RLK90_ARATH
ID RLK90_ARATH Reviewed; 647 AA.
AC Q9LVI6; Q8LD58;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable inactive receptor kinase RLK902;
DE AltName: Full=Receptor-like kinase 902;
DE Flags: Precursor;
GN Name=RLK902; OrderedLocusNames=At3g17840; ORFNames=MEB5.6;
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=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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [6]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=15388970; DOI=10.1271/bbb.68.1935;
RA Tarutani Y., Morimoto T., Sasaki A., Yasuda M., Nakashita H., Yoshida S.,
RA Yamaguchi I., Suzuki Y.;
RT "Molecular characterization of two highly homologous receptor-like kinase
RT genes, RLK902 and RKL1, in Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 68:1935-1941(2004).
RN [7]
RP AUTOPHOSPHORYLATION, INTERACTION WITH AT3G17950; AT3G27210 AND AT5G05190,
RP AND INDUCTION.
RX PubMed=15618630; DOI=10.1271/bbb.68.2581;
RA Tarutani Y., Sasaki A., Yasuda M., Nakashita H., Yoshida S., Yamaguchi I.,
RA Suzuki Y.;
RT "Identification of three clones which commonly interact with the kinase
RT domains of highly homologous two receptor-like kinases, RLK902 and RKL1.";
RL Biosci. Biotechnol. Biochem. 68:2581-2587(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 SUBCELLULAR LOCATION.
RX PubMed=17397506; DOI=10.1111/j.1365-313x.2007.03028.x;
RA Shahollari B., Vadassery J., Varma A., Oelmueller R.;
RT "A leucine-rich repeat protein is required for growth promotion and
RT enhanced seed production mediated by the endophytic fungus Piriformospora
RT indica in Arabidopsis thaliana.";
RL Plant J. 50:1-13(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [11]
RP IDENTIFICATION BY 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 -!- SUBUNIT: Interacts with At3g17950, At3g27210 and At5g05190.
CC {ECO:0000269|PubMed:15618630}.
CC -!- INTERACTION:
CC Q9LVI6; F4I336: At1g29730; NbExp=2; IntAct=EBI-1626936, EBI-20654003;
CC Q9LVI6; F4I065: At1g49100; NbExp=2; IntAct=EBI-1626936, EBI-20654598;
CC Q9LVI6; A0A178WLG7: At1g51790; NbExp=3; IntAct=EBI-1626936, EBI-20652336;
CC Q9LVI6; C0LGG6-2: At1g51890; NbExp=2; IntAct=EBI-1626936, EBI-20655952;
CC Q9LVI6; C0LGG8: At1g53430; NbExp=2; IntAct=EBI-1626936, EBI-20656135;
CC Q9LVI6; A0A1P8ASI5: At1g56120; NbExp=4; IntAct=EBI-1626936, EBI-20656718;
CC Q9LVI6; A0A178WK49: At1g62950; NbExp=3; IntAct=EBI-1626936, EBI-20657508;
CC Q9LVI6; C0LGH8: At1g63430; NbExp=4; IntAct=EBI-1626936, EBI-20657656;
CC Q9LVI6; C0LGJ1: At1g74360; NbExp=4; IntAct=EBI-1626936, EBI-20652666;
CC Q9LVI6; O64556: At2g19230; NbExp=4; IntAct=EBI-1626936, EBI-20662335;
CC Q9LVI6; Q9LIG2: At3g21340; NbExp=2; IntAct=EBI-1626936, EBI-941096;
CC Q9LVI6; Q9LFG1: At3g53590; NbExp=3; IntAct=EBI-1626936, EBI-20664191;
CC Q9LVI6; Q9LT96: At5g49770; NbExp=2; IntAct=EBI-1626936, EBI-17123993;
CC Q9LVI6; Q9SNA2: F18L15.70; NbExp=3; IntAct=EBI-1626936, EBI-20658889;
CC Q9LVI6; Q9LJM4: IKU2; NbExp=2; IntAct=EBI-1626936, EBI-20664220;
CC Q9LVI6; O64794: LRR-RLK; NbExp=2; IntAct=EBI-1626936, EBI-16887796;
CC Q9LVI6; C0LGP2: MEE39; NbExp=2; IntAct=EBI-1626936, EBI-20663701;
CC Q9LVI6; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-1626936, EBI-17121474;
CC Q9LVI6; Q9ZVR7: PSKR1; NbExp=2; IntAct=EBI-1626936, EBI-16172949;
CC Q9LVI6; Q9FN37: PSKR2; NbExp=2; IntAct=EBI-1626936, EBI-16902047;
CC Q9LVI6; C0LGF5: RGI5; NbExp=2; IntAct=EBI-1626936, EBI-16964286;
CC Q9LVI6; Q9SKB2: SOBIR1; NbExp=3; IntAct=EBI-1626936, EBI-16905883;
CC Q9LVI6; Q9ZU46: ZAR1; NbExp=4; IntAct=EBI-1626936, EBI-16954860;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15388970,
CC ECO:0000269|PubMed:17397506}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15388970, ECO:0000269|PubMed:17397506}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, lateral root primordia,
CC stipules, and floral organ abscission zones.
CC {ECO:0000269|PubMed:15388970}.
CC -!- INDUCTION: By wounding. Rapid but transient down-regulation by
CC salicylic acid treatment or pathogen infection.
CC {ECO:0000269|PubMed:15618630}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- PTM: Autophosphorylation.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:15388970}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Autophosphorylation is proposed although the protein kinase
CC domain is predicted to be catalytically inactive.
CC {ECO:0000305|PubMed:15618630}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB019230; BAB02707.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76013.1; -; Genomic_DNA.
DR EMBL; AY095994; AAM19950.1; -; mRNA.
DR EMBL; BT002283; AAN72294.1; -; mRNA.
DR EMBL; AY086189; AAM64268.1; ALT_INIT; mRNA.
DR RefSeq; NP_566589.1; NM_112665.3.
DR AlphaFoldDB; Q9LVI6; -.
DR SMR; Q9LVI6; -.
DR BioGRID; 6386; 78.
DR IntAct; Q9LVI6; 103.
DR STRING; 3702.AT3G17840.1; -.
DR iPTMnet; Q9LVI6; -.
DR PaxDb; Q9LVI6; -.
DR PRIDE; Q9LVI6; -.
DR ProteomicsDB; 226900; -.
DR EnsemblPlants; AT3G17840.1; AT3G17840.1; AT3G17840.
DR GeneID; 821053; -.
DR Gramene; AT3G17840.1; AT3G17840.1; AT3G17840.
DR KEGG; ath:AT3G17840; -.
DR Araport; AT3G17840; -.
DR TAIR; locus:2088500; AT3G17840.
DR eggNOG; ENOG502QSFF; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9LVI6; -.
DR OMA; IDCTEQH; -.
DR OrthoDB; 287580at2759; -.
DR PhylomeDB; Q9LVI6; -.
DR PRO; PR:Q9LVI6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVI6; baseline and differential.
DR Genevisible; Q9LVI6; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA: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; -; 1.
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; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..647
FT /note="Probable inactive receptor kinase RLK902"
FT /id="PRO_0000317073"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 69..93
FT /note="LRR 1"
FT REPEAT 94..118
FT /note="LRR 2"
FT REPEAT 119..142
FT /note="LRR 3"
FT REPEAT 144..165
FT /note="LRR 4"
FT REPEAT 166..192
FT /note="LRR 5"
FT DOMAIN 365..639
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 371..379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 388
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 520
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 618
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CONFLICT 117
FT /note="S -> R (in Ref. 4; AAM64268)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="S -> R (in Ref. 4; AAM64268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 70406 MW; 1FF91B013B75A1DA CRC64;
MRLFFTPSMS NLSIFFSILL LSLPLPSIGD LAADKSALLS FRSAVGGRTL LWDVKQTSPC
NWTGVLCDGG RVTALRLPGE TLSGHIPEGI FGNLTQLRTL SLRLNGLTGS LPLDLGSCSD
LRRLYLQGNR FSGEIPEVLF SLSNLVRLNL AENEFSGEIS SGFKNLTRLK TLYLENNKLS
GSLLDLDLSL DQFNVSNNLL NGSIPKSLQK FDSDSFVGTS LCGKPLVVCS NEGTVPSQPI
SVGNIPGTVE GSEEKKKRKK LSGGAIAGIV IGCVVGLSLI VMILMVLFRK KGNERTRAID
LATIKHHEVE IPGEKAAVEA PENRSYVNEY SPSAVKAVEV NSSGMKKLVF FGNATKVFDL
EDLLRASAEV LGKGTFGTAY KAVLDAVTLV AVKRLKDVTM ADREFKEKIE VVGAMDHENL
VPLRAYYYSG DEKLLVYDFM PMGSLSALLH GNKGAGRPPL NWEVRSGIAL GAARGLDYLH
SQDPLSSHGN VKSSNILLTN SHDARVSDFG LAQLVSASST TPNRATGYRA PEVTDPRRVS
QKADVYSFGV VLLELLTGKA PSNSVMNEEG MDLARWVHSV AREEWRNEVF DSELMSIETV
VSVEEEMAEM LQLGIDCTEQ HPDKRPVMVE VVRRIQELRQ SGADRVG
