Y5659_ARATH
ID Y5659_ARATH Reviewed; 625 AA.
AC Q9FMD7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable inactive receptor kinase At5g16590;
DE Flags: Precursor;
GN OrderedLocusNames=At5g16590; ORFNames=MTG13.3;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619 AND SER-624, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619 AND SER-624, AND
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16146321; DOI=10.1016/j.jplph.2004.08.012;
RA Shahollari B., Varma A., Oelmueller R.;
RT "Expression of a receptor kinase in Arabidopsis roots is stimulated by the
RT basidiomycete Piriformospora indica and the protein accumulates in Triton
RT X-100 insoluble plasma membrane microdomains.";
RL J. Plant Physiol. 162:945-958(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND IDENTIFICATION BY
RP 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 -!- FUNCTION: Might be involved in early recognition of growth promoting
CC fungi. Appears to be specific for P.indica.
CC {ECO:0000269|PubMed:17397506}.
CC -!- INTERACTION:
CC Q9FMD7; F4I065: At1g49100; NbExp=2; IntAct=EBI-16903983, EBI-20654598;
CC Q9FMD7; C0LGH8: At1g63430; NbExp=3; IntAct=EBI-16903983, EBI-20657656;
CC Q9FMD7; Q9M2R4: T10K17.40; NbExp=3; IntAct=EBI-16903983, EBI-20657109;
CC Q9FMD7; P43298: TMK1; NbExp=2; IntAct=EBI-16903983, EBI-2023970;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16146321,
CC ECO:0000269|PubMed:17397506}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16146321, ECO:0000269|PubMed:17397506}.
CC -!- INDUCTION: Transiently up-regulated by the endophytic fungus
CC Piriformospora indica. {ECO:0000269|PubMed:16146321,
CC ECO:0000269|PubMed:17397506}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- MISCELLANEOUS: Induction of At5g16590 is not observed in mutants devoid
CC of PII-2, another leucine-rich repeat protein normally associated with
CC the plasma membrane microdomains.
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; AB008270; BAB10186.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92314.1; -; Genomic_DNA.
DR EMBL; AK228885; BAF00775.1; -; mRNA.
DR EMBL; BT011691; AAS49054.1; -; mRNA.
DR EMBL; BT012270; AAS76757.1; -; mRNA.
DR RefSeq; NP_197162.1; NM_121665.4.
DR AlphaFoldDB; Q9FMD7; -.
DR SMR; Q9FMD7; -.
DR BioGRID; 16797; 96.
DR IntAct; Q9FMD7; 87.
DR STRING; 3702.AT5G16590.1; -.
DR iPTMnet; Q9FMD7; -.
DR SwissPalm; Q9FMD7; -.
DR PaxDb; Q9FMD7; -.
DR PRIDE; Q9FMD7; -.
DR ProteomicsDB; 243022; -.
DR EnsemblPlants; AT5G16590.1; AT5G16590.1; AT5G16590.
DR GeneID; 831521; -.
DR Gramene; AT5G16590.1; AT5G16590.1; AT5G16590.
DR KEGG; ath:AT5G16590; -.
DR Araport; AT5G16590; -.
DR TAIR; locus:2174190; AT5G16590.
DR eggNOG; ENOG502QSFF; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9FMD7; -.
DR OMA; DSRPTMP; -.
DR OrthoDB; 287580at2759; -.
DR PhylomeDB; Q9FMD7; -.
DR PRO; PR:Q9FMD7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMD7; baseline and differential.
DR Genevisible; Q9FMD7; 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; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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 GO; GO:0009610; P:response to symbiotic fungus; IEP:TAIR.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..625
FT /note="Probable inactive receptor kinase At5g16590"
FT /id="PRO_0000317071"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 88..111
FT /note="LRR 1"
FT REPEAT 112..134
FT /note="LRR 2"
FT REPEAT 136..158
FT /note="LRR 3"
FT REPEAT 160..182
FT /note="LRR 4"
FT REPEAT 183..204
FT /note="LRR 5"
FT DOMAIN 343..613
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 349..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 442
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 496
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 593
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:19376835"
SQ SEQUENCE 625 AA; 67463 MW; D31DE2D3ED1075F4 CRC64;
MKNKTNLGLS VFFFFICLVS VTSDLEADRR ALIALRDGVH GRPLLWNLTA PPCTWGGVQC
ESGRVTALRL PGVGLSGPLP IAIGNLTKLE TLSFRFNALN GPLPPDFANL TLLRYLYLQG
NAFSGEIPSF LFTLPNIIRI NLAQNNFLGR IPDNVNSATR LATLYLQDNQ LTGPIPEIKI
KLQQFNVSSN QLNGSIPDPL SGMPKTAFLG NLLCGKPLDA CPVNGTGNGT VTPGGKGKSD
KLSAGAIVGI VIGCFVLLLV LFLIVFCLCR KKKKEQVVQS RSIEAAPVPT SSAAVAKESN
GPPAVVANGA SENGVSKNPA AVSKDLTFFV KSFGEFDLDG LLKASAEVLG KGTFGSSYKA
SFDHGLVVAV KRLRDVVVPE KEFREKLQVL GSISHANLVT LIAYYFSRDE KLVVFEYMSR
GSLSALLHGN KGSGRSPLNW ETRANIALGA ARAISYLHSR DATTSHGNIK SSNILLSESF
EAKVSDYCLA PMISPTSTPN RIDGYRAPEV TDARKISQKA DVYSFGVLIL ELLTGKSPTH
QQLHEEGVDL PRWVSSITEQ QSPSDVFDPE LTRYQSDSNE NMIRLLNIGI SCTTQYPDSR
PTMPEVTRLI EEVSRSPASP GPLSD
