ID Y1561_ARATH Reviewed; 1032 AA.
AC C0LGH2; Q9C7J1; Q9SGT9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g56130;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g56130; ORFNames=F14G9.25, T6H22.8;
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=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 {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C0LGH2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0LGH2-2; Sequence=VSP_038283, VSP_038284;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02838.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50912.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009894; AAF02838.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069159; AAG50912.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; ANM59201.1; -; Genomic_DNA.
DR EMBL; FJ708662; ACN59257.1; -; mRNA.
DR PIR; F96602; F96602.
DR RefSeq; NP_176009.1; NM_104491.2. [C0LGH2-1]
DR AlphaFoldDB; C0LGH2; -.
DR SMR; C0LGH2; -.
DR BioGRID; 27290; 20.
DR IntAct; C0LGH2; 20.
DR STRING; 3702.C0LGH2; -.
DR PaxDb; 3702-AT1G56130-1; -.
DR ProteomicsDB; 242390; -. [C0LGH2-1]
DR EnsemblPlants; AT1G56130.2; AT1G56130.2; AT1G56130. [C0LGH2-1]
DR GeneID; 842065; -.
DR Gramene; AT1G56130.2; AT1G56130.2; AT1G56130. [C0LGH2-1]
DR KEGG; ath:AT1G56130; -.
DR Araport; AT1G56130; -.
DR TAIR; AT1G56130; -.
DR eggNOG; ENOG502QUW9; Eukaryota.
DR HOGENOM; CLU_000288_114_1_1; -.
DR InParanoid; C0LGH2; -.
DR OMA; LEWAWYL; -.
DR OrthoDB; 382610at2759; -.
DR PhylomeDB; C0LGH2; -.
DR PRO; PR:C0LGH2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGH2; baseline and differential.
DR Genevisible; C0LGH2; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR021720; Malectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48006:SF94; LEUCINE-RICH REPEAT TRANSMEMBRANE PROTEIN KINASE; 1.
DR PANTHER; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1032
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g56130"
FT /id="PRO_0000387535"
FT TOPO_DOM 30..636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..1032
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 101..122
FT /note="LRR 1"
FT REPEAT 123..146
FT /note="LRR 2"
FT REPEAT 148..170
FT /note="LRR 3"
FT REPEAT 171..194
FT /note="LRR 4"
FT REPEAT 196..217
FT /note="LRR 5"
FT REPEAT 242..265
FT /note="LRR 6"
FT REPEAT 290..314
FT /note="LRR 7"
FT REPEAT 315..338
FT /note="LRR 8"
FT REPEAT 340..360
FT /note="LRR 9"
FT REPEAT 361..385
FT /note="LRR 10"
FT DOMAIN 694..968
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1008..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 818
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 700..708
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 722
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 683
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 767
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 852
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 857
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 865
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
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 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 509..522
FT /note="YYGLGLENGGYTVT -> FYFYHLERFGTTTF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20064227"
FT /id="VSP_038283"
FT VAR_SEQ 523..1032
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20064227"
FT /id="VSP_038284"
FT CONFLICT 151
FT /note="W -> WI (in Ref. 1; AAG50912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1032 AA; 113042 MW; 8E0AC1A89E52142E CRC64;
MTRIRRSPCL LLLIIWFMCI AGSVQVVQSQ NQTGATTHPD EARALNSIFA AWKIQAPREW
NISGELCSGA AIDASVLDSN PAYNPLIKCD CSFQNSTICR ITNIKVYAID VVGPIPPELW
TLTYLTNLNL GQNVLTGSLP PAIGNLTRMQ WMTFGINALS GPVPKEIGLL TDLRLLGISS
NNFSGSIPDE IGRCTKLQQM YIDSSGLSGR IPLSFANLVQ LEQAWIADLE VTDQIPDFIG
DWTKLTTLRI IGTGLSGPIP SSFSNLTSLT ELRLGDISSG SSSLDFIKDM KSLSVLVLRN
NNLTGTIPST IGEHSSLRQV DLSFNKLHGP IPASLFNLSQ LTHLFLGNNT LNGSFPTQKT
QSLRNVDVSY NDLSGSLPSW VSLPSLKLNL VANNFTLEGL DNRVLPGLNC LQKNFPCNRG
KGIYSDFSIN CGGPEKRSVT GALFEREDED FGPASFFVSA GQRWAASSVG LFAGSSNNIY
IATSQSQFVN TLDSELFQSA RLSASSVRYY GLGLENGGYT VTLQFAEIQI LGSTSTTWKG
LGRRRFDIYV QGRLVEKDFD VRRTAGDSTV RAVQRVYKAN VSENHLEVHL FWAGKGTCCI
PIQGAYGPLI SAVSATPDFT PTVANKPPSK GKNRTGTIVG VIVGVGLLSI LAGVVMFTIR
KRRKRYTDDE ELLGMDVKPY IFTYSELKSA TQDFDPSNKL GEGGFGPVYK GNLNDGRVVA
VKLLSVGSRQ GKGQFVAEIV AISSVLHRNL VKLYGCCFEG EHRMLVYEYL PNGSLDQALF
GDKTLHLDWS TRYEICLGVA RGLVYLHEEA SVRIVHRDVK ASNILLDSRL VPQISDFGLA
KLYDDKKTHI STRVAGTIGY LAPEYAMRGH LTEKTDVYAF GVVALELVSG RPNSDENLEE
EKKYLLEWAW NLHEKSRDIE LIDDKLTDFN MEEAKRMIGI ALLCTQTSHA LRPPMSRVVA
MLSGDVEIGD VTSKPGYVSD WRFDDTTGSS LSGFQIKDTT GYSMSLVAPG SEISPRDSDF
KPMLGSKINE GR
//
