IRK_ARATH
ID IRK_ARATH Reviewed; 964 AA.
AC Q9LY03; Q8VYT7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase IRK {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Inflorescence and root apices receptor-like kinase {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=IRK {ECO:0000303|Ref.1};
GN OrderedLocusNames=At3g56370 {ECO:0000312|Araport:AT3G56370};
GN ORFNames=T5P19.20 {ECO:0000312|EMBL:CAB88040.1};
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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX DOI=10.5511/plantbiotechnology.19.113;
RA Kanamoto H., Hattan J., Takemura M., Yokota A., Kouchi T.;
RT "Molecular cloning and characterization of a gene coding for a putative
RT receptor-like protein kinase with a leucine-rich repeat expressed in
RT inflorescence and root apices from Arabidopsis.";
RL Plant Biotechnol. 19:113-120(2002).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [6]
RP INTERACTION WITH IRKI.
RX PubMed=15618632; DOI=10.1271/bbb.68.2598;
RA Hattan J., Kanamoto H., Takemura M., Yokota A., Kohchi T.;
RT "Molecular characterization of the cytoplasmic interacting protein of the
RT receptor kinase IRK expressed in the inflorescence and root apices of
RT Arabidopsis.";
RL Biosci. Biotechnol. Biochem. 68:2598-2606(2004).
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: Interacts with IRKI. {ECO:0000269|PubMed:15618632}.
CC -!- INTERACTION:
CC Q9LY03; Q8W4S5: At5g63710; NbExp=2; IntAct=EBI-1392485, EBI-16934827;
CC Q9LY03; Q9LXU9: IRKI; NbExp=2; IntAct=EBI-1392485, EBI-1392508;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.1}; Single-pass
CC type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in root tips, shoot apices and
CC developing flowers. {ECO:0000269|Ref.1}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|Ref.1}.
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; AB076906; BAB85646.1; -; mRNA.
DR EMBL; AB076907; BAB85647.1; -; Genomic_DNA.
DR EMBL; AL163972; CAB88040.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79514.1; -; Genomic_DNA.
DR EMBL; AY070033; AAL49790.1; -; mRNA.
DR EMBL; FJ708741; ACN59335.1; -; mRNA.
DR PIR; T49038; T49038.
DR RefSeq; NP_191196.1; NM_115495.4.
DR AlphaFoldDB; Q9LY03; -.
DR SMR; Q9LY03; -.
DR IntAct; Q9LY03; 30.
DR STRING; 3702.AT3G56370.1; -.
DR iPTMnet; Q9LY03; -.
DR PaxDb; Q9LY03; -.
DR PRIDE; Q9LY03; -.
DR ProteomicsDB; 247045; -.
DR EnsemblPlants; AT3G56370.1; AT3G56370.1; AT3G56370.
DR GeneID; 824804; -.
DR Gramene; AT3G56370.1; AT3G56370.1; AT3G56370.
DR KEGG; ath:AT3G56370; -.
DR Araport; AT3G56370; -.
DR TAIR; locus:2102499; AT3G56370.
DR eggNOG; ENOG502QU7G; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9LY03; -.
DR OMA; WNDRFNI; -.
DR OrthoDB; 151146at2759; -.
DR PhylomeDB; Q9LY03; -.
DR PRO; PR:Q9LY03; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY03; baseline and differential.
DR Genevisible; Q9LY03; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP 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; IEA:UniProtKB-EC.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0051302; P:regulation of cell division; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 5.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 16.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..964
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase IRK"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433166"
FT TOPO_DOM 21..603
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..964
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 92..116
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 117..141
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 143..166
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 168..190
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 191..214
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 215..238
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 240..261
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 263..286
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 287..310
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 312..334
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 335..358
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 375..399
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 400..423
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 425..447
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 448..471
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 472..495
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 496..519
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 521..544
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT DOMAIN 678..951
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 684..692
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 27
FT /note="D -> G (in Ref. 4; AAL49790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 964 AA; 103854 MW; 3A3D17F5A7C26FFC CRC64;
MYKALIFTVL LVSAVAPVRS LDPPLNDDVL GLIVFKADLR DPEQKLASWN EDDYTPCSWN
GVKCHPRTNR VTELNLDGFS LSGRIGRGLL QLQFLHKLSL SNNNLTGIIN PNMLLSLVNL
KVVDLSSNGL SGSLPDEFFR QCGSLRVLSL AKNKLTGKIP VSISSCSSLA ALNLSSNGFS
GSMPLGIWSL NTLRSLDLSR NELEGEFPEK IDRLNNLRAL DLSRNRLSGP IPSEIGSCML
LKTIDLSENS LSGSLPNTFQ QLSLCYSLNL GKNALEGEVP KWIGEMRSLE TLDLSMNKFS
GQVPDSIGNL LALKVLNFSG NGLIGSLPVS TANCINLLAL DLSGNSLTGK LPMWLFQDGS
RDVSALKNDN STGGIKKIQV LDLSHNAFSG EIGAGLGDLR DLEGLHLSRN SLTGPIPSTI
GELKHLSVLD VSHNQLNGMI PRETGGAVSL EELRLENNLL EGNIPSSIKN CSSLRSLILS
HNKLLGSIPP ELAKLTRLEE VDLSFNELAG TLPKQLANLG YLHTFNISHN HLFGELPAGG
IFNGLSPSSV SGNPGICGAV VNKSCPAISP KPIVLNPNAT FDPYNGEIVP PGAGHKRILL
SISSLIAISA AAAIVVGVIA ITVLNLRVRA STVSRSAVPL TFSGGDDFSR SPTTDSNSGK
LVMFSGEPDF STGTHALLNK DCELGRGGFG AVYRTVIRDG YPVAIKKLTV SSLVKSQDEF
EREVKKLGKL RHSNLVKLEG YYWTTSLQLL IYEFLSGGSL YKQLHEAPGG NSSLSWNDRF
NIILGTAKCL AYLHQSNIIH YNIKSSNVLL DSSGEPKVGD YGLARLLPML DRYVLSSKIQ
SALGYMAPEF ACRTVKITEK CDVYGFGVLV LEVVTGKKPV EYMEDDVVVL CDMVREALED
GRADECIDPR LQGKFPVEEA VAVIKLGLIC TSQVPSSRPH MGEAVNILRM IRCPSGSSDE
LGSS
