ID A0A2U3V6G3_TURTR Unreviewed; 383 AA.
AC A0A2U3V6G3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=glutaminyl-peptide cyclotransferase {ECO:0000256|ARBA:ARBA00012012};
DE EC=2.3.2.5 {ECO:0000256|ARBA:ARBA00012012};
GN Name=QPCTL {ECO:0000313|RefSeq:XP_004323600.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_004323600.1};
RN [1] {ECO:0000313|RefSeq:XP_004323600.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_004323600.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00000001};
CC -!- SIMILARITY: Belongs to the glutaminyl-peptide cyclotransferase family.
CC {ECO:0000256|ARBA:ARBA00006014}.
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DR RefSeq; XP_004323600.1; XM_004323552.3.
DR AlphaFoldDB; A0A2U3V6G3; -.
DR STRING; 9739.ENSTTRP00000013553; -.
DR GeneID; 101322001; -.
DR OrthoDB; 3091175at2759; -.
DR Proteomes; UP000245320; Chromosome 19.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IEA:UniProtKB-EC.
DR CDD; cd03880; M28_QC_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR037457; M28_QC.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR040234; QC/QCL.
DR PANTHER; PTHR12283; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR PANTHER; PTHR12283:SF3; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE-LIKE PROTEIN; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..375
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 42747 MW; 0C34C789F4927352 CRC64;
MRSGGRGRPR LRLGERGLLE PPSPPKRRLL PRAQLLPLLL LALAVASVLY TSWSGWHRQS
EELPLGRELR GPSIGSLPEA GVRRVVGQLD PHRLWNNYLR PLLVVRTPGS PGNLQVRKFL
EATLRTLTAG WHVELDPFTA STPLGPLHFS NVVATLDPRA ARHLTLACHY DSKLFPSGSA
PFVGATDSAV PCALLLELAQ ALDLELARAK EQAAPVTLQL LFLDGEEALK EWGPQDSLYG
SRHLAQLMES APHSPGFTRI QAIDLFMLLD LLGAPNPTFY SHFPRTVRWF HRLRSIEKRL
HRLNLLQSHP WEVMYFQPGE PPGSVEDDHI PFLRRGVPVL HLISTPFPSV WHTSDDSEAN
LHPPTVHNLS RILAVFLAEY LGL
//