Y1699_ARATH
ID Y1699_ARATH Reviewed; 591 AA.
AC C0LGI5; O04545;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g69990;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g69990; ORFNames=F20P5.27;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=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).
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 C0LGI5; C0LGD9: At1g07560; NbExp=2; IntAct=EBI-20651225, EBI-16902423;
CC C0LGI5; C0LGI5: At1g69990; NbExp=2; IntAct=EBI-20651225, EBI-20651225;
CC C0LGI5; Q9ZQR3: At2g14510; NbExp=2; IntAct=EBI-20651225, EBI-20651957;
CC C0LGI5; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-20651225, EBI-16902452;
CC C0LGI5; Q94F62: BAK1; NbExp=4; IntAct=EBI-20651225, EBI-617138;
CC C0LGI5; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-20651225, EBI-16895926;
CC C0LGI5; Q9C8I6: IOS1; NbExp=4; IntAct=EBI-20651225, EBI-16924837;
CC C0LGI5; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-20651225, EBI-20651739;
CC C0LGI5; Q9LFS4: NIK1; NbExp=2; IntAct=EBI-20651225, EBI-16146189;
CC C0LGI5; C0LGR3: RGI3; NbExp=3; IntAct=EBI-20651225, EBI-20659695;
CC C0LGI5; Q9ZRF9: RPK1; NbExp=3; IntAct=EBI-20651225, EBI-1238953;
CC C0LGI5; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-20651225, EBI-6290483;
CC C0LGI5; Q8LPS5: SERK5; NbExp=2; IntAct=EBI-20651225, EBI-16887868;
CC C0LGI5; Q9C8M9: SRF6; NbExp=3; IntAct=EBI-20651225, EBI-16954301;
CC C0LGI5; Q8RWZ1: SUB; NbExp=3; IntAct=EBI-20651225, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61113.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002062; AAB61113.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35006.1; -; Genomic_DNA.
DR EMBL; FJ708675; ACN59270.1; -; mRNA.
DR PIR; E96722; E96722.
DR RefSeq; NP_177157.1; NM_105668.1.
DR AlphaFoldDB; C0LGI5; -.
DR SMR; C0LGI5; -.
DR BioGRID; 28557; 28.
DR IntAct; C0LGI5; 42.
DR STRING; 3702.AT1G69990.1; -.
DR PaxDb; C0LGI5; -.
DR PRIDE; C0LGI5; -.
DR EnsemblPlants; AT1G69990.1; AT1G69990.1; AT1G69990.
DR GeneID; 843336; -.
DR Gramene; AT1G69990.1; AT1G69990.1; AT1G69990.
DR KEGG; ath:AT1G69990; -.
DR Araport; AT1G69990; -.
DR TAIR; locus:2020558; AT1G69990.
DR eggNOG; ENOG502QRP1; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; C0LGI5; -.
DR OMA; GMFWWFF; -.
DR OrthoDB; 681595at2759; -.
DR PhylomeDB; C0LGI5; -.
DR PRO; PR:C0LGI5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGI5; baseline and differential.
DR Genevisible; C0LGI5; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; -; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..591
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g69990"
FT /id="PRO_0000387541"
FT TOPO_DOM 19..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 66..88
FT /note="LRR 1"
FT REPEAT 90..111
FT /note="LRR 2"
FT REPEAT 115..137
FT /note="LRR 3"
FT REPEAT 139..162
FT /note="LRR 4"
FT REPEAT 163..185
FT /note="LRR 5"
FT DOMAIN 295..573
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 301..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 463
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 591 AA; 65553 MW; D3AF9B8A24DABFB0 CRC64;
MKTISIFFVI ILMSSSHAED DVLCLKGFKS SLKDPSNQLN TWSFPNSSSS ICKLTGVSCW
NAKENRILSL QLQSMQLSGQ IPESLKLCRS LQSLDLSFND FSGLIPSQIC SWLPYLVTLD
LSGNKLSGSI PSQIVDCKFL NSLALNQNKL TGSIPSELTR LNRLQRLSLA DNDLSGSIPS
ELSHYGEDGF RGNGGLCGKP LSNCGSFNGK NLTIIVTAGV IGAVGSLCVG FGMFWWFFIR
DRRKMNNYGY GAGKCKDDSD WIGLLRSHKL VQVTLFQKPI VKIKLVDLIE ATNGFDSGNI
VVSSRSGVSY KADLPDGSTL EVKRLSSCCE LSEKQFRSEI NKLGQIRHPN LVPLLGFCVV
EDEILLVYKH MANGTLYSQL QQWDIDWPTR VRVAVGAARG LAWLHHGCQP LYMHQYISSN
VILLDEDFDA RVIDYGLGKL VSSQDSKDSS FSNGKFGYVA PEYSSTMVAS LSGDVYGFGI
VLLEIVTGQK PVLINNGEEG FKESLVEWVS KHLSNGRSKD AIDRRIFGKG YDDEIMQVLR
IACSCVVSRP KERPLMIQVY ESLKNLGDQH GFFSEYSDEF PLIFNKQEHL K
