IRE1B_ARATH
ID IRE1B_ARATH Reviewed; 881 AA.
AC Q93VJ2; Q94IG5; Q9FIN6;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Serine/threonine-protein kinase/endoribonuclease IRE1b;
DE AltName: Full=Endoplasmic reticulum-to-nucleus signaling 1-1;
DE AltName: Full=Inositol-requiring protein 1-1;
DE Short=AtIRE1-1;
DE AltName: Full=Serine/threonine-protein kinase/endoribonuclease IRE1-1;
DE Includes:
DE RecName: Full=Serine/threonine-protein kinase;
DE EC=2.7.11.1;
DE Includes:
DE RecName: Full=Endoribonuclease;
DE EC=3.1.26.-;
DE Flags: Precursor;
GN Name=IRE1B; Synonyms=IRE1-1; OrderedLocusNames=At5g24360;
GN ORFNames=K16H17.7;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11706177; DOI=10.1104/pp.010636;
RA Koizumi N., Martinez I.M., Kimata Y., Kohno K., Sano H., Chrispeels M.J.;
RT "Molecular characterization of two Arabidopsis Ire1 homologs, endoplasmic
RT reticulum-located transmembrane protein kinases.";
RL Plant Physiol. 127:949-962(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=12020828; DOI=10.1016/s0167-4781(02)00237-3;
RA Noh S.J., Kwon C.S., Chung W.I.;
RT "Characterization of two homologs of Ire1p, a kinase/endoribonuclease in
RT yeast, in Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1575:130-134(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP GENE FAMILY.
RX PubMed=12805585; DOI=10.1104/pp.103.021964;
RA Shiu S.H., Bleecker A.B.;
RT "Expansion of the receptor-like kinase/Pelle gene family and receptor-like
RT proteins in Arabidopsis.";
RL Plant Physiol. 132:530-543(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21482766; DOI=10.1073/pnas.1102117108;
RA Deng Y., Humbert S., Liu J.X., Srivastava R., Rothstein S.J., Howell S.H.;
RT "Heat induces the splicing by IRE1 of a mRNA encoding a transcription
RT factor involved in the unfolded protein response in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7247-7252(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22355548; DOI=10.1038/srep00029;
RA Nagashima Y., Mishiba K., Suzuki E., Shimada Y., Iwata Y., Koizumi N.;
RT "Arabidopsis IRE1 catalyses unconventional splicing of bZIP60 mRNA to
RT produce the active transcription factor.";
RL Sci. Rep. 1:29-29(2011).
RN [9]
RP FUNCTION.
RX PubMed=23175745; DOI=10.1105/tpc.112.101535;
RA Liu Y., Burgos J.S., Deng Y., Srivastava R., Howell S.H., Bassham D.C.;
RT "Degradation of the endoplasmic reticulum by autophagy during endoplasmic
RT reticulum stress in Arabidopsis.";
RL Plant Cell 24:4635-4651(2012).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21914012; DOI=10.1111/j.1365-313x.2011.04788.x;
RA Chen Y., Brandizzi F.;
RT "AtIRE1A/AtIRE1B and AGB1 independently control two essential unfolded
RT protein response pathways in Arabidopsis.";
RL Plant J. 69:266-277(2012).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=22359644; DOI=10.1371/journal.pone.0031944;
RA Moreno A.A., Mukhtar M.S., Blanco F., Boatwright J.L., Moreno I.,
RA Jordan M.R., Chen Y., Brandizzi F., Dong X., Orellana A.,
RA Pajerowska-Mukhtar K.M.;
RT "IRE1/bZIP60-mediated unfolded protein response plays distinct roles in
RT plant immunity and abiotic stress responses.";
RL PLoS ONE 7:E31944-E31944(2012).
RN [12]
RP FUNCTION.
RX PubMed=22701744; DOI=10.1371/journal.pone.0039023;
RA Humbert S., Zhong S., Deng Y., Howell S.H., Rothstein S.J.;
RT "Alteration of the bZIP60/IRE1 pathway affects plant response to ER stress
RT in Arabidopsis thaliana.";
RL PLoS ONE 7:E39023-E39023(2012).
RN [13]
RP REVIEW.
RX PubMed=22796463; DOI=10.1016/j.tplants.2012.06.014;
RA Iwata Y., Koizumi N.;
RT "Plant transducers of the endoplasmic reticulum unfolded protein
RT response.";
RL Trends Plant Sci. 17:720-727(2012).
CC -!- FUNCTION: Senses unfolded proteins in the lumen of the endoplasmic
CC reticulum via its N-terminal domain which leads to enzyme auto-
CC activation. The active endoribonuclease domain splices bZIP60 mRNA to
CC generate a new C-terminus, converting it into a potent unfolded-protein
CC response transcriptional activator which then induces transcription of
CC UPR target genes. Involved in organ growth regulation. Plays a role in
CC plant immunity and abiotic stress responses. Required for ER stress-
CC induced autophagy. {ECO:0000269|PubMed:11706177,
CC ECO:0000269|PubMed:21482766, ECO:0000269|PubMed:21914012,
CC ECO:0000269|PubMed:22355548, ECO:0000269|PubMed:22359644,
CC ECO:0000269|PubMed:22701744, ECO:0000269|PubMed:23175745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: The kinase domain is activated by trans-
CC autophosphorylation. Kinase activity is required for activation of the
CC endoribonuclease domain (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Dimer formation is driven by
CC hydrophobic interactions within the N-terminal luminal domains and
CC stabilized by disulfide bridges (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11706177}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:11706177}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q93VJ2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in the apical meristem, at
CC leaf margins where vascular bundles end, in the anthers before pollen
CC is formed and in the ovules at a very early stage of development. There
CC is no expression in more mature embryos. Also strongly expressed in the
CC cotyledons immediately after germination but not later on.
CC {ECO:0000269|PubMed:11706177, ECO:0000269|PubMed:12020828}.
CC -!- INDUCTION: By ER stress inducer tunicamycin, by salicylic acid (SA) and
CC by bacterial pathogen infection. {ECO:0000269|PubMed:22359644}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Ire1a and ire1b double
CC mutant is more sensitive to the ER stress inducer tunicamycin than the
CC wild-type and is enable to give rise to the spliced bZIP60 mRNA form
CC (PubMed:22355548). Ire1a and ire1b double mutant displays short roots
CC and a ER stress-sensitive phenotype (PubMed:21914012).
CC {ECO:0000269|PubMed:21482766, ECO:0000269|PubMed:21914012,
CC ECO:0000269|PubMed:22355548, ECO:0000269|PubMed:22359644}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11229.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB049936; BAB63366.1; -; mRNA.
DR EMBL; AY057897; AAL17714.1; -; mRNA.
DR EMBL; AB016884; BAB11229.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93301.1; -; Genomic_DNA.
DR EMBL; AY057480; AAL09714.1; -; mRNA.
DR RefSeq; NP_568444.1; NM_122344.5. [Q93VJ2-1]
DR AlphaFoldDB; Q93VJ2; -.
DR SMR; Q93VJ2; -.
DR BioGRID; 17782; 2.
DR STRING; 3702.AT5G24360.2; -.
DR iPTMnet; Q93VJ2; -.
DR PaxDb; Q93VJ2; -.
DR ProteomicsDB; 232226; -. [Q93VJ2-1]
DR EnsemblPlants; AT5G24360.1; AT5G24360.1; AT5G24360. [Q93VJ2-1]
DR GeneID; 832507; -.
DR Gramene; AT5G24360.1; AT5G24360.1; AT5G24360. [Q93VJ2-1]
DR KEGG; ath:AT5G24360; -.
DR Araport; AT5G24360; -.
DR eggNOG; KOG1027; Eukaryota.
DR InParanoid; Q93VJ2; -.
DR OMA; MYRETED; -.
DR PhylomeDB; Q93VJ2; -.
DR PRO; PR:Q93VJ2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93VJ2; baseline and differential.
DR Genevisible; Q93VJ2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0034263; P:positive regulation of autophagy in response to ER overload; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009751; P:response to salicylic acid; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR Gene3D; 1.20.1440.180; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13954; PTHR13954; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Autophagy; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Immunity; Kinase;
KW Magnesium; Membrane; Metal-binding; mRNA processing; mRNA splicing;
KW Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW Unfolded protein response.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..881
FT /note="Serine/threonine-protein kinase/endoribonuclease
FT IRE1b"
FT /id="PRO_0000422138"
FT TOPO_DOM 22..357
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..881
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 459..744
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 747..878
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 481..502
FT /note="ATP selon article"
FT REGION 642..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 608
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 465..473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 647
FT /note="T -> I (in Ref. 1; BAB63366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 881 AA; 99616 MW; AECD3585336081F8 CRC64;
MRGSALLDLI LFLLVSPLAH SFKGSEISKF YDKSISNQIS QSDRESGYVL VSTVDGSISL
VDMSSQKLDW TFHTNEPIYS SYQAPHYHYT TDEERSSVLG DDFYMDCDKD WRLYNSSVRK
GKRVNEIVDA SEFIGTLPYT STDRIVLGKK DTSVFLLDWK TGKLVKRYRM DELYSNTVVE
NDKEKAIVLS KEAPLLFGSG FKKSEDFPEL VYIERKDFKI QCISKFGDVL WSVSYAKMEA
KLQNHESVQF ISGLSSSVGK NQFPLSYTTS VPMVQLRNVK YETLFPRLGF LDEALYLPFQ
DRKPNQLAIG DGNQLTLPGN KEAEEVLSLP LPETVISQIT DIIDGSTKQA GFASKFSGLI
VLIFGFCVTM LSVCGLFFYR LRQSIRIKEP YVSEVPIATP KKKKSKKNGT TKAVHKKENG
FISGGNKDPS HEENEKRLLT AFPGLNNSSA EGYRVGKLFV SNKEIAKGSN GTVVLEGSYE
GRLVAVKRLV QSHHDVAQKE ILNLMASDKH SNIVRWYGVD QDEHFIYISL ELCACSLNDL
IYASSALLES PMASSSIHSI QINPIFENGK GVELWKENGH PSPVLLKLMR DIVAGLVHLH
DIGIVHRDLK PQNVLIVKNS SLCAKLSDMG ISKRLPADTS ALTRNSTGLG SGSSGWQAPE
QLRNERQTRA VDLFSLGCVL FFCMTGGKHP YGDNYERDVN VLNDQKDLFL IESLPEAVHL
LTGLLNPDPN LRPRAQDVMH HPLFWNSDMR LSFLRDASDR VELENREEGS QLLAALESTA
AVTLNGRWDE KLDSIFLDNI GRYRRYKFDS IRDLLRVIRN KLNHYRELPK ELQELLGSVP
EGFERYFSSR FPKLLIQVYT VLFDYCNNEE FFFKYSKTTV F
