IRE_ARATH
ID IRE_ARATH Reviewed; 1168 AA.
AC Q9LE81;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable serine/threonine protein kinase IRE {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein INCOMPLETE ROOT HAIR ELONGATION {ECO:0000303|PubMed:12000677};
DE Short=AtIRE {ECO:0000303|PubMed:17237187};
GN Name=IRE {ECO:0000303|PubMed:12000677};
GN OrderedLocusNames=At5g62310 {ECO:0000312|Araport:AT5G62310};
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [4]
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 -!- FUNCTION: Modulates root tip growth. May play a common role in the tip
CC growth of plant cells. {ECO:0000269|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 -!- TISSUE SPECIFICITY: Highly expressed in roots, elongating root hair
CC cells and pollen grains. {ECO:0000269|PubMed:12000677}.
CC -!- DISRUPTION PHENOTYPE: Reduced root hair length.
CC {ECO:0000269|PubMed:12000677}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AB037133; BAA89783.1; -; Genomic_DNA.
DR EMBL; AB019235; BAA97195.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97595.1; -; Genomic_DNA.
DR RefSeq; NP_201037.1; NM_125625.3.
DR AlphaFoldDB; Q9LE81; -.
DR SMR; Q9LE81; -.
DR STRING; 3702.AT5G62310.1; -.
DR iPTMnet; Q9LE81; -.
DR PaxDb; Q9LE81; -.
DR PRIDE; Q9LE81; -.
DR ProteomicsDB; 248492; -.
DR EnsemblPlants; AT5G62310.1; AT5G62310.1; AT5G62310.
DR GeneID; 836352; -.
DR Gramene; AT5G62310.1; AT5G62310.1; AT5G62310.
DR KEGG; ath:AT5G62310; -.
DR Araport; AT5G62310; -.
DR TAIR; locus:2167953; AT5G62310.
DR eggNOG; KOG0606; Eukaryota.
DR HOGENOM; CLU_000288_130_2_1; -.
DR InParanoid; Q9LE81; -.
DR OMA; ELWVKCE; -.
DR OrthoDB; 90737at2759; -.
DR PhylomeDB; Q9LE81; -.
DR PRO; PR:Q9LE81; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LE81; baseline and differential.
DR Genevisible; Q9LE81; AT.
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 GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
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; Growth regulation; Kinase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1168
FT /note="Probable serine/threonine protein kinase IRE"
FT /id="PRO_0000431353"
FT DOMAIN 754..1043
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1044..1144
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 488..507
FT /note="C2H2-type; atypical"
FT /evidence="ECO:0000303|PubMed:12000677"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 877
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 760..768
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 783
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1168 AA; 130147 MW; 072E1E696314DF71 CRC64;
MSTTEPSPEN DRDPQPTTIS TPTSTNAKLL KKIPAIPFRH SDKEGEDEQA KTDEVTTELA
GEGPMSHDSP EILAPSSLGL NHIRTKSSPA PSPLRFSSAT PLISPGQDDK DVAKEKPRVG
VVDARADARA RWPIPPHQPD QGKKVQWSQS KSQRVPANSN PGVESTHVGL AKETQSPRFQ
AILRVTSGRK KKAHDIKSFS HELNSKGVRP FPVWRSRAVG HMEEIMAAIR TKFDKQKEDV
DADLGVFAGY LVTTLESTPE SNKELRVGLE DLLVEARQCA TMPASEFWLK CEGIVQKLDD
KRQELPMGGL KQAHNRLLFI LTRCNRLVQF RKESGYVEEH ILGMHQLSDL GVYPEQMVEI
SRQQDLLREK EIQKINEKQN LAGKQDDQNS NSGADGVEVN TARSTDSTSS NFRMSSWKKL
PSAAEKNRSL NNTPKAKGES KIQPKVYGDE NAENLHSPSG QPASADRSAL WGFWADHQCV
TYDNSMICRI CEVEIPVVHV EEHSRICTIA DRCDLKGINV NLRLERVAES LEKILESWTP
KSSVTPRAVA DSARLSNSSR QEDLDEISQR CSDDMLDCVP RSQNTFSLDE LNILNEMSMT
NGTKDSSAGS LTPPSPATPR NSQVDLLLSG RKTISELENY QQINKLLDIA RSVANVNVCG
YSSLDFMIEQ LDELKYVIQD RKADALVVET FGRRIEKLLQ EKYIELCGLI DDEKVDSSNA
MPDEESSADE DTVRSLRASP LNPRAKDRTS IEDFEIIKPI SRGAFGRVFL AKKRATGDLF
AIKVLKKADM IRKNAVESIL AERNILISVR NPFVVRFFYS FTCRENLYLV MEYLNGGDLF
SLLRNLGCLD EDMARIYIAE VVLALEYLHS VNIIHRDLKP DNLLINQDGH IKLTDFGLSK
VGLINSTDDL SGESSLGNSG FFAEDGSKAQ HSQGKDSRKK HAVVGTPDYL APEILLGMGH
GKTADWWSVG VILFEVLVGI PPFNAETPQQ IFENIINRDI PWPNVPEEIS YEAHDLINKL
LTENPVQRLG ATGAGEVKQH HFFKDINWDT LARQKAMFVP SAEPQDTSYF MSRYIWNPED
ENVHGGSDFD DLTDTCSSSS FNTQEEDGDE CGSLAEFGNG PNLAVKYSFS NFSFKNLSQL
ASINYDLVLK NAKESVEASN QSAPRPET
