IRE1_ORYSJ
ID IRE1_ORYSJ Reviewed; 893 AA.
AC Q7XIT1; Q9FS17;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine/threonine-protein kinase/endoribonuclease IRE1 {ECO:0000305};
DE AltName: Full=Endoplasmic reticulum-to-nucleus signaling 1 {ECO:0000305};
DE AltName: Full=Inositol-requiring protein 1 {ECO:0000305};
DE Short=OsIRE1 {ECO:0000303|PubMed:12040100};
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=IRE1 {ECO:0000303|PubMed:12040100};
GN OrderedLocusNames=Os07g0471000 {ECO:0000312|EMBL:BAF21520.1},
GN LOC_Os07g28820 {ECO:0000305};
GN ORFNames=OJ1103_E04.109 {ECO:0000312|EMBL:BAC79579.1},
GN OsJ_24190 {ECO:0000312|EMBL:EEE67138.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-519.
RX PubMed=12040100; DOI=10.1093/pcp/pcf063;
RA Okushima Y., Koizumi N., Yamaguchi Y., Kimata Y., Kohno K., Sano H.;
RT "Isolation and characterization of a putative transducer of endoplasmic
RT reticulum stress in Oryza sativa.";
RL Plant Cell Physiol. 43:532-539(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION.
RX PubMed=22199238; DOI=10.1093/mp/ssr115;
RA Lu S.J., Yang Z.T., Sun L., Sun L., Song Z.T., Liu J.X.;
RT "Conservation of IRE1-regulated bZIP74 mRNA unconventional splicing in rice
RT (Oryza sativa L.) involved in ER stress responses.";
RL Mol. Plant 5:504-514(2012).
RN [8]
RP FUNCTION.
RX PubMed=22050533; DOI=10.1111/j.1365-313x.2011.04844.x;
RA Hayashi S., Wakasa Y., Takahashi H., Kawakatsu T., Takaiwa F.;
RT "Signal transduction by IRE1-mediated splicing of bZIP50 and other stress
RT sensors in the endoplasmic reticulum stress response of rice.";
RL Plant J. 69:946-956(2012).
CC -!- FUNCTION: Involved in endoplasmic reticulum (ER) stress response.
CC Senses unfolded proteins in the lumen of the ER via its N-terminal
CC domain which leads to enzyme auto-activation. The active
CC endoribonuclease domain splices bZIP50 mRNA to generate a new C-
CC terminus, converting it into a potent unfolded-protein response (UPR)
CC transcriptional activator, which then induces transcription of UPR
CC target genes, such as luminal-binding protein (BiP) chaperones.
CC {ECO:0000269|PubMed:22050533, ECO:0000269|PubMed:22199238}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
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:0000250|UniProtKB:Q9C5S2}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, nodes, internodes, leaf
CC sheaths, leaf blades, young ears and mature ears.
CC {ECO:0000269|PubMed:12040100}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:12040100}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB031396; BAB20385.1; -; mRNA.
DR EMBL; AP003806; BAC79579.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21520.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01421.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE67138.1; -; Genomic_DNA.
DR EMBL; AK068617; BAG90994.1; -; mRNA.
DR RefSeq; XP_015647364.1; XM_015791878.1.
DR AlphaFoldDB; Q7XIT1; -.
DR SMR; Q7XIT1; -.
DR STRING; 4530.OS07T0471000-01; -.
DR PaxDb; Q7XIT1; -.
DR PRIDE; Q7XIT1; -.
DR EnsemblPlants; Os07t0471000-01; Os07t0471000-01; Os07g0471000.
DR GeneID; 4343198; -.
DR Gramene; Os07t0471000-01; Os07t0471000-01; Os07g0471000.
DR KEGG; osa:4343198; -.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_004875_3_1_1; -.
DR InParanoid; Q7XIT1; -.
DR OMA; ANIMQNA; -.
DR OrthoDB; 1019877at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; 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: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:0036498; P:IRE1-mediated unfolded protein response; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; Kinase; Membrane; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..893
FT /note="Serine/threonine-protein kinase/endoribonuclease
FT IRE1"
FT /evidence="ECO:0000255"
FT /id="PRO_5008177494"
FT TOPO_DOM 20..379
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 380..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..893
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 491..759
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 762..890
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 451..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 625
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 497..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 519
FT /note="K->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:22050533"
SQ SEQUENCE 893 AA; 99088 MW; E32EC6BFC5163255 CRC64;
MRSLRRVLLQ LVLLAGVAFR GVRFDDAADA AAAAQGSSDL FELPSPSPTL ALPGGGDEGA
STEIIAAPWP GRHGLFTPPR STSQPARAVV QPAADFGSQL QFYDNGTIQL VDLLSKLPRW
QFSTGPPLSK HITTSKPDLN YVIYLDGSET SDLIEVHNGS GVRLPWKLEE FIAETPYIRD
SFVTIGSKVS TTFVVNADSG EIIYKHSLPV ALNEVGGPLV EEIPSKLDAA RSGTSANIIV
VVRTDYSISA SDLGEHLFNW TRTSFTANYY ARYGHQDMLA QSSCLRGNIP CIRTEGPPIK
LYLPDSSSDN AIVLRPVNEV SAVDALEPLL PPKKLPQPAG ESNVALDSAQ NQTADIALGH
FVPADTELTN SVTKFSYRWL FPTFLMLLIM ACLVKLADAS KYCRQFVIRF LKPFMRDEKL
MDPRGKSEGT SKRRKARKKD GLINSTQIFS ASDKEGNGTG GSTEAQSNKA HDSTNVELPN
GLNGRQIGKL CVYSKEIGKG SNGTVVFEGS YGGREVAVKR LLRSHNDIAS KEIENLIASD
QDPNIVRMYG FEQDNDFVYI SLERCRCSLA DLIQLHSVPP FSNTKGTDIE LWRQDGLPSA
QLLKLMRDVV AGIVHLHSLG IIHRDLKPQN VLISKEGPLR AKLSDMGISK RLQEDMTSVS
HHGTGFGSSG WQAPEQLRHG RQTRAIDLFS LGCLIFYCIT KGKHPFGEYY ERDMKIINNQ
FDLFIVDHIP EAVHLISQLL DPDPEKRPTA VYVMHHPFFW SPELCLSFLR DTSDRIEKTS
ETDLIDALEG INVEAFGKNW GEKLDAALLA DMGRYRKYSF ESTRDLLRLI RNKSGHYREF
SDDLKELLGS LPEGFVQYFS SRFPKLLIKV YEVMSEHCKD EEAFSKYFLG SSA
