IRE1A_ARATH
ID IRE1A_ARATH Reviewed; 841 AA.
AC Q9C5S2; Q0WPT1; Q56WN0; Q9SHL6;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Serine/threonine-protein kinase/endoribonuclease IRE1a;
DE AltName: Full=Endoplasmic reticulum-to-nucleus signaling 1-2;
DE AltName: Full=Inositol-requiring protein 1-2;
DE Short=AtIRE1-2;
DE AltName: Full=Serine/threonine-protein kinase/endoribonuclease IRE1-2;
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=IRE1A; Synonyms=IRE1-2; OrderedLocusNames=At2g17520; ORFNames=MJB20.8;
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, AUTOPHOSPHORYLATION, MUTAGENESIS OF
RP LYS-442, SUBCELLULAR LOCATION, AND TISSUE 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], FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF
RP LYS-442, 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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 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, 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 [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [11]
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.
CC {ECO:0000269|PubMed:11706177, ECO:0000269|PubMed:12020828,
CC ECO:0000269|PubMed:21914012, ECO:0000269|PubMed:22355548,
CC ECO:0000269|PubMed:22359644}.
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.
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 -!- TISSUE SPECIFICITY: Ubiquitous. Detected in the vascular bundles of
CC young plants, leaves, roots, seedlings and in the receptacles of
CC flowers and vascular bundles of the petals.
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.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype but shows enhanced
CC susceptibility to a bacterial pathogen and deficiency in establishing
CC systemic acquired resistance (SAR). Ire1a and ire1b double mutant is
CC more sensitive to the ER stress inducer tunicamycin than the wild-type
CC 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 ---------------------------------------------------------------------------
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; AB049937; BAB63367.1; -; mRNA.
DR EMBL; AF308596; AAK15470.1; -; mRNA.
DR EMBL; AC007584; AAD32909.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06640.1; -; Genomic_DNA.
DR EMBL; AK222006; BAD94631.1; -; mRNA.
DR EMBL; AK228980; BAF00868.1; -; mRNA.
DR PIR; B84553; B84553.
DR RefSeq; NP_565419.1; NM_127306.4.
DR AlphaFoldDB; Q9C5S2; -.
DR SMR; Q9C5S2; -.
DR BioGRID; 1615; 3.
DR STRING; 3702.AT2G17520.1; -.
DR PaxDb; Q9C5S2; -.
DR PRIDE; Q9C5S2; -.
DR ProteomicsDB; 232281; -.
DR EnsemblPlants; AT2G17520.1; AT2G17520.1; AT2G17520.
DR GeneID; 816258; -.
DR Gramene; AT2G17520.1; AT2G17520.1; AT2G17520.
DR KEGG; ath:AT2G17520; -.
DR Araport; AT2G17520; -.
DR TAIR; locus:2053928; AT2G17520.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_004875_3_1_1; -.
DR InParanoid; Q9C5S2; -.
DR OMA; ITGCKHP; -.
DR OrthoDB; 1019877at2759; -.
DR PhylomeDB; Q9C5S2; -.
DR PRO; PR:Q9C5S2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9C5S2; baseline and differential.
DR Genevisible; Q9C5S2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:TAIR.
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:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:endoribonuclease activity; IMP:TAIR.
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:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IGI:TAIR.
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:0006379; P:mRNA cleavage; IDA:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:TAIR.
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 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; IPR008271; Ser/Thr_kinase_AS.
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; SSF56112; SSF56112; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Immunity; Kinase; Magnesium; Membrane; Metal-binding;
KW mRNA processing; mRNA splicing; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW Unfolded protein response.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..841
FT /note="Serine/threonine-protein kinase/endoribonuclease
FT IRE1a"
FT /id="PRO_0000422137"
FT TOPO_DOM 31..323
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..841
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 414..704
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 707..838
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 352..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 570
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 420..428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 442
FT /note="K->A: Loss of autophosphorylation activity."
FT /evidence="ECO:0000269|PubMed:11706177,
FT ECO:0000269|PubMed:12020828"
FT CONFLICT 39
FT /note="P -> T (in Ref. 5; BAF00868)"
FT /evidence="ECO:0000305"
FT CONFLICT 780
FT /note="N -> S (in Ref. 5; BAF00868)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="N -> D (in Ref. 5; BAD94631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 841 AA; 95138 MW; B3662AB218C31013 CRC64;
MPPRCPFLRH LFFLLLLLSP WIMSPCGGAA DDVTYPIVPS SPGRRSILQI RREPPTEPNT
KLVVDRDGKV FLKQQPKETP YWSFSTGSPM HSLYQAPANN NTENATEITR PHIIVEYLNN
SKAATTVDGY HNWTVQEFFR QKPLVTDDGV TLGSETTSAY LVDGRSGRLI HVYKSTGDTK
ITNALVKPAS TEDFVNEPLL IRRTDSKLEH FSKTTGKLVW NLTVSHFRAA LLCDPVFNSG
YDLGPKLQTG IYMPLLCGSQ IDVRGPEIVI RVLHDQPMNV KMLPSPSLNH FESENSIMPF
GKARESRKLQ EQHKQKYTYL FGQWSPVKLL APLVLLGVVV SVFIKKFSSR GSDVSLKAGP
SKKKKNRKSA KDTNRQSVPR GQDQFELIEG GQMLLGFNNF QSGATDGRKI GKLFLSSKEI
AKGSNGTVVF EGIYEGRPVA VKRLVRSHHE VAFKEIQNLI ASDQHTNIIR WYGVEYDQDF
VYLSLERCTC SLDDLIKSYL EFSMTKVLEN NDSTEGVAAY KIQLDSLEGV IKGNNFWKVG
GHPSPLMLKL MRDIVCGIVH LHELGIVHRD LKPQNVLISK DMTLSAKLSD MGISKRMSRD
MSSLGHLATG SGSSGWQAPE QLLQGRQTRA VDMFSLGCVI FYTITGCKHP FGDDLERDVN
IVKNKVDLFL VEHVPEASDL ISRLLNPDPD LRPSATEVLL HPMFWNSEMR LSFLRDASDR
VELENREADS EILKAMESTA PVAIGGKWDE KLEPVFITNI GRYRRYKYDS IRDLLRVIRN
KLNHHRELPP EIQELVGTVP EGFDEYFAVR FPKLLIEVYR VISLHCREEE VFRKYFKCDI
I
