QPCTL_MOUSE
ID QPCTL_MOUSE Reviewed; 383 AA.
AC Q8BH73; Q9D8T5; Q9D8Y3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Pancreas, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=18486145; DOI=10.1016/j.jmb.2008.03.078;
RA Cynis H., Rahfeld J.U., Stephan A., Kehlen A., Koch B., Wermann M.,
RA Demuth H.U., Schilling S.;
RT "Isolation of an isoenzyme of human glutaminyl cyclase: retention in the
RT Golgi complex suggests involvement in the protein maturation machinery.";
RL J. Mol. Biol. 379:966-980(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BH73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BH73-2; Sequence=VSP_027904;
CC -!- TISSUE SPECIFICITY: Detected in thalamus, hippocampus, brain cortex,
CC cerebellum, kidney, lung and liver, and at low levels in heart and
CC spleen. {ECO:0000269|PubMed:18486145}.
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; AK007555; BAB25105.1; -; mRNA.
DR EMBL; AK007701; BAB25199.1; -; mRNA.
DR EMBL; AK035587; BAC29114.1; -; mRNA.
DR EMBL; AK045687; BAC32458.1; -; mRNA.
DR EMBL; BC058181; AAH58181.1; -; mRNA.
DR CCDS; CCDS20891.1; -. [Q8BH73-1]
DR RefSeq; NP_080387.2; NM_026111.3. [Q8BH73-1]
DR AlphaFoldDB; Q8BH73; -.
DR SMR; Q8BH73; -.
DR BioGRID; 212139; 1.
DR STRING; 10090.ENSMUSP00000032566; -.
DR MEROPS; M28.016; -.
DR iPTMnet; Q8BH73; -.
DR PhosphoSitePlus; Q8BH73; -.
DR EPD; Q8BH73; -.
DR MaxQB; Q8BH73; -.
DR PaxDb; Q8BH73; -.
DR PeptideAtlas; Q8BH73; -.
DR PRIDE; Q8BH73; -.
DR ProteomicsDB; 255020; -. [Q8BH73-1]
DR ProteomicsDB; 255021; -. [Q8BH73-2]
DR Antibodypedia; 31379; 118 antibodies from 19 providers.
DR DNASU; 67369; -.
DR Ensembl; ENSMUST00000032566; ENSMUSP00000032566; ENSMUSG00000030407. [Q8BH73-1]
DR GeneID; 67369; -.
DR KEGG; mmu:67369; -.
DR UCSC; uc009fku.1; mouse. [Q8BH73-1]
DR CTD; 54814; -.
DR MGI; MGI:1914619; Qpctl.
DR VEuPathDB; HostDB:ENSMUSG00000030407; -.
DR eggNOG; KOG3946; Eukaryota.
DR GeneTree; ENSGT00390000003107; -.
DR HOGENOM; CLU_045003_3_0_1; -.
DR InParanoid; Q8BH73; -.
DR OMA; CDRVRMP; -.
DR OrthoDB; 1257754at2759; -.
DR PhylomeDB; Q8BH73; -.
DR TreeFam; TF315071; -.
DR BioGRID-ORCS; 67369; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Qpctl; mouse.
DR PRO; PR:Q8BH73; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BH73; protein.
DR Bgee; ENSMUSG00000030407; Expressed in granulocyte and 213 other tissues.
DR Genevisible; Q8BH73; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Disulfide bond; Golgi apparatus;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..383
FT /note="Glutaminyl-peptide cyclotransferase-like protein"
FT /id="PRO_0000302004"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
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"
FT VAR_SEQ 224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027904"
FT CONFLICT 194
FT /note="L -> P (in Ref. 1; BAB25199)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="W -> L (in Ref. 1; BAB25105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 42692 MW; 44F4E35B296146BA CRC64;
MSPGSRGRPR QRLEDRGLMK PPSLSKRRLL PRVQFLPLLL LALAMGLAFY IVWNSWHPGV
EEMSRSRDLR VPLIGSLSEA KLRLVVGQLD PQRLWGTFLR PLLIVRPPGS SGNLQVRKFL
EATLQSLSAG WHVELDPFTA STPLGPLDFG NVVATLDPGA ARHLTLACHY DSKFFPPGLP
PFVGATDSAV PCALLLELVQ ALDAMLSRIK QQAAPVTLQL LFLDGEEALK EWGPKDSLYG
SRHLAQIMES IPHSPGPTRI QAIELFVLLD LLGASSPIFF SHFPRTARWF QRLRSIEKRL
HRLNLLQSHP QEVMYFQPGE PPGPVEDDHI PFLRRGVPVL HLIATPFPAV WHTPADTEAN
LHPPTVHNLS RILAVFLAEY LGL
