ID   QPCTL_MACFA             Reviewed;         382 AA.
AC   Q4R942;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Glutaminyl-peptide cyclotransferase-like protein;
DE            EC=2.3.2.5;
DE   AltName: Full=Golgi-resident glutaminyl-peptide cyclotransferase;
DE   AltName: Full=isoQC;
DE            Short=gQC;
GN   Name=QPCTL; ORFNames=QtsA-10761;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides.
CC       {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: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type I membrane protein {ECO:0000250}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB168255; BAE00379.1; -; mRNA.
DR   RefSeq; NP_001270871.1; NM_001283942.1.
DR   RefSeq; XP_015296440.1; XM_015440954.1.
DR   AlphaFoldDB; Q4R942; -.
DR   SMR; Q4R942; -.
DR   STRING; 9541.XP_005589663.1; -.
DR   MEROPS; M28.016; -.
DR   Ensembl; ENSMFAT00000042623; ENSMFAP00000010695; ENSMFAG00000009032.
DR   GeneID; 102124146; -.
DR   KEGG; mcf:102124146; -.
DR   CTD; 54814; -.
DR   VEuPathDB; HostDB:ENSMFAG00000009032; -.
DR   eggNOG; KOG3946; Eukaryota.
DR   GeneTree; ENSGT00390000003107; -.
DR   OMA; HNPRRST; -.
DR   OrthoDB; 1257754at2759; -.
DR   Proteomes; UP000233100; Chromosome 19.
DR   Bgee; ENSMFAG00000009032; Expressed in skeletal muscle tissue and 13 other tissues.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Golgi apparatus; Membrane; Metal-binding;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..382
FT                   /note="Glutaminyl-peptide cyclotransferase-like protein"
FT                   /id="PRO_0000302003"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        225
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
FT   DISULFID        167..191
FT                   /evidence="ECO:0000250|UniProtKB:Q16769"
SQ   SEQUENCE   382 AA;  42738 MW;  5C4AD78595184678 CRC64;
     MRSGGRGRPR LRLGERGVME PLLPPKRRLL PRVRLLPLLL ALAVGSAFYT IWSGWHRRTE
     ELPLGRELRV PLIGSLPEAR LRRVVGQLDP QRLWGTYLRP LLVVRTPGSP GNLQVRKFLE
     ATLRSLTAGW HVELDPFTAS TPLGPVDFGN VVATLDPGAA RHLTLACHYD SKLFPPGSTP
     FVGATDSAVP CALLLELAQA LDLELSRAKE QAAPVTLQLL FLDGEEALKE WGPKDSLYGS
     RHLAQLMESI PHSPGPTRIQ AIELFMLLDL LGAPNPTFYS HFPRTVRWFH RLRSIEKRLH
     RLNLLQSHPQ EVMYFQPGEP FGSVEDDHIP FLRRGVPVLH LISTPFPAVW HTPADTEANL
     HPPTVHNLSR ILAVFLAEYL GL