ID   QPCT_BOVIN              Reviewed;         361 AA.
AC   Q28120;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 108.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1946423; DOI=10.1073/pnas.88.22.10059;
RA   Pohl T., Zimmer M., Mugele K., Spiess J.;
RT   "Primary structure and functional expression of a glutaminyl cyclase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:10059-10063(1991).
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 mainly in brain tissue.
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; M80626; AAA30549.1; -; mRNA.
DR   PIR; A41535; A41535.
DR   RefSeq; NP_803472.1; NM_177506.2.
DR   AlphaFoldDB; Q28120; -.
DR   SMR; Q28120; -.
DR   STRING; 9913.ENSBTAP00000018493; -.
DR   MEROPS; M28.974; -.
DR   PaxDb; Q28120; -.
DR   GeneID; 281437; -.
DR   KEGG; bta:281437; -.
DR   CTD; 25797; -.
DR   eggNOG; KOG3946; Eukaryota.
DR   InParanoid; Q28120; -.
DR   OrthoDB; 1257754at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Metal-binding; Reference proteome; Secreted; Signal; Transferase; Zinc.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..361
FT                   /note="Glutaminyl-peptide cyclotransferase"
FT                   /id="PRO_0000022194"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   ACT_SITE        248
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        139..164
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
SQ   SEQUENCE   361 AA;  41224 MW;  EF72BE77C07369DA CRC64;
     MAGCRDPRVV DTLHLLLLVA VLPLAVSGVR RGAVDWTQEK NYHQPALLNV SSLRQVAEGT
     SISEMWQNDL RPLLIERYPG SPGSFAARQH IMQRIQRLQA DWVLEVDTFL SQTPYGYRSF
     SNIISTLNPT AKRHLVLACH YDSKYFPHWD DRVFVGATDS AVPCAMMLEL ARALDKQLFS
     LKNISDSRPD LSLQLIFFDG EEAFHLWSPQ DSLYGSRHLA SKMASTPHPP GARDTNQLHG
     MDLLVLLDLI GAPFPTFPNF FPNTARWFGR LEAIEHGLRE LGLLKDHSSE RWYFRNYGYG
     GVIQDDHIPF LRRGVPVLHL ISSPFPEVWH TMDDNEENLD RTTIDNLNKI LQVFVLEYLH
     L