Q28120 (QPCT_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutaminyl-peptide cyclotransferase
EC=2.3.2.5

Alternative name(s):
Glutaminyl cyclase
Short name=QC
Glutaminyl-tRNA cyclotransferase

Gene names

Name:

QPCT

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Also catalyzes N-terminal pyroglutamate formation 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.
Tissue specificity	Expressed mainly in brain tissue.
Sequence similarities	Belongs to the glutaminyl-peptide cyclotransferase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutaminyl-peptide cyclotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB peptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 361	333	Glutaminyl-peptide cyclotransferase		PRO_0000022194
Sites
	Active site	201	1	Proton acceptor By similarity
	Active site	248	1	Proton acceptor By similarity
	Metal binding	159	1	Zinc; catalytic By similarity
	Metal binding	202	1	Zinc; catalytic By similarity
	Metal binding	330	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	49	1	N-linked (GlcNAc...) Potential
	Glycosylation	183	1	N-linked (GlcNAc...) Potential
	Disulfide bond	139 ↔ 164		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q28120 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: EF72BE77C07369DA	FASTA	361	41,224
	10 20 30 40 50 60 MAGCRDPRVV DTLHLLLLVA VLPLAVSGVR RGAVDWTQEK NYHQPALLNV SSLRQVAEGT 70 80 90 100 110 120 SISEMWQNDL RPLLIERYPG SPGSFAARQH IMQRIQRLQA DWVLEVDTFL SQTPYGYRSF 130 140 150 160 170 180 SNIISTLNPT AKRHLVLACH YDSKYFPHWD DRVFVGATDS AVPCAMMLEL ARALDKQLFS 190 200 210 220 230 240 LKNISDSRPD LSLQLIFFDG EEAFHLWSPQ DSLYGSRHLA SKMASTPHPP GARDTNQLHG 250 260 270 280 290 300 MDLLVLLDLI GAPFPTFPNF FPNTARWFGR LEAIEHGLRE LGLLKDHSSE RWYFRNYGYG 310 320 330 340 350 360 GVIQDDHIPF LRRGVPVLHL ISSPFPEVWH TMDDNEENLD RTTIDNLNKI LQVFVLEYLH L

References

[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(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M80626 mRNA. Translation: AAA30549.1.
IPI	IPI00700666.
PIR	A41535.
RefSeq	NP_803472.1. NM_177506.2.
UniGene	Bt.412.
3D structure databases
ProteinModelPortal	Q28120.
SMR	Q28120. Positions 33-361.
ModBase	Search...
Protein family/group databases
MEROPS	M28.974.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	281437.
KEGG	bta:281437.
Organism-specific databases
CTD	25797.
Phylogenomic databases
eggNOG	NOG298226.
HOGENOM	HOG000189291.
HOVERGEN	HBG009812.
InParanoid	Q28120.
KO	K00683.
OrthoDB	EOG4XSKQ7.
Family and domain databases
InterPro	IPR007484. Peptidase_M28. [Graphical view]
Pfam	PF04389. Peptidase_M28. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20805423.

Entry information

Entry name

QPCT_BOVIN

Accession

Primary (citable) accession number: Q28120

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program