Y1765_ARATH
ID Y1765_ARATH Reviewed; 1014 AA.
AC C0LGE0; Q94JZ3; Q9LQN8; Q9LQN9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g07650;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g07650; ORFNames=F24B9.28, F24B9.29;
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] (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 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 C0LGE0; Q9SHI2: At1g17230; NbExp=3; IntAct=EBI-16954597, EBI-20651261;
CC C0LGE0; Q9LP24-3: At1g35710; NbExp=3; IntAct=EBI-16954597, EBI-20651291;
CC C0LGE0; F4I2N7-2: RLK7; NbExp=3; IntAct=EBI-16954597, EBI-20651307;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C0LGE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0LGE0-2; Sequence=VSP_038292;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF75092.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF75093.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007583; AAF75092.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007583; AAF75093.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28155.1; -; Genomic_DNA.
DR EMBL; AF370513; AAK43890.1; -; mRNA.
DR EMBL; BT000348; AAN15667.1; -; mRNA.
DR EMBL; AK221671; BAD95357.1; -; mRNA.
DR EMBL; FJ708629; ACN59225.1; -; mRNA.
DR PIR; A86211; A86211.
DR PIR; B86211; B86211.
DR RefSeq; NP_172244.2; NM_100638.5. [C0LGE0-1]
DR AlphaFoldDB; C0LGE0; -.
DR SMR; C0LGE0; -.
DR BioGRID; 22519; 52.
DR IntAct; C0LGE0; 53.
DR STRING; 3702.AT1G07650.2; -.
DR CAZy; CBM57; Carbohydrate-Binding Module Family 57.
DR iPTMnet; C0LGE0; -.
DR PaxDb; C0LGE0; -.
DR PRIDE; C0LGE0; -.
DR ProteomicsDB; 242422; -. [C0LGE0-1]
DR EnsemblPlants; AT1G07650.1; AT1G07650.1; AT1G07650. [C0LGE0-1]
DR GeneID; 837278; -.
DR Gramene; AT1G07650.1; AT1G07650.1; AT1G07650. [C0LGE0-1]
DR KEGG; ath:AT1G07650; -.
DR Araport; AT1G07650; -.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR HOGENOM; CLU_000288_114_2_1; -.
DR InParanoid; C0LGE0; -.
DR PhylomeDB; C0LGE0; -.
DR PRO; PR:C0LGE0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGE0; baseline and differential.
DR Genevisible; C0LGE0; 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; IBA:GO_Central.
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; IPR021720; Malectin_dom.
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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 3.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1014
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g07650"
FT /id="PRO_0000387545"
FT TOPO_DOM 24..619
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 641..1014
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 89..112
FT /note="LRR 1"
FT REPEAT 113..137
FT /note="LRR 2"
FT REPEAT 139..160
FT /note="LRR 3"
FT REPEAT 161..184
FT /note="LRR 4"
FT REPEAT 186..207
FT /note="LRR 5"
FT REPEAT 208..234
FT /note="LRR 6"
FT REPEAT 256..279
FT /note="LRR 7"
FT REPEAT 280..304
FT /note="LRR 8"
FT REPEAT 305..327
FT /note="LRR 9"
FT REPEAT 329..352
FT /note="LRR 10"
FT REPEAT 354..376
FT /note="LRR 11"
FT REPEAT 516..539
FT /note="LRR 12"
FT DOMAIN 678..960
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 989..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 805
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 684..692
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 667
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 751
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 839
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 844
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 852
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
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 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 392..1014
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.4"
FT /id="VSP_038292"
SQ SEQUENCE 1014 AA; 112902 MW; 28030F4118203E06 CRC64;
MIYLHRIYFI IVLFTLIFHG RLGFSDNNKL HEAEVRALKE IGKKLGKKDW DFNKDPCSGE
GTWIVTTYTT KGFESNITCD CSFLPQNSSC HVIRIALKSQ NLTGIVPPEF SKLRHLKVLD
LSRNSLTGSI PKEWASMRLE DLSFMGNRLS GPFPKVLTRL TMLRNLSLEG NQFSGPIPPD
IGQLVHLEKL HLPSNAFTGP LTEKLGLLKN LTDMRISDNN FTGPIPDFIS NWTRILKLQM
HGCGLDGPIP SSISSLTSLT DLRISDLGGK PSSFPPLKNL ESIKTLILRK CKIIGPIPKY
IGDLKKLKTL DLSFNLLSGE IPSSFENMKK ADFIYLTGNK LTGGVPNYFV ERNKNVDVSF
NNFTDESSIP SHDCNRVTSN LVESFALGNK SHKGSTCFLQ RMPCVHPKRY HLYKLYINCG
GGEVKVDKEI TYQADDEPKG ASMYVLGANK RWALSSTGNF MDNDDDADEY TVQNTSRLSV
NASSPSFGLY RTARVSPLSL TYYGICLGNG NYTVNLHFAE IIFTDDNTLY SLGKRLFDIY
VQDQLVIKNF NIQEAARGSG KPIIKSFLVN VTDHTLKIGL RWAGKGTTGI PIRGVYGPMI
SAISVEPNFK PPVYYDTKDI ILKVGVPVAA ATLLLFIIVG VFWKKRRDKN DIDKELRGLD
LQTGTFTLRQ IKAATDNFDV TRKIGEGGFG SVYKGELSEG KLIAVKQLSA KSRQGNREFV
NEIGMISALQ HPNLVKLYGC CVEGNQLILV YEYLENNCLS RALFGKDESS RLKLDWSTRK
KIFLGIAKGL TFLHEESRIK IVHRDIKASN VLLDKDLNAK ISDFGLAKLN DDGNTHISTR
IAGTIGYMAP EYAMRGYLTE KADVYSFGVV ALEIVSGKSN TNFRPTEDFV YLLDWAYVLQ
ERGSLLELVD PTLASDYSEE EAMLMLNVAL MCTNASPTLR PTMSQVVSLI EGKTAMQELL
SDPSFSTVNP KLKALRNHFW QNELSRSLSF STSGPRTASA NSLVDAEEKT GLLD
