Y3359_ARATH
ID Y3359_ARATH Reviewed; 937 AA.
AC Q9LFG1; F4JAH5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative leucine-rich repeat receptor-like serine/threonine-protein kinase At3g53590;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At3g53590; ORFNames=F4P12.290;
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).
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 -!- INTERACTION:
CC Q9LFG1; Q9FL28: FLS2; NbExp=3; IntAct=EBI-20664191, EBI-1799448;
CC Q9LFG1; Q9LFS4: NIK1; NbExp=3; IntAct=EBI-20664191, EBI-16146189;
CC Q9LFG1; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-20664191, EBI-16914444;
CC Q9LFG1; Q9LVI6: RLK902; NbExp=3; IntAct=EBI-20664191, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB67666.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL132966; CAB67666.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T45899; T45899.
DR AlphaFoldDB; Q9LFG1; -.
DR SMR; Q9LFG1; -.
DR BioGRID; 9844; 17.
DR IntAct; Q9LFG1; 21.
DR PeptideAtlas; Q9LFG1; -.
DR PRIDE; Q9LFG1; -.
DR Araport; AT3G53590; -.
DR TAIR; locus:2084016; AT3G53590.
DR InParanoid; Q9LFG1; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LFG1; -.
DR PRO; PR:Q9LFG1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LFG1; 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; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 7.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..937
FT /note="Putative leucine-rich repeat receptor-like
FT serine/threonine-protein kinase At3g53590"
FT /id="PRO_0000403350"
FT TOPO_DOM 21..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..937
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 102..126
FT /note="LRR 1"
FT REPEAT 127..150
FT /note="LRR 2"
FT REPEAT 152..173
FT /note="LRR 3"
FT REPEAT 174..198
FT /note="LRR 4"
FT REPEAT 200..222
FT /note="LRR 5"
FT REPEAT 223..249
FT /note="LRR 6"
FT REPEAT 251..270
FT /note="LRR 7"
FT REPEAT 271..294
FT /note="LRR 8"
FT REPEAT 296..316
FT /note="LRR 9"
FT REPEAT 317..341
FT /note="LRR 10"
FT REPEAT 343..360
FT /note="LRR 11"
FT DOMAIN 614..886
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 738
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 620..628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 642
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 50
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 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
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 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 937 AA; 104889 MW; DD7D1327F4EBFAAA CRC64;
MIPPNINVLI RSICINLVTS LPLNFAYIFI HFAVNALREI KRSLIDPMRN LSNWAKGDPC
NSNWTGIICF GRSHNDGHFH VRELQLMRLN LSGELAPEVG QLLYLEILDV MWNNLTGRIP
LEIGRISSLK LLLLNGNKFT GSLPPELGNL QNLNRLQVDE NNITGSVPFS FGNLRSIKHL
HLNNNTISGE IPVELSKLPK LVHMILDNNN LTGTLPLELA QLPSLTILQL DNNNFEGSTI
PEAYGHFSRL VKLSLRNCGL QGSIPDLSRI ENLSYLDLSW NHLTGTIPES KLSDNMTTIE
LSYNHLTGSI PQSFSDLNSL QLLSLENNSL SGSVPTEIWQ DKSFENNKLQ VYDLNNNFSD
ATGNLRTPDN VTLYLRGNPI CKSTSIPMVT QFFEYICGEK KQTSTNSNTP CSNVSCPFEN
VKVSPGICLC TAPLSIDYRL KSPSFFFFTP YIERQFREYI TSSLQLETHQ LAIDRLVDEN
RLRPRMYLKL VPKGRITFNK SEVIRIRDRF MSWSFNKTDF FGPYELLDFP LQGPYADLLA
QTSGIRTIVW MMIVAGSVVA ATVLSVTATL LYVRKRRENS HTLTKKRVFR TISREIKGVK
KFSFVELSDA TNGFDSSTLI GRGSYGKVYK GILSNKTEVA IKRGEETSLQ SEKEFLNEID
LLSRLHHRNL VSLIGYSSDI GEQMLVYEYM PNGNVRDWLS ANAADTLSFS MRSHVALGSA
KGILYLHTEA NPPVIHRDIK TSNILLDCQL HAKVADFGLS RLAPAFGEGD GEPAHVSTVV
RGTPGYLDPE YFMTQQLTVR SDVYSFGVVL LELLTGMHPF FEGTHIIREV RTANECGTVL
SVADSRMGQC SPDKVKKLAE LALWCCEDRP ETRPPMSKVV KELEGICQSV REPEMFSETT
KLLCSKTSPS SSSVPSPLSL LPGSNLDSGF FHAVKPR
