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Q9CYK2 (QPCT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutaminyl-peptide cyclotransferase
EC=2.3.2.5
Alternative name(s):
Glutaminyl cyclase
Short name=QC
Glutaminyl-tRNA cyclotransferase
Gene names
Name:Qpct
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glutaminyl-peptide cyclotransferase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9CYK2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9CYK2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     42-90: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 362327Glutaminyl-peptide cyclotransferase
PRO_0000022196

Sites

Active site2021Proton acceptor By similarity
Active site2491Proton acceptor By similarity
Metal binding1601Zinc; catalytic By similarity
Metal binding2031Zinc; catalytic By similarity
Metal binding3311Zinc; catalytic By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation501N-linked (GlcNAc...) Ref.3
Disulfide bond140 ↔ 165 Ref.3

Natural variations

Alternative sequence42 – 9049Missing in isoform 2.
VSP_013911

Experimental info

Sequence conflict81R → L in BAC29748. Ref.1
Sequence conflict81R → L in BAC32556. Ref.1
Sequence conflict81R → L in BAB30831. Ref.1
Sequence conflict311S → N in AAH20023. Ref.2
Sequence conflict351A → G in AAH20023. Ref.2
Sequence conflict2131S → T in BAB30831. Ref.1
Sequence conflict3261F → S in BAB30831. Ref.1

Secondary structure

1 .................................................... 362
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: F23637D4EF6ED1F6

FASTA36241,119
        10         20         30         40         50         60 
MAGSEDKRVV GTLHLLLLQA TVLSLTAGNL SLVSAAWTQE KNHHQPAHLN SSSLQQVAEG 

        70         80         90        100        110        120 
TSISEMWQND LRPLLIERYP GSPGSYSARQ HIMQRIQRLQ AEWVVEVDTF LSRTPYGYRS 

       130        140        150        160        170        180 
FSNIISTLNP EAKRHLVLAC HYDSKYFPRW DSRVFVGATD SAVPCAMMLE LARALDKKLH 

       190        200        210        220        230        240 
SLKDVSGSKP DLSLRLIFFD GEEAFHHWSP QDSLYGSRHL AQKMASSPHP PGSRGTNQLD 

       250        260        270        280        290        300 
GMDLLVLLDL IGAANPTFPN FFPKTTRWFN RLQAIEKELY ELGLLKDHSL ERKYFQNFGY 

       310        320        330        340        350        360 
GNIIQDDHIP FLRKGVPVLH LIASPFPEVW HTMDDNEENL HASTIDNLNK IIQVFVLEYL 


HL

« Hide

Isoform 2 [UniParc].

Checksum: B5FB17040CD91883
Show »

FASTA31335,648

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Corpora quadrigemina, Embryo and Skin.
[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] (ISOFORM 2).
Strain: Czech II.
Tissue: Mammary gland.
[3]"Structures of glycosylated mammalian glutaminyl cyclases reveal conformational variability near the active center."
Ruiz-Carrillo D., Koch B., Parthier C., Wermann M., Dambe T., Buchholz M., Ludwig H.H., Heiser U., Rahfeld J.U., Stubbs M.T., Schilling S., Demuth H.U.
Biochemistry 50:6280-6288(2011) [PubMed: 21671571] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 36-362, GLYCOSYLATION AT ASN-50, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK037197 mRNA. Translation: BAC29748.1.
AK045974 mRNA. Translation: BAC32556.1.
AK017598 mRNA. Translation: BAB30831.1.
BC020023 mRNA. Translation: AAH20023.1.
IPIIPI00461022.
IPI00606704.
RefSeqNP_081731.1. NM_027455.2.
UniGeneMm.293870.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SI1X-ray2.90A36-362[»]
3SI2X-ray1.80A36-362[»]
ProteinModelPortalQ9CYK2.
SMRQ9CYK2. Positions 36-362.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9CYK2.

Protein family/group databases

MEROPSM28.979.

Proteomic databases

PRIDEQ9CYK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040789; ENSMUSP00000038732; ENSMUSG00000024084.
GeneID70536.
KEGGmmu:70536.
UCSCuc008dpv.1. mouse.
uc008dpw.1. mouse.

Organism-specific databases

CTD25797.
MGIMGI:1917786. Qpct.

Phylogenomic databases

GeneTreeENSGT00390000003107.
HOGENOMHBG314483.
HOVERGENHBG009812.
InParanoidQ9CYK2.
OrthoDBEOG4XSKQ7.
PhylomeDBQ9CYK2.

Gene expression databases

ArrayExpressQ9CYK2.
BgeeQ9CYK2.
GenevestigatorQ9CYK2.
GermOnlineENSMUSG00000024084. Mus musculus.

Family and domain databases

InterProIPR007484. Peptidase_M28.
[Graphical view]
KOK00683.
PfamPF04389. Peptidase_M28. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio331811.
SOURCESearch...

Entry information

Entry nameQPCT_MOUSE
AccessionPrimary (citable) accession number: Q9CYK2
Secondary accession number(s): Q8BH20, Q8VE07
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) 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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents