IREH1_ARATH
ID IREH1_ARATH Reviewed; 1296 AA.
AC F4J6F6; Q8GZ40; Q9LVI5; Q9MB45;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Probable serine/threonine protein kinase IREH1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein IRE homolog 1 {ECO:0000303|PubMed:12000677};
DE Short=AtIREH1 {ECO:0000303|PubMed:17237187};
GN Name=IREH1 {ECO:0000303|PubMed:12000677};
GN OrderedLocusNames=At3g17850 {ECO:0000312|Araport:AT3G17850};
GN ORFNames=MEB5.7 {ECO:0000312|EMBL:BAB02708.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 274-1296, AND FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12000677; DOI=10.1046/j.1365-313x.2002.01290.x;
RA Oyama T., Shimura Y., Okada K.;
RT "The IRE gene encodes a protein kinase homologue and modulates root hair
RT growth in Arabidopsis.";
RL Plant J. 30:289-299(2002).
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: May be involved in root hair elongation.
CC {ECO:0000303|PubMed:12000677}.
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=BAB02708.1; 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; AB019230; BAB02708.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76015.1; -; Genomic_DNA.
DR EMBL; AK117224; BAC41900.1; -; mRNA.
DR EMBL; AB037134; BAA89784.1; -; Genomic_DNA.
DR RefSeq; NP_188412.2; NM_112666.3.
DR AlphaFoldDB; F4J6F6; -.
DR SMR; F4J6F6; -.
DR BioGRID; 6387; 1.
DR STRING; 3702.AT3G17850.1; -.
DR iPTMnet; F4J6F6; -.
DR PaxDb; F4J6F6; -.
DR PRIDE; F4J6F6; -.
DR ProMEX; F4J6F6; -.
DR ProteomicsDB; 248491; -.
DR EnsemblPlants; AT3G17850.1; AT3G17850.1; AT3G17850.
DR GeneID; 821054; -.
DR Gramene; AT3G17850.1; AT3G17850.1; AT3G17850.
DR KEGG; ath:AT3G17850; -.
DR Araport; AT3G17850; -.
DR TAIR; locus:2088515; AT3G17850.
DR eggNOG; KOG0606; Eukaryota.
DR HOGENOM; CLU_000288_130_2_1; -.
DR InParanoid; F4J6F6; -.
DR OMA; PTHYVEN; -.
DR OrthoDB; 90737at2759; -.
DR PRO; PR:F4J6F6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J6F6; baseline and differential.
DR Genevisible; F4J6F6; 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; HDA:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW ATP-binding; Growth regulation; Kinase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1296
FT /note="Probable serine/threonine protein kinase IREH1"
FT /id="PRO_0000431354"
FT DOMAIN 882..1171
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1172..1277
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 602..621
FT /note="C2H2-type; atypical"
FT /evidence="ECO:0000303|PubMed:12000677"
FT REGION 1..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1005
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 888..896
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 911
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:0007744|PubMed:19376835"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42818"
FT CONFLICT 179
FT /note="K -> R (in Ref. 3; BAC41900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1131
FT /note="P -> H (in Ref. 3; BAC41900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1296 AA; 143792 MW; 214898C3E127A6D6 CRC64;
MVFKNKLFFS SKKSGSSSPD SSNSPRSVGS NSPIRSDKKK SKSASKDEPP IPIPGFVGVG
CKQTQIKDGL KKKDGSSKGK QLSSEVQAHS IGKSNLSPSS EVKKPPPPEV KEGPAFVSPI
MASSLGLNRI KTRSGPLPQE RVFNYRNDPA TSNLSKMGAD GGDLGSGSAT SGSGSGNRKK
EAGSSKLGLE ENMDRTRPSD NKSDRDSLSP DTGPPRSLSP TLPPSGSRLQ NVASSSGTGR
SEMSSGRSGP LRNSDFCTPE NSYEWENPKE SESPRYQALL RMTSAPRKRF PGDIKSFSHE
LNSKGVRPFP LWKPRRSNNV EEVLNLIRAK FEKAKEEVNS DLAVFAADLV GVLEKNAESH
PEWEETFEDL LILARSCAMT TPGDFWLQCE GIVQDLDDRR QELPPGVLKQ LHTRMLFILT
RCTRLLQFHK ESWGEEEQVV QLRQSRVLHS IEKIPPSGAG RSYSAAKVPS TKKAYSQEQH
GLDWKEDAVV RSVPPLAPPE NYAIKESESP ANIDRMSSWK KLPSPALKTV KEAPASEEQN
DSKVEPPNIV GSRQGRDDAA VAILNFPPAK DSHEHSSKHR HNISWGYWGE QPLISEESSI
MCRICEEEVP TTHVEDHSRV CTLADKYDQK GLSVDERLMA VAGTLDKIAE TFRHKDSLAA
AESPDGMKVS NSHLTEESDV LSPRLSDWSR KGSEDMLDCF PEADNSIFMD DLRGLPLMSC
RTRFGPKSDQ GMTTSSASSM TPRSPIPTPR PDPIEQILGG KGTFHDQDDI PQMSELADIA
KCAADAIPGD DQSIPFLLSC LEDLRVVIDR RKFDALTVET FGTRIEKLIR EKYVHMCELM
DDEKVDLLST VIDEDAPLED DVVRSLRTSP VHPRDRTSID DFEIIKPISR GAFGRVFLAK
KRTTGDLFAI KVLKKADMIR KNAVESILAE RDILINVRNP FVVRFFYSFT CRDNLYLVME
YLNGGDLYSL LRNLGCLEED IVRVYIAEVV LALEYLHSEG VVHRDLKPDN LLIAHDGHIK
LTDFGLSKVG LINSTDDLAG PAVSGTSLLD EEESRLAASE EQLERRKKRS AVGTPDYLAP
EILLGTGHGA TADWWSVGII LFELIVGIPP FNAEHPQQIF DNILNRKIPW PHVPEEMSAE
AHDIIDRFLT EDPHQRLGAR GAAEVKQHIF FKDINWDTLA RQKAAFVPAS ESAIDTSYFR
SRYSWNTSDE QFFPSGEVPD YSDADSMTNS SGCSSNHHEE GEAEECEGHA EFESGIPVDY
SFSNFSFKNL SQLASINYDL LSKGWKDEPQ QIPHHK
