Y5371_ARATH
ID Y5371_ARATH Reviewed; 614 AA.
AC Q8W4S5; Q9FFP3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At5g63710;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g63710; ORFNames=MBK5.19;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(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;
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].
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 Q8W4S5; A0A178WK49: At1g62950; NbExp=4; IntAct=EBI-16934827, EBI-20657508;
CC Q8W4S5; C0LGH8: At1g63430; NbExp=3; IntAct=EBI-16934827, EBI-20657656;
CC Q8W4S5; Q8LFN2: At3g03770; NbExp=2; IntAct=EBI-16934827, EBI-17121194;
CC Q8W4S5; Q9SNA3: At3g46340; NbExp=3; IntAct=EBI-16934827, EBI-20664802;
CC Q8W4S5; A0A178V0F6: At4g20790; NbExp=3; IntAct=EBI-16934827, EBI-20665764;
CC Q8W4S5; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-16934827, EBI-20654480;
CC Q8W4S5; C0LGS3: At4g37250; NbExp=3; IntAct=EBI-16934827, EBI-16955335;
CC Q8W4S5; C0LGT5: At5g16900; NbExp=2; IntAct=EBI-16934827, EBI-16954237;
CC Q8W4S5; C0LGU1: At5g37450; NbExp=3; IntAct=EBI-16934827, EBI-20661217;
CC Q8W4S5; A0A178UAF6: AXX17_At5g67350; NbExp=2; IntAct=EBI-16934827, EBI-20661274;
CC Q8W4S5; Q9LY03: IRK; NbExp=2; IntAct=EBI-16934827, EBI-1392485;
CC Q8W4S5; O22178: LRR-RLK; NbExp=2; IntAct=EBI-16934827, EBI-20662530;
CC Q8W4S5; Q8GY50: LRR-RLK; NbExp=2; IntAct=EBI-16934827, EBI-20658163;
CC Q8W4S5; C0LGP2: MEE39; NbExp=2; IntAct=EBI-16934827, EBI-20663701;
CC Q8W4S5; Q9SSL9: PEPR1; NbExp=5; IntAct=EBI-16934827, EBI-15588112;
CC Q8W4S5; Q9FZ59: PEPR2; NbExp=2; IntAct=EBI-16934827, EBI-20652612;
CC Q8W4S5; Q9FN37: PSKR2; NbExp=2; IntAct=EBI-16934827, EBI-16902047;
CC Q8W4S5; F4I2N7-2: RLK7; NbExp=2; IntAct=EBI-16934827, EBI-20651307;
CC Q8W4S5; Q9XGZ2: T1N24.22; NbExp=4; IntAct=EBI-16934827, EBI-20654648;
CC Q8W4S5; Q9SIT1: TMK3; NbExp=3; IntAct=EBI-16934827, EBI-16896864;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10464.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005234; BAB10464.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97788.1; -; Genomic_DNA.
DR EMBL; AY060554; AAL31184.1; -; mRNA.
DR EMBL; AY142025; AAM98289.1; -; mRNA.
DR EMBL; FJ708813; ACN59404.1; -; mRNA.
DR RefSeq; NP_001330851.1; NM_001345607.1.
DR RefSeq; NP_001330852.1; NM_001345605.1.
DR RefSeq; NP_568977.1; NM_125766.3.
DR AlphaFoldDB; Q8W4S5; -.
DR SMR; Q8W4S5; -.
DR BioGRID; 21733; 82.
DR IntAct; Q8W4S5; 100.
DR STRING; 3702.AT5G63710.1; -.
DR PaxDb; Q8W4S5; -.
DR PRIDE; Q8W4S5; -.
DR ProteomicsDB; 243112; -.
DR EnsemblPlants; AT5G63710.1; AT5G63710.1; AT5G63710.
DR GeneID; 836491; -.
DR Gramene; AT5G63710.1; AT5G63710.1; AT5G63710.
DR KEGG; ath:AT5G63710; -.
DR Araport; AT5G63710; -.
DR TAIR; locus:2160644; AT5G63710.
DR eggNOG; ENOG502QPJ2; Eukaryota.
DR HOGENOM; CLU_000288_92_8_1; -.
DR InParanoid; Q8W4S5; -.
DR PhylomeDB; Q8W4S5; -.
DR PRO; PR:Q8W4S5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W4S5; baseline and differential.
DR Genevisible; Q8W4S5; AT.
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; -; 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; PF00560; LRR_1; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 3.
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; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..614
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At5g63710"
FT /id="PRO_0000409730"
FT TOPO_DOM 51..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 115..139
FT /note="LRR 1"
FT REPEAT 141..163
FT /note="LRR 2"
FT REPEAT 164..187
FT /note="LRR 3"
FT DOMAIN 289..573
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 416
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 295..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 286
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 449
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 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 463
FT /note="Phosphotyrosine"
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 MOD_RES 545
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 614 AA; 68434 MW; A7DD893619273D76 CRC64;
MAHSGNGESF HDPLRGFIQR NCFRWNNQKL ILQCFMALAF VGITSSTTQP DIEGGALLQL
RDSLNDSSNR LKWTRDFVSP CYSWSYVTCR GQSVVALNLA SSGFTGTLSP AITKLKFLVT
LELQNNSLSG ALPDSLGNMV NLQTLNLSVN SFSGSIPASW SQLSNLKHLD LSSNNLTGSI
PTQFFSIPTF DFSGTQLICG KSLNQPCSSS SRLPVTSSKK KLRDITLTAS CVASIILFLG
AMVMYHHHRV RRTKYDIFFD VAGEDDRKIS FGQLKRFSLR EIQLATDSFN ESNLIGQGGF
GKVYRGLLPD KTKVAVKRLA DYFSPGGEAA FQREIQLISV AVHKNLLRLI GFCTTSSERI
LVYPYMENLS VAYRLRDLKA GEEGLDWPTR KRVAFGSAHG LEYLHEHCNP KIIHRDLKAA
NILLDNNFEP VLGDFGLAKL VDTSLTHVTT QVRGTMGHIA PEYLCTGKSS EKTDVFGYGI
TLLELVTGQR AIDFSRLEEE ENILLLDHIK KLLREQRLRD IVDSNLTTYD SKEVETIVQV
ALLCTQGSPE DRPAMSEVVK MLQGTGGLAE KWTEWEQLEE VRNKEALLLP TLPATWDEEE
TTVDQESIRL STAR
