Y5524_ARATH
ID Y5524_ARATH Reviewed; 607 AA.
AC C0LGX1; Q93Y10; Q9FJP1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At5g65240;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g65240; ORFNames=MQN23.19;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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] (ISOFORM 1).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C0LGX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0LGX1-2; Sequence=VSP_041397;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {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=BAB11660.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB013395; BAB11660.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98027.1; -; Genomic_DNA.
DR EMBL; AY059844; AAL24326.1; -; mRNA.
DR EMBL; BT006309; AAP13417.1; -; mRNA.
DR EMBL; FJ708815; ACN59406.1; -; mRNA.
DR RefSeq; NP_201327.4; NM_125922.5. [C0LGX1-1]
DR AlphaFoldDB; C0LGX1; -.
DR SMR; C0LGX1; -.
DR BioGRID; 21891; 10.
DR IntAct; C0LGX1; 10.
DR STRING; 3702.AT5G65240.2; -.
DR PaxDb; C0LGX1; -.
DR PRIDE; C0LGX1; -.
DR ProteomicsDB; 243162; -. [C0LGX1-1]
DR EnsemblPlants; AT5G65240.1; AT5G65240.1; AT5G65240. [C0LGX1-1]
DR GeneID; 836649; -.
DR Gramene; AT5G65240.1; AT5G65240.1; AT5G65240. [C0LGX1-1]
DR KEGG; ath:AT5G65240; -.
DR Araport; AT5G65240; -.
DR eggNOG; ENOG502QPJ2; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; C0LGX1; -.
DR OMA; WKGQWWR; -.
DR PhylomeDB; C0LGX1; -.
DR PRO; PR:C0LGX1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGX1; baseline and differential.
DR Genevisible; C0LGX1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; -; 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 InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..607
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At5g65240"
FT /id="PRO_0000409729"
FT TOPO_DOM 25..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 87..111
FT /note="LRR 1"
FT REPEAT 112..135
FT /note="LRR 2"
FT REPEAT 137..159
FT /note="LRR 3"
FT REPEAT 160..183
FT /note="LRR 4"
FT DOMAIN 284..568
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 411
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 290..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 444
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..331
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_041397"
SQ SEQUENCE 607 AA; 67718 MW; 015572BD20E0606C CRC64;
MALLIITALV FSSLWSSVSP DAQGDALFAL RSSLRASPEQ LSDWNQNQVD PCTWSQVICD
DKKHVTSVTL SYMNFSSGTL SSGIGILTTL KTLTLKGNGI MGGIPESIGN LSSLTSLDLE
DNHLTDRIPS TLGNLKNLQF LTLSRNNLNG SIPDSLTGLS KLINILLDSN NLSGEIPQSL
FKIPKYNFTA NNLSCGGTFP QPCVTESSPS GDSSSRKTGI IAGVVSGIAV ILLGFFFFFF
CKDKHKGYKR DVFVDVAGEV DRRIAFGQLR RFAWRELQLA TDEFSEKNVL GQGGFGKVYK
GLLSDGTKVA VKRLTDFERP GGDEAFQREV EMISVAVHRN LLRLIGFCTT QTERLLVYPF
MQNLSVAYCL REIKPGDPVL DWFRRKQIAL GAARGLEYLH EHCNPKIIHR DVKAANVLLD
EDFEAVVGDF GLAKLVDVRR TNVTTQVRGT MGHIAPECIS TGKSSEKTDV FGYGIMLLEL
VTGQRAIDFS RLEEEDDVLL LDHVKKLERE KRLEDIVDKK LDEDYIKEEV EMMIQVALLC
TQAAPEERPA MSEVVRMLEG EGLAERWEEW QNLEVTRQEE FQRLQRRFDW GEDSINNQDA
IELSGGR
