QPCT_GLOBL
ID QPCT_GLOBL Reviewed; 368 AA.
AC Q90YA8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Glutaminyl-peptide cyclotransferase;
DE EC=2.3.2.5;
DE AltName: Full=Glutaminyl cyclase;
DE Short=QC;
DE AltName: Full=Glutaminyl-tRNA cyclotransferase;
DE Flags: Precursor;
GN Name=QPCT;
OS Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=242054;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Murayama N.;
RT "Agkistrodon blomhoffi mRNA for glutaminyl cyclase precursor, complete
RT cds.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides.
CC Has a bias against acidic and tryptophan residues adjacent to the N-
CC terminal glutaminyl residue and a lack of importance of chain length
CC after the second residue. Also catalyzes N-terminal pyroglutamate
CC formation (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-glutaminyl-[peptide] = N-terminal 5-oxo-L-prolyl-
CC [peptide] + NH4(+); Xref=Rhea:RHEA:23652, Rhea:RHEA-COMP:11736,
CC Rhea:RHEA-COMP:11846, ChEBI:CHEBI:28938, ChEBI:CHEBI:64722,
CC ChEBI:CHEBI:87215; EC=2.3.2.5;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the glutaminyl-peptide cyclotransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is unclear whether this protein requires a metal cofactor
CC for catalysis. It was originally proposed to be a Zn(2+)-dependent
CC metalloenzyme based on structural similarities to bacterial
CC aminopeptidases and the observation that it can bind Zn(2+) ions,
CC typically in a 1:1 stoichiometry (By similarity). However, a recent
CC study suggests a Zn(2+)-independent catalytic mechanism (By
CC similarity). {ECO:0000250|UniProtKB:B7QK46,
CC ECO:0000250|UniProtKB:Q16769}.
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DR EMBL; AB059426; BAB69586.1; -; mRNA.
DR AlphaFoldDB; Q90YA8; -.
DR SMR; Q90YA8; -.
DR MEROPS; M28.974; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0017186; P:peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase; ISS:UniProtKB.
DR CDD; cd03880; M28_QC_like; 1.
DR InterPro; IPR037457; M28_QC.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR040234; QC/QCL.
DR PANTHER; PTHR12283; PTHR12283; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Disulfide bond; Glycoprotein; Metal-binding; Secreted;
KW Signal; Transferase; Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..368
FT /note="Glutaminyl-peptide cyclotransferase"
FT /id="PRO_0000407859"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 143..169
FT /evidence="ECO:0000250|UniProtKB:Q16769"
SQ SEQUENCE 368 AA; 42267 MW; 61959488048DE899 CRC64;
MARERRDSKA ATFFCLAWAL CLALPGFPQH VSGREDRVDW TQEKYSHRPT ILNATCILQV
TSQTNVNRMW QNDLHPILIE RYPGSPGSYA VRQHIKHRLQ GLQAGWLVEE DTFQSHTPYG
YRTFSNIIST LNPLAKRHLV IACHYDSKYF PPQLDGKVFV GATDSAVPCA MMLELARSLD
RQLSFLKQSS LPPKADLSLK LIFFDGEEAF VRWSPSDSLY GSRSLAQKMA STPHPPGARN
TYQIQGIDLF VLLDLIGARN PVFPVYFLNT ARWFGRLEAI EQNLYDLGLL NNYSSERQYF
RSNLRRHPVE DDHIPFLRRG VPILHLIPSP FPRVWHTMED NEENLDKPTI DNLSKILQVF
VLEYLNLG