IMK3_ARATH
ID IMK3_ARATH Reviewed; 784 AA.
AC C0LGP9; F4IY70; Q56WQ4; Q8GWS6; Q9LYN1;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Probable leucine-rich repeat receptor-like protein kinase IMK3;
DE EC=2.7.11.1;
DE AltName: Full=Protein INFLORESCENCE MERISTEM RECEPTOR-LIKE KINASE 3;
DE AltName: Full=Protein MERISTEMATIC RECEPTOR-LIKE KINASE;
DE Flags: Precursor;
GN Name=IMK3; Synonyms=MRLK; OrderedLocusNames=At3g56100; ORFNames=F18O21.60;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 562-784.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 562-784.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-784.
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 [7]
RP TISSUE SPECIFICITY.
RA Takemura M., Kohchi T., Kanamoto H., Asai T., Nemoto K., Yokota A.;
RT "Structural and functional analysis of the receptor-like kinase genes
RT expressed at Arabidopsis inflorescence.";
RL (In) Proceedings of the 9th international conference on Arabidopsis
RL research, abstract#501708527, Madison (1998).
RN [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RA Takemura M., Kanamoto H., Hasegawa M., Yokota A., Kohchi T.;
RT "Analysis of the receptor-like kinase gene expressed in the meristems.";
RL (In) Proceedings of the 10th international conference on Arabidopsis
RL research, abstract#12-15, Melbourne (1999).
RN [9]
RP FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH AGL24, AND ACTIVITY.
RA Takemura M., Tani E., Takeda Y., Yokota A., Kohchi T.;
RT "Functional analysis of the receptor-like kinase gene expressed in both
RT shoot and root apical meristems.";
RL (In) Proceedings of the 11th international conference on Arabidopsis
RL research, abstract#295, Madison (2000).
CC -!- FUNCTION: Can phosphorylate AGL24. {ECO:0000269|Ref.9}.
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 -!- 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;
CC -!- SUBUNIT: Interacts with AGL24. {ECO:0000269|Ref.9}.
CC -!- INTERACTION:
CC C0LGP9; Q9SN80: F1P2.130; NbExp=2; IntAct=EBI-20664977, EBI-16955068;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.8}; Single-pass
CC type I membrane protein {ECO:0000269|Ref.8}.
CC -!- TISSUE SPECIFICITY: Expressed in meristems, including roots,
CC vegetative, inflorescence and floral meristems, and in embryos.
CC {ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. Lacks the conserved Asp active site at position 612, which is
CC replaced by an Asn residue. However, according to Ref.9, the kinase
CC activity is conserved.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94529.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB87409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB87409.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL163763; CAB87409.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79477.2; -; Genomic_DNA.
DR EMBL; FJ708740; ACN59334.1; -; mRNA.
DR EMBL; AK118661; BAC43256.1; -; mRNA.
DR EMBL; AK221981; BAD94529.1; ALT_INIT; mRNA.
DR EMBL; BT005241; AAO63305.1; -; mRNA.
DR PIR; T47727; T47727.
DR RefSeq; NP_001319765.1; NM_001339765.1.
DR AlphaFoldDB; C0LGP9; -.
DR SMR; C0LGP9; -.
DR BioGRID; 10092; 19.
DR IntAct; C0LGP9; 17.
DR PRIDE; C0LGP9; -.
DR ProteomicsDB; 248437; -.
DR GeneID; 824776; -.
DR KEGG; ath:AT3G56100; -.
DR Araport; AT3G56100; -.
DR InParanoid; C0LGP9; -.
DR OrthoDB; 199108at2759; -.
DR PhylomeDB; C0LGP9; -.
DR PRO; PR:C0LGP9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; C0LGP9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 9.
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; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..48
FT /evidence="ECO:0000255"
FT CHAIN 49..784
FT /note="Probable leucine-rich repeat receptor-like protein
FT kinase IMK3"
FT /id="PRO_0000389458"
FT TOPO_DOM 49..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 126..148
FT /note="LRR 1"
FT REPEAT 150..172
FT /note="LRR 2"
FT REPEAT 174..197
FT /note="LRR 3"
FT REPEAT 198..220
FT /note="LRR 4"
FT REPEAT 222..242
FT /note="LRR 5"
FT REPEAT 247..268
FT /note="LRR 6"
FT REPEAT 271..294
FT /note="LRR 7"
FT REPEAT 295..317
FT /note="LRR 8"
FT REPEAT 319..342
FT /note="LRR 9"
FT REPEAT 343..365
FT /note="LRR 10"
FT DOMAIN 488..773
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 441..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 494..502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 784 AA; 84687 MW; 6F9B3F69661F2CFF CRC64;
MEFITQNQAI TSLSMINTDI DQPKASLRSR FLLHLIICLL FFVPPCSSQA WDGVVITQAD
YQGLQAVKQE LIDPRGFLRS WNGSGFSACS GGWAGIKCAQ GQVIVIQLPW KSLGGRISEK
IGQLQALRKL SLHDNNLGGS IPMSLGLIPN LRGVQLFNNR LTGSIPASLG VSHFLQTLDL
SNNLLSEIIP PNLADSSKLL RLNLSFNSLS GQIPVSLSRS SSLQFLALDH NNLSGPILDT
WGSKSLNLRV LSLDHNSLSG PFPFSLCNLT QLQDFSFSHN RIRGTLPSEL SKLTKLRKMD
ISGNSVSGHI PETLGNISSL IHLDLSQNKL TGEIPISISD LESLNFFNVS YNNLSGPVPT
LLSQKFNSSS FVGNSLLCGY SVSTPCPTLP SPSPEKERKP SHRNLSTKDI ILIASGALLI
VMLILVCVLC CLLRKKANET KAKGGEAGPG AVAAKTEKGG EAEAGGETGG KLVHFDGPMA
FTADDLLCAT AEIMGKSTYG TVYKATLEDG SQVAVKRLRE KITKSQKEFE NEINVLGRIR
HPNLLALRAY YLGPKGEKLV VFDYMSRGSL ATFLHARGPD VHINWPTRMS LIKGMARGLF
YLHTHANIIH GNLTSSNVLL DENITAKISD YGLSRLMTAA AGSSVIATAG ALGYRAPELS
KLKKANTKTD VYSLGVIILE LLTGKSPSEA LNGVDLPQWV ATAVKEEWTN EVFDLELLND
VNTMGDEILN TLKLALHCVD ATPSTRPEAQ QVMTQLGEIR PEETTATTSE PLIDVPEASA
STSQ
