ID Y5694_ARATH Reviewed; 872 AA.
AC Q9FL51;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Probably inactive leucine-rich repeat receptor-like protein kinase At5g06940;
DE Flags: Precursor;
GN OrderedLocusNames=At5g06940; ORFNames=MOJ9.11;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. Lacks the conserved Asp active site at position 712, 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; AB010697; BAB11152.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91084.1; -; Genomic_DNA.
DR RefSeq; NP_196311.1; NM_120776.2.
DR AlphaFoldDB; Q9FL51; -.
DR SMR; Q9FL51; -.
DR STRING; 3702.Q9FL51; -.
DR PaxDb; 3702-AT5G06940-1; -.
DR ProteomicsDB; 243164; -.
DR EnsemblPlants; AT5G06940.1; AT5G06940.1; AT5G06940.
DR GeneID; 830585; -.
DR Gramene; AT5G06940.1; AT5G06940.1; AT5G06940.
DR KEGG; ath:AT5G06940; -.
DR Araport; AT5G06940; -.
DR TAIR; AT5G06940; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9FL51; -.
DR OMA; EPLCRVP; -.
DR OrthoDB; 397564at2759; -.
DR PhylomeDB; Q9FL51; -.
DR PRO; PR:Q9FL51; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FL51; baseline and differential.
DR Genevisible; Q9FL51; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR48010:SF55; OS01G0607900 PROTEIN; 1.
DR PANTHER; PTHR48010; OS05G0588300 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 6.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..872
FT /note="Probably inactive leucine-rich repeat receptor-like
FT protein kinase At5g06940"
FT /id="PRO_0000389455"
FT TOPO_DOM 27..540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 79..98
FT /note="LRR 1"
FT REPEAT 99..122
FT /note="LRR 2"
FT REPEAT 123..146
FT /note="LRR 3"
FT REPEAT 147..169
FT /note="LRR 4"
FT REPEAT 171..193
FT /note="LRR 5"
FT REPEAT 195..217
FT /note="LRR 6"
FT REPEAT 219..243
FT /note="LRR 7"
FT REPEAT 244..267
FT /note="LRR 8"
FT REPEAT 269..292
FT /note="LRR 9"
FT REPEAT 294..316
FT /note="LRR 10"
FT REPEAT 317..340
FT /note="LRR 11"
FT REPEAT 341..365
FT /note="LRR 12"
FT REPEAT 367..389
FT /note="LRR 13"
FT REPEAT 391..412
FT /note="LRR 14"
FT REPEAT 413..435
FT /note="LRR 15"
FT REPEAT 436..459
FT /note="LRR 16"
FT REPEAT 460..482
FT /note="LRR 17"
FT REPEAT 484..506
FT /note="LRR 18"
FT DOMAIN 589..863
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 595..603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 585
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 662
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 699
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 754
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 761
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 872 AA; 95682 MW; 4782EEAB3F0E4E39 CRC64;
MATRFKHQFS ISLALTFFFF FTKTFSFTEN EELGNLLRFK ASFDDPKGSL SGWFNTSSSH
HCNWTGITCT RAPTLYVSSI NLQSLNLSGE ISDSICDLPY LTHLDLSLNF FNQPIPLQLS
RCVTLETLNL SSNLIWGTIP DQISEFSSLK VIDFSSNHVE GMIPEDLGLL FNLQVLNLGS
NLLTGIVPPA IGKLSELVVL DLSENSYLVS EIPSFLGKLD KLEQLLLHRS GFHGEIPTSF
VGLTSLRTLD LSLNNLSGEI PRSLGPSLKN LVSLDVSQNK LSGSFPSGIC SGKRLINLSL
HSNFFEGSLP NSIGECLSLE RLQVQNNGFS GEFPVVLWKL PRIKIIRADN NRFTGQVPES
VSLASALEQV EIVNNSFSGE IPHGLGLVKS LYKFSASQNR FSGELPPNFC DSPVLSIVNI
SHNRLLGKIP ELKNCKKLVS LSLAGNAFTG EIPPSLADLH VLTYLDLSDN SLTGLIPQGL
QNLKLALFNV SFNGLSGEVP HSLVSGLPAS FLQGNPELCG PGLPNSCSSD RSNFHKKGGK
ALVLSLICLA LAIATFLAVL YRYSRKKVQF KSTWRSEFYY PFKLTEHELM KVVNESCPSG
SEVYVLSLSS GELLAVKKLV NSKNISSKSL KAQVRTIAKI RHKNITRILG FCFKDEMIFL
IYEFTQNGSL HDMLSRAGDQ LPWSIRLKIA LGVAQALAYI SKDYVPHLLH RNLKSANIFL
DKDFEPKLSD FALDHIVGET AFQSLVHANT NSCYTAPENH YSKKATEDMD VYSFGVVLLE
LVTGQSAEKA EEGSSGESLD IVKQVRRKIN LTDGAAQVLD QKILSDSCQS DMRKTLDIAL
DCTAVAAEKR PSLVKVIKLL EGISSSVSPV SA
//
