IRE3_ARATH
ID IRE3_ARATH Reviewed; 1235 AA.
AC F4HYG2; C0Z2M9; Q94F38; Q9LP76;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable serine/threonine protein kinase IRE3 {ECO:0000305};
DE Short=AtIRE3 {ECO:0000303|PubMed:17237187};
DE EC=2.7.11.1 {ECO:0000305};
GN Name=IRE3 {ECO:0000303|PubMed:17237187};
GN OrderedLocusNames=At1g48490 {ECO:0000312|Araport:AT1G48490};
GN ORFNames=T1N15.10 {ECO:0000312|EMBL:AAF79714.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 297-1235.
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 [5]
RP GENE FAMILY.
RX PubMed=17237187; DOI=10.1104/pp.106.092494;
RA Pislariu C.I., Dickstein R.;
RT "An IRE-like AGC kinase gene, MtIRE, has unique expression in the invasion
RT zone of developing root nodules in Medicago truncatula.";
RL Plant Physiol. 144:682-694(2007).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79714.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC020889; AAF79714.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32299.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32300.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32301.1; -; Genomic_DNA.
DR EMBL; AK318843; BAH56958.1; -; mRNA.
DR EMBL; AF385743; AAK60333.1; -; mRNA.
DR EMBL; BT002248; AAN72259.1; -; mRNA.
DR RefSeq; NP_001031155.4; NM_001036078.4.
DR RefSeq; NP_001154409.1; NM_001160937.2.
DR RefSeq; NP_564529.4; NM_103745.7.
DR AlphaFoldDB; F4HYG2; -.
DR SMR; F4HYG2; -.
DR STRING; 3702.AT1G48490.2; -.
DR iPTMnet; F4HYG2; -.
DR PaxDb; F4HYG2; -.
DR PRIDE; F4HYG2; -.
DR ProteomicsDB; 232227; -.
DR EnsemblPlants; AT1G48490.1; AT1G48490.1; AT1G48490.
DR EnsemblPlants; AT1G48490.2; AT1G48490.2; AT1G48490.
DR EnsemblPlants; AT1G48490.3; AT1G48490.3; AT1G48490.
DR GeneID; 841270; -.
DR Gramene; AT1G48490.1; AT1G48490.1; AT1G48490.
DR Gramene; AT1G48490.2; AT1G48490.2; AT1G48490.
DR Gramene; AT1G48490.3; AT1G48490.3; AT1G48490.
DR KEGG; ath:AT1G48490; -.
DR Araport; AT1G48490; -.
DR TAIR; locus:2198012; AT1G48490.
DR eggNOG; KOG0606; Eukaryota.
DR HOGENOM; CLU_000288_130_2_1; -.
DR InParanoid; F4HYG2; -.
DR OMA; NDHNEEI; -.
DR PRO; PR:F4HYG2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HYG2; baseline and differential.
DR Genevisible; F4HYG2; AT.
DR GO; GO:0035618; C:root hair; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS: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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1235
FT /note="Probable serine/threonine protein kinase IRE3"
FT /id="PRO_0000431355"
FT DOMAIN 828..1111
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1112..1216
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 552..571
FT /note="C2H2-type; atypical"
FT /evidence="ECO:0000250|UniProtKB:Q9LE81"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 951
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 834..842
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 857
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4J6F6"
FT MOD_RES 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42818"
SQ SEQUENCE 1235 AA; 137349 MW; 89C298EC25FF3D1F CRC64;
MVFKSKLFFS SKKSRSSSPS SSNSPRSVGS DSPIRSDKKK PKSNSKEETR SPNTKKHVSA
KGKEASLEVH SSSPGKSNSS SSGSEAKKPI TETPATSDVK EESPASVSPI MASSLGLNRI
KTRSGPLPQE SFFSFENDYA IPVLPCYKLS KLDTGKKEAG SSKVDIGPLR SSNPALLASG
TGQFKVSPTI SGPEGSAEVC TPENSYDLDD PKESDSPRYQ ALLRMTSAPR KRFPGDIKSF
SHELNSKGVR PFPLWKPRRL NNLEDILNLI RTKFDKAKEE VNSDLFAFGG DLLDIYDKNK
ESHPELLVTI EDLLVLAKTC AKTTSKEFWL QCEGIVQDLD DRRQELPPGV LKQLHTRMLF
ILTRCTRLLQ FHKESWGQEE DAVQLRQSGV LHSADKRDPT GEVRDGKGSS TANALKVPST
KKAYSQEQRG LNWIEGFFVR PAPLSSPYNE TSKDSESPAN IDKMSSWKRL PSPASKGVQE
AAVSKEQNDR KVEPPQVVKK LVAISDDMAV AKLPEVSSAK ASQEHMSKNR HNISWGYWGH
QSCISEESSI ICRICEEEIP TTHVEDHSRI CALADKYDQK GVGVDERLMA VAVTLEKITD
NVIQKDSLAA VESPEGMKIS NASLTEELDV LSPKLSDWSR RGSEDMLDCF PETDNSVFMD
DMGCLPSMSC RTRFGPKSDQ GMATSSAGSM TPRSPIPTPR PDPIELLLEG KGTFHDQDDF
PQMSELADIA RCAANAIPVD DQSIQLLLSC LEDLRVVIDR RKFDALIVET FGTRIEKLIQ
EKYLQLCELM DDEKGTIIDE DAPLEDDVVR SLRTSPVHLR DRISIDDFEV MKSISRGAFG
HVILARKNTT GDLFAIKVLR KADMIRKNAV ESILAERDIL INARNPFVVR FFYSFTCSEN
LYLVMEYLNG GDFYSMLRKI GCLDEANARV YIAEVVLALE YLHSEGVVHR DLKPDNLLIA
HDGHVKLTDF GLSKVGLINN TDDLSGPVSS ATSLLVEEKP KLPTLDHKRS AVGTPDYLAP
EILLGTGHGA TADWWSVGII LYEFLVGIPP FNADHPQQIF DNILNRNIQW PPVPEDMSHE
ARDLIDRLLT EDPHQRLGAR GAAEVKQHSF FKDIDWNTLA QQKAAFVPDS ENAFDTSYFQ
SRYSWNYSGE RCFPTNENED SSEGDSLCGS SGRLSNHHDE GVDIPCGPAE FETSVSENYP
FDNFSFKNLS QLAYINYNLM SKGHKDETQP SLQRR
