QPCTL_BOVIN
ID QPCTL_BOVIN Reviewed; 383 AA.
AC Q0V8G3; Q1JP99; Q1JPE4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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;
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 [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal medulla;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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}.
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DR EMBL; BT025409; ABF57365.1; -; mRNA.
DR EMBL; BT025454; ABF57410.1; -; mRNA.
DR EMBL; BT026254; ABG67093.1; -; mRNA.
DR EMBL; BT026255; ABG67094.1; -; mRNA.
DR EMBL; BC120182; AAI20183.1; -; mRNA.
DR RefSeq; NP_001069408.1; NM_001075940.2.
DR AlphaFoldDB; Q0V8G3; -.
DR SMR; Q0V8G3; -.
DR STRING; 9913.ENSBTAP00000032205; -.
DR PaxDb; Q0V8G3; -.
DR PRIDE; Q0V8G3; -.
DR Ensembl; ENSBTAT00000032269; ENSBTAP00000032205; ENSBTAG00000012176.
DR GeneID; 530871; -.
DR KEGG; bta:530871; -.
DR CTD; 54814; -.
DR VEuPathDB; HostDB:ENSBTAG00000012176; -.
DR VGNC; VGNC:33599; QPCTL.
DR eggNOG; KOG3946; Eukaryota.
DR GeneTree; ENSGT00390000003107; -.
DR HOGENOM; CLU_045003_3_0_1; -.
DR InParanoid; Q0V8G3; -.
DR OMA; CDRVRMP; -.
DR OrthoDB; 1257754at2759; -.
DR TreeFam; TF315071; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000012176; Expressed in prostate gland and 103 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..383
FT /note="Glutaminyl-peptide cyclotransferase-like protein"
FT /id="PRO_0000302001"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q16769"
FT DISULFID 168..192
FT /evidence="ECO:0000250|UniProtKB:Q16769"
SQ SEQUENCE 383 AA; 42898 MW; CEB6C81B975C862C CRC64;
MPSGGRGRPR LQVGERSLLE RPSPPKRRLI PRAQLLPQLL LALTVASVFY TIWRIWHSQT
EELPLGRELR GPLIGSLPEA RVRRVVGQLD PHRLWNTFLR PLLVVRTPGS PGNLQVRKFL
EATLRTLSAG WHIELDSFTA STPVGPLDFS NVVATLDPGA ARHLTLACHY DSKLFPSDSA
PFVGATDSAV PCSLLLELAQ ALDQELGKAK ERAAPMTLQL IFLDGEEALK QWGPKDSLYG
SRHLAQLMES TPHGLGSTRI QAIELFMLLD LLGAPNPTFY SHFPRTARWF HRLRSIEKRL
HRLNLLQSHP WEVMYFQTGE PPGSVEDDHI PFLRRGVPVL HLIATPFPSV WHTSDDSEAN
LHPPTVHNLS RILAVFLAEY LGL
