Y1124_ARATH
ID Y1124_ARATH Reviewed; 882 AA.
AC C0LGE4; B9DI39; Q84WP1; Q9LN92; Q9LN98;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g12460;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g12460; ORFNames=F5O11.21, T12C24.1;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-882.
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(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 C0LGE4; A0A178WLG7: At1g51790; NbExp=3; IntAct=EBI-17126713, EBI-20652336;
CC C0LGE4; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-17126713, EBI-20651541;
CC C0LGE4; C0LGL4: At2g28960; NbExp=3; IntAct=EBI-17126713, EBI-16946048;
CC C0LGE4; A0A1P8BAS1: At5g01950; NbExp=2; IntAct=EBI-17126713, EBI-20652362;
CC C0LGE4; Q9XIC7: SERK2; NbExp=4; IntAct=EBI-17126713, EBI-6299033;
CC C0LGE4; O64483: SIRK; NbExp=2; IntAct=EBI-17126713, EBI-16905038;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79640.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF88073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC025416; AAF79640.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC025417; AAF88073.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28886.1; -; Genomic_DNA.
DR EMBL; BT002951; AAO22764.1; -; mRNA.
DR EMBL; FJ708633; ACN59229.1; -; mRNA.
DR EMBL; AK317750; BAH20406.1; -; mRNA.
DR RefSeq; NP_172708.1; NM_101118.4.
DR AlphaFoldDB; C0LGE4; -.
DR SMR; C0LGE4; -.
DR BioGRID; 23043; 19.
DR IntAct; C0LGE4; 25.
DR STRING; 3702.AT1G12460.1; -.
DR iPTMnet; C0LGE4; -.
DR PaxDb; C0LGE4; -.
DR PRIDE; C0LGE4; -.
DR ProteomicsDB; 243181; -.
DR EnsemblPlants; AT1G12460.1; AT1G12460.1; AT1G12460.
DR GeneID; 837803; -.
DR Gramene; AT1G12460.1; AT1G12460.1; AT1G12460.
DR KEGG; ath:AT1G12460; -.
DR Araport; AT1G12460; -.
DR TAIR; locus:2034725; AT1G12460.
DR eggNOG; ENOG502QUME; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; C0LGE4; -.
DR OMA; HAAIGYI; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; C0LGE4; -.
DR PRO; PR:C0LGE4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGE4; baseline and differential.
DR Genevisible; C0LGE4; 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; IPR003591; Leu-rich_rpt_typical-subtyp.
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; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..882
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g12460"
FT /id="PRO_0000387524"
FT TOPO_DOM 22..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..882
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 92..113
FT /note="LRR 1"
FT REPEAT 116..138
FT /note="LRR 2"
FT REPEAT 140..162
FT /note="LRR 3"
FT REPEAT 165..187
FT /note="LRR 4"
FT REPEAT 189..210
FT /note="LRR 5"
FT REPEAT 213..235
FT /note="LRR 6"
FT REPEAT 237..258
FT /note="LRR 7"
FT REPEAT 261..283
FT /note="LRR 8"
FT REPEAT 285..308
FT /note="LRR 9"
FT REPEAT 309..331
FT /note="LRR 10"
FT REPEAT 333..355
FT /note="LRR 11"
FT REPEAT 357..379
FT /note="LRR 12"
FT REPEAT 381..404
FT /note="LRR 13"
FT REPEAT 405..427
FT /note="LRR 14"
FT REPEAT 429..451
FT /note="LRR 15"
FT REPEAT 453..475
FT /note="LRR 16"
FT DOMAIN 593..876
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 599..607
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 589
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 770
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 82
FT /note="T -> A (in Ref. 3; AAO22764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 882 AA; 97022 MW; 228F33D8A05028C4 CRC64;
MRKVHLFLVL VHFIYISTSR SDSISERDIL LQFKGSISDD PYNSLASWVS DGDLCNSFNG
ITCNPQGFVD KIVLWNTSLA GTLAPGLSNL KFIRVLNLFG NRFTGNLPLD YFKLQTLWTI
NVSSNALSGP IPEFISELSS LRFLDLSKNG FTGEIPVSLF KFCDKTKFVS LAHNNIFGSI
PASIVNCNNL VGFDFSYNNL KGVLPPRICD IPVLEYISVR NNLLSGDVSE EIQKCQRLIL
VDLGSNLFHG LAPFAVLTFK NITYFNVSWN RFGGEIGEIV DCSESLEFLD ASSNELTGRI
PTGVMGCKSL KLLDLESNKL NGSIPGSIGK MESLSVIRLG NNSIDGVIPR DIGSLEFLQV
LNLHNLNLIG EVPEDISNCR VLLELDVSGN DLEGKISKKL LNLTNIKILD LHRNRLNGSI
PPELGNLSKV QFLDLSQNSL SGPIPSSLGS LNTLTHFNVS YNNLSGVIPP VPMIQAFGSS
AFSNNPFLCG DPLVTPCNSR GAAAKSRNSD ALSISVIIVI IAAAVILFGV CIVLALNLRA
RKRRKDEEIL TVETTPLASS IDSSGVIIGK LVLFSKNLPS KYEDWEAGTK ALLDKENIIG
MGSIGSVYRA SFEGGVSIAV KKLETLGRIR NQEEFEQEIG RLGGLQHPNL SSFQGYYFSS
TMQLILSEFV PNGSLYDNLH LRIFPGTSSS YGNTDLNWHR RFQIALGTAK ALSFLHNDCK
PAILHLNVKS TNILLDERYE AKLSDYGLEK FLPVMDSFGL TKKFHNAVGY IAPELAQQSL
RASEKCDVYS YGVVLLELVT GRKPVESPSE NQVLILRDYV RDLLETGSAS DCFDRRLREF
EENELIQVMK LGLLCTSENP LKRPSMAEVV QVLESIRNGF GS
