPP GARDTNQLHG MDLLVLLDLI
260 270 280 290 300
GAPFPTFPNF FPNTARWFGR LEAIEHGLRE LGLLKDHSSE RWYFRNYGYG
310 320 330 340 350
GVIQDDHIPF LRRGVPVLHL ISSPFPEVWH TMDDNEENLD RTTIDNLNKI
360
LQVFVLEYLH L
Length:361
Mass (Da):41,224
Last modified:November 1, 1997 - v1
Checksum:iEF72BE77C07369DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80626 mRNA. Translation: AAA30549.1.
PIRiA41535.
RefSeqiNP_803472.1. NM_177506.2.
UniGeneiBt.412.

Genome annotation databases

GeneIDi281437.
KEGGibta:281437.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80626 mRNA. Translation: AAA30549.1.
PIRiA41535.
RefSeqiNP_803472.1. NM_177506.2.
UniGeneiBt.412.

3D structure databases

ProteinModelPortaliQ28120.
SMRiQ28120. Positions 33-361.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM28.974.

Proteomic databases

PRIDEiQ28120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281437.
KEGGibta:281437.

Organism-specific databases

CTDi25797.

Phylogenomic databases

eggNOGiNOG298226.
HOGENOMiHOG000189291.
HOVERGENiHBG009812.
InParanoidiQ28120.
KOiK00683.

Miscellaneous databases

NextBioi20805423.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure and functional expression of a glutaminyl cyclase."
    Pohl T., Zimmer M., Mugele K., Spiess J.
    Proc. Natl. Acad. Sci. U.S.A. 88:10059-10063(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiQPCT_BOVIN
AccessioniPrimary (citable) accession number: Q28120
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.