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Y1677_ARATH
ID   Y1677_ARATH             Reviewed;         929 AA.
AC   C0LGI2; Q9FXD7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g67720;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g67720; ORFNames=F12A21.30;
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=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       C0LGI2; Q9LIG2: At3g21340; NbExp=2; IntAct=EBI-17070892, EBI-941096;
CC       C0LGI2; Q9LRT1: At3g28040; NbExp=2; IntAct=EBI-17070892, EBI-16956175;
CC       C0LGI2; Q8GX94: LRR-RLK; NbExp=2; IntAct=EBI-17070892, EBI-16955556;
CC       C0LGI2; Q9LZV7: PXC2; NbExp=2; IntAct=EBI-17070892, EBI-1238200;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG28906.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC008113; AAG28906.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE34687.1; -; Genomic_DNA.
DR   EMBL; FJ708672; ACN59267.1; -; mRNA.
DR   RefSeq; NP_564904.1; NM_105440.2.
DR   AlphaFoldDB; C0LGI2; -.
DR   SMR; C0LGI2; -.
DR   BioGRID; 28318; 30.
DR   IntAct; C0LGI2; 30.
DR   STRING; 3702.AT1G67720.1; -.
DR   PaxDb; C0LGI2; -.
DR   PRIDE; C0LGI2; -.
DR   ProteomicsDB; 243033; -.
DR   EnsemblPlants; AT1G67720.1; AT1G67720.1; AT1G67720.
DR   GeneID; 843097; -.
DR   Gramene; AT1G67720.1; AT1G67720.1; AT1G67720.
DR   KEGG; ath:AT1G67720; -.
DR   Araport; AT1G67720; -.
DR   TAIR; locus:2008565; AT1G67720.
DR   eggNOG; ENOG502QSBF; Eukaryota.
DR   HOGENOM; CLU_000288_41_3_1; -.
DR   InParanoid; C0LGI2; -.
DR   OMA; CVEQHGV; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; C0LGI2; -.
DR   PRO; PR:C0LGI2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; C0LGI2; baseline and differential.
DR   Genevisible; C0LGI2; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR024788; Malectin-like_Carb-bd_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; PF13855; LRR_8; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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   ATP-binding; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..929
FT                   /note="Probable LRR receptor-like serine/threonine-protein
FT                   kinase At1g67720"
FT                   /id="PRO_0000387539"
FT   TOPO_DOM        22..531
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        532..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        553..929
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          413..437
FT                   /note="LRR 1"
FT   REPEAT          438..460
FT                   /note="LRR 2"
FT   REPEAT          461..484
FT                   /note="LRR 3"
FT   REPEAT          485..508
FT                   /note="LRR 4"
FT   DOMAIN          606..880
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        731
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         612..620
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         679
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         764
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         770
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         778
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   929 AA;  103753 MW;  AC460DA336D01A4E CRC64;
     MGLCLAQLAV TCLFLVPFVL SQVTEFVSID CGCSSNYTDP RTGLGWVSDS EIIKQGKPVT
     LANTNWNSMQ YRRRRDFPTD NKKYCYRLST KERRRYIVRT TFLYGGLGSE EAYPKFQLYL
     DATKWATVTI QEVSRVYVEE LIVRATSSYV DVCVCCAITG SPFMSTLELR PLNLSMYATD
     YEDNFFLKVA ARVNFGAPNM DALRYPDDPY DRIWESDINK RPNYLVGVAP GTTRINTSKT
     INTLTREYPP MKVMQTAVVG TQGLISYRLN LEDFPANARA YAYFAEIEEL GANETRKFKL
     VQPYFPDYSN AVVNIAENAN GSYTLYEPSY MNVTLDFVLT FSFGKTKDST QGPLLNAIEI
     SKYLPISVKT DRSDVSVLDA IRSMSPDSDW ASEGGDPCIP VLWSWVNCSS TSPPRVTKIA
     LSRKNLRGEI PPGINYMEAL TELWLDDNEL TGTLPDMSKL VNLKIMHLEN NQLSGSLPPY
     LAHLPNLQEL SIENNSFKGK IPSALLKGKV LFKYNNNPEL QNEAQRKHFW QILGISIAAV
     AILLLLVGGS LVLLCALRKT KRADKGDSTE TKKKGLVAYS AVRGGHLLDE GVAYFISLPV
     LEEATDNFSK KVGRGSFGSV YYGRMKDGKE VAVKITADPS SHLNRQFVTE VALLSRIHHR
     NLVPLIGYCE EADRRILVYE YMHNGSLGDH LHGSSDYKPL DWLTRLQIAQ DAAKGLEYLH
     TGCNPSIIHR DVKSSNILLD INMRAKVSDF GLSRQTEEDL THVSSVAKGT VGYLDPEYYA
     SQQLTEKSDV YSFGVVLFEL LSGKKPVSAE DFGPELNIVH WARSLIRKGD VCGIIDPCIA
     SNVKIESVWR VAEVANQCVE QRGHNRPRMQ EVIVAIQDAI RIERGNENGL KSSSSSSSKA
     QSSRKTLLTS FLELESPDIS RNSLAPAAR
 
 
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