ID   QPCT_BOIIR              Reviewed;         368 AA.
AC   A7ISW1;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 38.
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   Boiga irregularis (Brown tree snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Boiga.
OX   NCBI_TaxID=92519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Pawlak J., Kini M.R.;
RT   "Glutaminyl cyclase expressed in Boiga irregularis venom gland tissue.";
RL   Submitted (FEB-2006) 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; DQ404533; ABD64599.1; -; mRNA.
DR   AlphaFoldDB; A7ISW1; -.
DR   SMR; A7ISW1; -.
DR   MEROPS; M28.974; -.
DR   BRENDA; 2.3.2.5; 9166.
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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..368
FT                   /note="Glutaminyl-peptide cyclotransferase"
FT                   /id="PRO_0000407861"
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;  41990 MW;  A6548DC3707FA399 CRC64;
     MAGERRDSKA AAFFCLAWAL CLALPGFPQH VGGREDRADW TQEKYSHRPT ILNATSILQV
     TSQTNVNRMW QNDLHPILIE RYPGSPGSYA VRQHIKHRLQ GLQAGWLVEE DTFQSHTPYG
     YRTFSNIIST LNPLAKRHLV VACHYDSKYF LPQLDGKVFV GATDSAVPCA MMLELARSLD
     RQLSFLKQSS LPPKADLSLK LIFFDGEEAF VRWSPSDSLY GSRSLAQKMA STPHPPGARN
     TNQIQGIDLF VLLDLIGARN PVFPVYFLNT ARWFGRLEAI EQSLHDLGLL NNYSSERQYF
     RSNLRRYPVE DDHIPFLRRG VPILHLIPSP FPRVWHTMED NEENLDKPTI DNISKILQVF
     VLEYLNLG