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 02-JUN-2021, entry version 140. 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}; 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; 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 SMR; Q93VJ2; -. DR BioGRID; 17782; 2. DR STRING; 3702.AT5G24360.2; -. DR iPTMnet; Q93VJ2; -. DR PaxDb; Q93VJ2; -. DR PRIDE; 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; WDEKMET; -. 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:UniProtKB-EC. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0106311; F:protein threonine kinase activity; IEA:UniProtKB-EC. 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: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; 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 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 NP_BIND 465..473 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" 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 487 FT /note="ATP" 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 //