IMK2_ARATH
ID IMK2_ARATH Reviewed; 836 AA.
AC Q9SCT4;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probably inactive leucine-rich repeat receptor-like protein kinase IMK2;
DE AltName: Full=Protein INFLORESCENCE MERISTEM RECEPTOR-LIKE KINASE 2;
DE Flags: Precursor;
GN Name=IMK2; OrderedLocusNames=At3g51740; ORFNames=T18N14.120;
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=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 [4]
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 [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [8]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206,
CC ECO:0000269|PubMed:15308754, ECO:0000269|Ref.6,
CC ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:15308754,
CC ECO:0000269|Ref.6, ECO:0000305|PubMed:17644812}.
CC -!- TISSUE SPECIFICITY: Expressed in meristems, including roots,
CC vegetative, inflorescence and floral meristems. {ECO:0000269|Ref.5,
CC ECO:0000269|Ref.6}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. Lacks the conserved Asp active site at position 661, which is
CC replaced by an Asn residue.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; AL132968; CAB63160.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78832.1; -; Genomic_DNA.
DR EMBL; AF372978; AAK50115.1; -; mRNA.
DR EMBL; AY054515; AAK96706.1; -; mRNA.
DR EMBL; BT006350; AAP21158.1; -; mRNA.
DR EMBL; FJ708739; ACN59333.1; -; mRNA.
DR PIR; T46070; T46070.
DR RefSeq; NP_190742.1; NM_115033.4.
DR AlphaFoldDB; Q9SCT4; -.
DR SMR; Q9SCT4; -.
DR BioGRID; 9655; 13.
DR IntAct; Q9SCT4; 9.
DR STRING; 3702.AT3G51740.1; -.
DR iPTMnet; Q9SCT4; -.
DR SwissPalm; Q9SCT4; -.
DR PaxDb; Q9SCT4; -.
DR PRIDE; Q9SCT4; -.
DR ProteomicsDB; 248550; -.
DR EnsemblPlants; AT3G51740.1; AT3G51740.1; AT3G51740.
DR GeneID; 824337; -.
DR Gramene; AT3G51740.1; AT3G51740.1; AT3G51740.
DR KEGG; ath:AT3G51740; -.
DR Araport; AT3G51740; -.
DR TAIR; locus:2098267; AT3G51740.
DR eggNOG; ENOG502QRJ8; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9SCT4; -.
DR OMA; CSGWAGI; -.
DR OrthoDB; 199108at2759; -.
DR PhylomeDB; Q9SCT4; -.
DR PRO; PR:Q9SCT4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCT4; baseline and differential.
DR Genevisible; Q9SCT4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13855; LRR_8; 2.
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; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..836
FT /note="Probably inactive leucine-rich repeat receptor-like
FT protein kinase IMK2"
FT /id="PRO_0000389457"
FT TOPO_DOM 34..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..836
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 119..142
FT /note="LRR 1"
FT REPEAT 143..166
FT /note="LRR 2"
FT REPEAT 167..189
FT /note="LRR 3"
FT REPEAT 191..212
FT /note="LRR 4"
FT REPEAT 215..237
FT /note="LRR 5"
FT REPEAT 240..261
FT /note="LRR 6"
FT REPEAT 264..286
FT /note="LRR 7"
FT REPEAT 288..310
FT /note="LRR 8"
FT REPEAT 312..334
FT /note="LRR 9"
FT REPEAT 336..358
FT /note="LRR 10"
FT REPEAT 360..381
FT /note="LRR 11"
FT REPEAT 384..406
FT /note="LRR 12"
FT DOMAIN 537..808
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 430..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 543..551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 539
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 636
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 700
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 836 AA; 90261 MW; EAF6C7BD69193361 CRC64;
MNHLYKNPFR IYEISFHFCA SLLLCFLLFS AQAVAGGGGG GHSWDGIVVT QANYQALQAI
KHELIDFTGV LKSWNNSASS QVCSGWAGIK CLRGQVVAIQ LPWKGLGGTI SEKIGQLGSL
RKLSLHNNVI AGSVPRSLGY LKSLRGVYLF NNRLSGSIPV SLGNCPLLQN LDLSSNQLTG
AIPPSLTEST RLYRLNLSFN SLSGPLPVSV ARSYTLTFLD LQHNNLSGSI PDFFVNGSHP
LKTLNLDHNR FSGAVPVSLC KHSLLEEVSI SHNQLSGSIP RECGGLPHLQ SLDFSYNSIN
GTIPDSFSNL SSLVSLNLES NHLKGPIPDA IDRLHNLTEL NLKRNKINGP IPETIGNISG
IKKLDLSENN FTGPIPLSLV HLAKLSSFNV SYNTLSGPVP PVLSKKFNSS SFLGNIQLCG
YSSSNPCPAP DHHHPLTLSP TSSQEPRKHH HRKLSVKDVI LIAIGALLAI LLLLCCILLC
CLIKKRAALK QKDGKDKTSE KTVSAGVAGT ASAGGEMGGK LVHFDGPFVF TADDLLCATA
EIMGKSTYGT AYKATLEDGN EVAVKRLREK TTKGVKEFEG EVTALGKIRH QNLLALRAYY
LGPKGEKLLV FDYMSKGSLS AFLHARGPET LIPWETRMKI AKGISRGLAH LHSNENMIHE
NLTASNILLD EQTNAHIADY GLSRLMTAAA ATNVIATAGT LGYRAPEFSK IKNASAKTDV
YSLGIIILEL LTGKSPGEPT NGMDLPQWVA SIVKEEWTNE VFDLELMRET QSVGDELLNT
LKLALHCVDP SPAARPEANQ VVEQLEEIRP ETEVETETTP FGSGGEGGKD LGSNEE
