Y1680_ARATH
ID Y1680_ARATH Reviewed; 670 AA.
AC Q9M9C5; Q94JL9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable leucine-rich repeat receptor-like protein kinase At1g68400;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g68400; ORFNames=T2E12.5;
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=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 Q9M9C5; C0LGD7-2: At1g06840; NbExp=2; IntAct=EBI-1238661, EBI-20651159;
CC Q9M9C5; C0LGG6-2: At1g51890; NbExp=2; IntAct=EBI-1238661, EBI-20655952;
CC Q9M9C5; A0A178WK49: At1g62950; NbExp=3; IntAct=EBI-1238661, EBI-20657508;
CC Q9M9C5; Q9LRT1: At3g28040; NbExp=3; IntAct=EBI-1238661, EBI-16956175;
CC Q9M9C5; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-1238661, EBI-20654480;
CC Q9M9C5; Q9SN97: F18L15.140; NbExp=3; IntAct=EBI-1238661, EBI-20655031;
CC Q9M9C5; Q9SNA2: F18L15.70; NbExp=3; IntAct=EBI-1238661, EBI-20658889;
CC Q9M9C5; Q8GY50: LRR-RLK; NbExp=3; IntAct=EBI-1238661, EBI-20658163;
CC Q9M9C5; Q9M0D8: LRR-RLK; NbExp=4; IntAct=EBI-1238661, EBI-16955231;
CC Q9M9C5; Q93ZS4: NIK3; NbExp=3; IntAct=EBI-1238661, EBI-17121474;
CC Q9M9C5; Q9FZ59: PEPR2; NbExp=3; IntAct=EBI-1238661, EBI-20652612;
CC Q9M9C5; Q9ZVR7: PSKR1; NbExp=3; IntAct=EBI-1238661, EBI-16172949;
CC Q9M9C5; Q9FN37: PSKR2; NbExp=3; IntAct=EBI-1238661, EBI-16902047;
CC Q9M9C5; Q9LZV7: PXC2; NbExp=3; IntAct=EBI-1238661, EBI-1238200;
CC Q9M9C5; Q9SKB2: SOBIR1; NbExp=3; IntAct=EBI-1238661, EBI-16905883;
CC Q9M9C5; Q9SIT1: TMK3; NbExp=4; IntAct=EBI-1238661, EBI-16896864;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC015986; AAF26042.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34789.1; -; Genomic_DNA.
DR EMBL; AF378890; AAK55693.1; -; mRNA.
DR EMBL; AY102147; AAM26714.1; -; mRNA.
DR EMBL; FJ708673; ACN59268.1; -; mRNA.
DR PIR; H96707; H96707.
DR RefSeq; NP_177007.1; NM_105511.3.
DR AlphaFoldDB; Q9M9C5; -.
DR SMR; Q9M9C5; -.
DR BioGRID; 28390; 60.
DR IntAct; Q9M9C5; 78.
DR STRING; 3702.AT1G68400.1; -.
DR iPTMnet; Q9M9C5; -.
DR PaxDb; Q9M9C5; -.
DR PRIDE; Q9M9C5; -.
DR ProteomicsDB; 242395; -.
DR EnsemblPlants; AT1G68400.1; AT1G68400.1; AT1G68400.
DR GeneID; 843169; -.
DR Gramene; AT1G68400.1; AT1G68400.1; AT1G68400.
DR KEGG; ath:AT1G68400; -.
DR Araport; AT1G68400; -.
DR TAIR; locus:2202359; AT1G68400.
DR eggNOG; ENOG502QPUR; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9M9C5; -.
DR OMA; MPRNSGG; -.
DR OrthoDB; 566336at2759; -.
DR PhylomeDB; Q9M9C5; -.
DR PRO; PR:Q9M9C5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9C5; baseline and differential.
DR Genevisible; Q9M9C5; 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; -; 2.
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; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 4.
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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..670
FT /note="Probable leucine-rich repeat receptor-like protein
FT kinase At1g68400"
FT /id="PRO_0000401342"
FT TOPO_DOM 30..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 69..91
FT /note="LRR 1"
FT REPEAT 92..114
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 REPEAT 186..207
FT /note="LRR 6"
FT DOMAIN 362..636
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 230..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 491
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 368..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 616
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
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 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 400
FT /note="G -> GK (in Ref. 3; AAK55693/AAM26714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 73521 MW; A27282EC4FB37C25 CRC64;
MAKSSFFNKH LLLSLLILLQ SCLLSSSSST DSETLLNFKL TADSTGKLNS WNTTTNPCQW
TGVSCNRNRV TRLVLEDINL TGSISSLTSL TSLRVLSLKH NNLSGPIPNL SNLTALKLLF
LSNNQFSGNF PTSITSLTRL YRLDLSFNNF SGQIPPDLTD LTHLLTLRLE SNRFSGQIPN
INLSDLQDFN VSGNNFNGQI PNSLSQFPES VFTQNPSLCG APLLKCTKLS SDPTKPGRPD
EAKASPLNKP ETVPSSPTSI HGGDKSNNTS RISTISLIAI ILGDFIILSF VSLLLYYCFW
RQYAVNKKKH SKILEGEKIV YSSNPYPTST QNNNNQNQQV GDKGKMVFFE GTRRFELEDL
LRASAEMLGK GGFGTAYKAV LEDGNEVAVK RLKDAVTVAG KKEFEQQMEV LGRLRHTNLV
SLKAYYFARE EKLLVYDYMP NGSLFWLLHG NRGPGRTPLD WTTRLKIAAG AARGLAFIHG
SCKTLKLTHG DIKSTNVLLD RSGNARVSDF GLSIFAPSQT VAKSNGYRAP ELIDGRKHTQ
KSDVYSFGVL LLEILTGKCP NMVETGHSGG AVDLPRWVQS VVREEWTAEV FDLELMRYKD
IEEEMVGLLQ IAMACTAVAA DHRPKMGHVV KLIEDIRGGG SEASPCNDGI NSAVDSPCLS
EDTCGGTTSQ
