ID IRE1L_ARATH Reviewed; 554 AA.
AC Q9SF12;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Inactive serine/threonine-protein kinase/endoribonuclease IRE1-like;
DE AltName: Full=Endoplasmic reticulum-to-nucleus signaling 1-like;
DE AltName: Full=Inositol-requiring protein 1-like;
DE Flags: Precursor;
GN OrderedLocusNames=At3g11870; ORFNames=F26K24.16;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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).
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. As the kinase activity is required for activation of the
CC endoribonuclease domain, the protein could be inactive.
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; AC016795; AAF23203.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75111.1; -; Genomic_DNA.
DR RefSeq; NP_187793.1; NM_112020.1.
DR AlphaFoldDB; Q9SF12; -.
DR SMR; Q9SF12; -.
DR STRING; 3702.Q9SF12; -.
DR PaxDb; 3702-AT3G11870-1; -.
DR EnsemblPlants; AT3G11870.1; AT3G11870.1; AT3G11870.
DR GeneID; 820360; -.
DR Gramene; AT3G11870.1; AT3G11870.1; AT3G11870.
DR KEGG; ath:AT3G11870; -.
DR Araport; AT3G11870; -.
DR TAIR; AT3G11870; IRE1C.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_004875_3_2_1; -.
DR InParanoid; Q9SF12; -.
DR OMA; MEIYAFI; -.
DR OrthoDB; 694853at2759; -.
DR PhylomeDB; Q9SF12; -.
DR PRO; PR:Q9SF12; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF12; baseline and differential.
DR Genevisible; Q9SF12; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR Gene3D; 1.20.1440.180; KEN domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR13954; IRE1-RELATED; 1.
DR PANTHER; PTHR13954:SF6; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00580; PUG; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..554
FT /note="Inactive serine/threonine-protein
FT kinase/endoribonuclease IRE1-like"
FT /id="PRO_0000422139"
FT DOMAIN 121..408
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 411..554
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 36..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 554 AA; 63260 MW; 3543FFF1A6651683 CRC64;
MWLLAISLVG LLVVVVCVFL RFSKDKGLDG IVNEKKRDKN SAPRVSASGE DGTKNEQVEK
KSDPSGGLGE ENEKTNSESK VLSVPSDQNI NKTLPVMLPS LELRKYDENE TPGKVVNRRL
LVSTNEMKYG RNGYEVFQGV YGRRSSVAVK CLDLAHTTEA FIQNEIDNHC LCDDHSNIIR
FHGLEQDQSF AYICLEPWKC SLDDLIKLSV RRTKRDTQAV APVDDLEKVM KRIKFWKEKG
KPLPLTPMLK LMRDVVCGLA HLHKLKTIHR NLNPQNVLII VKDMTLTAKI SDMSLSKHLG
GKKSSYKHLA TCSGSSGWQA PEQLNKDKKK KEDFPADMFN FGCLLHYAVM GTHPFGSPSE
RDTNIKTNNK TNLSLVTNLE AINLIEQLLN YKPDLRPSAT QVLLHPLFWD SEKRLFFLRE
ASDRIELDIT MWGDLNKTIA PRVLGESKDW ASKLGKTFIT HIENLAQAQP GQESRQYNRS
YKYWSLRHLL RLIRNILSHH REILDDPKIK EMVGKVPEGL DIFFTARFPN LMMEIYAFIS
MHCKGEEAFE KYFN
//
