QPCT_ARATH
ID QPCT_ARATH Reviewed; 320 AA.
AC Q84WV9; Q2V3F0; Q8LFT4; Q9T000;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glutaminyl-peptide cyclotransferase;
DE EC=2.3.2.5;
DE AltName: Full=Glutaminyl cyclase;
GN Name=QCT; Synonyms=QC; OrderedLocusNames=At4g25720; ORFNames=L73G19.100;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ALTERNATIVE SPLICING.
RX PubMed=17261077; DOI=10.1515/bc.2007.016;
RA Schilling S., Stenzel I., von Bohlen A., Wermann M., Schulz K.,
RA Demuth H.-U., Wasternack C.;
RT "Isolation and characterization of the glutaminyl cyclases from Solanum
RT tuberosum and Arabidopsis thaliana: implications for physiological
RT functions.";
RL Biol. Chem. 388:145-153(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18768907; DOI=10.1104/pp.108.125716;
RA Ohkama-Ohtsu N., Oikawa A., Zhao P., Xiang C., Saito K., Oliver D.J.;
RT "A gamma-glutamyl transpeptidase-independent pathway of glutathione
RT catabolism to glutamate via 5-oxoproline in Arabidopsis.";
RL Plant Physiol. 148:1603-1613(2008).
CC -!- FUNCTION: Converts glutamine and N-terminal glutamyl residues in
CC peptides to 5-oxoproline and 5-oxoproline residues. Not involved in the
CC major pathway for 5-oxoproline production.
CC {ECO:0000269|PubMed:17261077, ECO:0000269|PubMed:18768907}.
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:0000269|PubMed:17261077};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for H-Gln-7-amino-4-methylcoumarin
CC {ECO:0000269|PubMed:17261077};
CC KM=28 uM for H-Gln-beta-naphthylamine {ECO:0000269|PubMed:17261077};
CC KM=151 uM for H-Gln-tert-butyl ester {ECO:0000269|PubMed:17261077};
CC KM=480 uM for H-Gln-NH(2) {ECO:0000269|PubMed:17261077};
CC KM=1100 uM for H-Gln-Gly-OH {ECO:0000269|PubMed:17261077};
CC KM=294 uM for H-Gln-Ala-OH {ECO:0000269|PubMed:17261077};
CC KM=53 uM for H-Gln-Gln-OH {ECO:0000269|PubMed:17261077};
CC KM=265 uM for H-Gln-Glu-OH {ECO:0000269|PubMed:17261077};
CC KM=591 uM for H-Gln-Gly-Pro-OH {ECO:0000269|PubMed:17261077};
CC KM=14 uM for H-Gln-Val-Ala-OH {ECO:0000269|PubMed:17261077};
CC KM=106 uM for H-Gln-Phe-Ala-NH(2) {ECO:0000269|PubMed:17261077};
CC KM=80 uM for H-Gln-Glu-Ala-Phe-NH(2) {ECO:0000269|PubMed:17261077};
CC KM=86 uM for H-Gln-Glu-Tyr-Phe-NH(2) {ECO:0000269|PubMed:17261077};
CC KM=60 uM for H-Gln-Lys-Arg-Leu-NH(2) {ECO:0000269|PubMed:17261077};
CC KM=487 uM for H-Gln-Asp-Glu-Leu-NH(2) {ECO:0000269|PubMed:17261077};
CC Note=Requires an unprotonated substrate N-terminus and a protonated
CC basic group of the enzyme for binding and conversion of the
CC glutaminyl substrates.;
CC pH dependence:
CC Optimum pH is mildly basic for conversion of the glutaminyl
CC substrates and shifted to acidic for cyclization of glutamic acid.
CC {ECO:0000269|PubMed:17261077};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q84WV9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84WV9-2; Sequence=VSP_037808, VSP_037809;
CC Name=3;
CC IsoId=Q84WV9-3; Sequence=VSP_037807;
CC -!- PTM: Glycosylated.
CC -!- DISRUPTION PHENOTYPE: No effect on 5-oxoproline production.
CC {ECO:0000269|PubMed:18768907}.
CC -!- MISCELLANEOUS: Has a low metal affinity, in contrast to the mammalian
CC glutaminyl cyclases that contain one zinc ion per molecule.
CC -!- SIMILARITY: Belongs to the plant glutaminyl-peptide cyclotransferase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43703.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81382.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL050400; CAB43703.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81382.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85103.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85104.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85105.1; -; Genomic_DNA.
DR EMBL; BT001929; AAN71928.1; -; mRNA.
DR EMBL; AY084653; AAM61216.1; -; mRNA.
DR EMBL; AK316976; BAH19673.1; -; mRNA.
DR PIR; T09564; T09564.
DR RefSeq; NP_001031716.1; NM_001036639.3. [Q84WV9-2]
DR RefSeq; NP_001031717.1; NM_001036640.1. [Q84WV9-3]
DR RefSeq; NP_567727.1; NM_118704.2. [Q84WV9-1]
DR AlphaFoldDB; Q84WV9; -.
DR SMR; Q84WV9; -.
DR STRING; 3702.AT4G25720.1; -.
DR PaxDb; Q84WV9; -.
DR PRIDE; Q84WV9; -.
DR ProteomicsDB; 225916; -. [Q84WV9-1]
DR EnsemblPlants; AT4G25720.1; AT4G25720.1; AT4G25720. [Q84WV9-1]
DR EnsemblPlants; AT4G25720.2; AT4G25720.2; AT4G25720. [Q84WV9-2]
DR EnsemblPlants; AT4G25720.3; AT4G25720.3; AT4G25720. [Q84WV9-3]
DR GeneID; 828677; -.
DR Gramene; AT4G25720.1; AT4G25720.1; AT4G25720. [Q84WV9-1]
DR Gramene; AT4G25720.2; AT4G25720.2; AT4G25720. [Q84WV9-2]
DR Gramene; AT4G25720.3; AT4G25720.3; AT4G25720. [Q84WV9-3]
DR KEGG; ath:AT4G25720; -.
DR Araport; AT4G25720; -.
DR TAIR; locus:2131391; AT4G25720.
DR eggNOG; ENOG502QUQC; Eukaryota.
DR HOGENOM; CLU_060272_1_0_1; -.
DR InParanoid; Q84WV9; -.
DR OMA; FANIWYE; -.
DR OrthoDB; 1284492at2759; -.
DR PhylomeDB; Q84WV9; -.
DR BioCyc; ARA:AT4G25720-MON; -.
DR PRO; PR:Q84WV9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84WV9; baseline and differential.
DR Genevisible; Q84WV9; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IDA:TAIR.
DR GO; GO:0017186; P:peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase; IDA:TAIR.
DR InterPro; IPR007788; QCT.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR31270; PTHR31270; 1.
DR Pfam; PF05096; Glu_cyclase_2; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..320
FT /note="Glutaminyl-peptide cyclotransferase"
FT /id="PRO_0000380675"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..320
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 219..238
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_037807"
FT VAR_SEQ 290..297
FT /note="VTGKLWPK -> GNKSCYHP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037808"
FT VAR_SEQ 299..320
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037809"
FT CONFLICT 311
FT /note="G -> R (in Ref. 4; AAM61216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 36269 MW; 08935D17623A9770 CRC64;
MATRSPYKRQ TKRSMIQSLP ASSSASSRRR FISRKRFAMM IPLALLSGAV FLFFMPFNSW
GQSSGSSLDL SHRINEIEVV AEFPHDPDAF TQGLLYAGND TLFESTGLYG KSSVRKVDLR
TGKVEILEKM DNTYFGEGLT LLGERLFQVA WLTNTGFTYD LRNLSKVKPF KHHMKDGWGL
ATDGKALFGS DGTSTLYRMD PQTMKVTDKH IVRYNGREVR YLNELEYINN EVWANVWQSD
CIARISPKDG SLLGWILLSK LSRGLLKSGH RGIDVLNGIA WDSDKQRLFV TGKLWPKLYQ
IKLKQASAKS GNYIEQQCLV
