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 08-MAY-2019, entry version 129. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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.127.3.949; RA Koizumi N., Martinez I.M., Kimata Y., Kohno K., Sano H., RA Chrispeels M.J.; RT "Molecular characterization of two Arabidopsis Ire1 homologs, RT endoplasmic 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 RT in 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. RT Sequence features of the regions of 1,081,958 bp covered by seventeen RT physically 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 RT reference 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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- RT like 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., RA 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., RA Bassham D.C.; RT "Degradation of the endoplasmic reticulum by autophagy during RT endoplasmic 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 RT in 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 RT stress 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 CC to generate a new C-terminus, converting it into a potent CC unfolded-protein response transcriptional activator which then CC induces transcription of UPR target genes. Involved in organ CC growth regulation. Plays a role in plant immunity and abiotic CC stress responses. Required for ER stress-induced autophagy. CC {ECO:0000269|PubMed:11706177, ECO:0000269|PubMed:21482766, CC ECO:0000269|PubMed:21914012, ECO:0000269|PubMed:22355548, CC ECO:0000269|PubMed:22359644, ECO:0000269|PubMed:22701744, CC 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, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC 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 CC the 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, CC at leaf margins where vascular bundles end, in the anthers before CC pollen is formed and in the ovules at a very early stage of CC development. There is no expression in more mature embryos. Also CC strongly expressed in the cotyledons immediately after germination CC but not later on. {ECO:0000269|PubMed:11706177, CC ECO:0000269|PubMed:12020828}. CC -!- INDUCTION: By ER stress inducer tunicamycin, by salicylic acid CC (SA) and by bacterial pathogen infection. CC {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 CC the wild-type and is enable to give rise to the spliced bZIP60 CC mRNA form (PubMed:22355548). Ire1a and ire1b double mutant CC displays short roots and a ER stress-sensitive phenotype CC (PubMed:21914012). {ECO:0000269|PubMed:21482766, CC ECO:0000269|PubMed:21914012, ECO:0000269|PubMed:22355548, CC ECO:0000269|PubMed:22359644}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein 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 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 eggNOG; COG0515; LUCA. DR HOGENOM; HOG000084349; -. DR InParanoid; Q93VJ2; -. DR OMA; WDEKMET; -. DR OrthoDB; 1019877at2759; -. 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:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. 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:0004672; F:protein kinase activity; IBA:GO_Central. 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:0009816; P:defense response to bacterium, incompatible interaction; IMP:UniProtKB. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IBA:GO_Central. 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; IPR018997; PUB_domain. 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; SM00580; PUG; 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; Complete proteome; KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; KW Immunity; Kinase; Magnesium; Membrane; Metal-binding; mRNA processing; KW mRNA splicing; Multifunctional enzyme; Nucleotide-binding; KW Reference proteome; Serine/threonine-protein kinase; Signal; KW Transcription; Transcription regulation; Transferase; Transmembrane; KW Transmembrane helix; Unfolded protein response. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 881 Serine/threonine-protein FT kinase/endoribonuclease IRE1b. FT /FTId=PRO_0000422138. FT TOPO_DOM 22 357 Lumenal. {ECO:0000255}. FT TRANSMEM 358 378 Helical. {ECO:0000255}. FT TOPO_DOM 379 881 Cytoplasmic. {ECO:0000255}. FT DOMAIN 459 744 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT DOMAIN 747 878 KEN. {ECO:0000255|PROSITE- FT ProRule:PRU00725}. FT NP_BIND 465 473 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT REGION 481 502 ATP selon article. FT COMPBIAS 401 407 Poly-Lys. FT ACT_SITE 608 608 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 487 487 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT CARBOHYD 115 115 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CONFLICT 647 647 T -> I (in Ref. 1; BAB63366). FT {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 //