ID   Y3475_ARATH             Reviewed;        1010 AA.
AC   C0LGP4; Q8VZM3; Q9SN81;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At3g47570;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g47570; ORFNames=F1P2.120;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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   -!- 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=CAB61983.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL132955; CAB61983.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE78303.1; -; Genomic_DNA.
DR   EMBL; AY064013; AAL36369.1; -; mRNA.
DR   EMBL; FJ708735; ACN59329.1; -; mRNA.
DR   PIR; T45717; T45717.
DR   RefSeq; NP_566892.1; NM_114625.3.
DR   AlphaFoldDB; C0LGP4; -.
DR   SMR; C0LGP4; -.
DR   BioGRID; 9231; 5.
DR   IntAct; C0LGP4; 5.
DR   STRING; 3702.C0LGP4; -.
DR   iPTMnet; C0LGP4; -.
DR   PaxDb; 3702-AT3G47570-1; -.
DR   ProteomicsDB; 234609; -.
DR   EnsemblPlants; AT3G47570.1; AT3G47570.1; AT3G47570.
DR   GeneID; 823911; -.
DR   Gramene; AT3G47570.1; AT3G47570.1; AT3G47570.
DR   KEGG; ath:AT3G47570; -.
DR   Araport; AT3G47570; -.
DR   TAIR; AT3G47570; -.
DR   eggNOG; ENOG502QPYS; Eukaryota.
DR   HOGENOM; CLU_000288_22_0_1; -.
DR   InParanoid; C0LGP4; -.
DR   OMA; FQLKPCL; -.
DR   OrthoDB; 382073at2759; -.
DR   PhylomeDB; C0LGP4; -.
DR   PRO; PR:C0LGP4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; C0LGP4; baseline and differential.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; 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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27008:SF526; (RAPE) HYPOTHETICAL PROTEIN; 1.
DR   PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 9.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; C0LGP4; AT.
PE   2: Evidence at transcript 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1010
FT                   /note="Probable LRR receptor-like serine/threonine-protein
FT                   kinase At3g47570"
FT                   /id="PRO_0000387551"
FT   TOPO_DOM        20..645
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        646..666
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        667..1010
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          89..113
FT                   /note="LRR 1"
FT   REPEAT          114..137
FT                   /note="LRR 2"
FT   REPEAT          139..161
FT                   /note="LRR 3"
FT   REPEAT          162..185
FT                   /note="LRR 4"
FT   REPEAT          186..209
FT                   /note="LRR 5"
FT   REPEAT          211..233
FT                   /note="LRR 6"
FT   REPEAT          234..258
FT                   /note="LRR 7"
FT   REPEAT          259..282
FT                   /note="LRR 8"
FT   REPEAT          283..307
FT                   /note="LRR 9"
FT   REPEAT          310..333
FT                   /note="LRR 10"
FT   REPEAT          335..359
FT                   /note="LRR 11"
FT   REPEAT          361..384
FT                   /note="LRR 12"
FT   REPEAT          385..408
FT                   /note="LRR 13"
FT   REPEAT          410..432
FT                   /note="LRR 14"
FT   REPEAT          433..455
FT                   /note="LRR 15"
FT   REPEAT          457..480
FT                   /note="LRR 16"
FT   REPEAT          481..504
FT                   /note="LRR 17"
FT   REPEAT          505..528
FT                   /note="LRR 18"
FT   REPEAT          530..551
FT                   /note="LRR 19"
FT   REPEAT          552..574
FT                   /note="LRR 20"
FT   REPEAT          575..600
FT                   /note="LRR 21"
FT   DOMAIN          702..1002
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        839
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         708..716
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         731
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         699
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         781
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         826
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   MOD_RES         887
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        582
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        600
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        995
FT                   /note="I -> V (in Ref. 3; AAL36369)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1010 AA;  110901 MW;  5B06436E11E9F879 CRC64;
     MRLFLLLAFN ALMLLETHGF TDETDRQALL QFKSQVSEDK RVVLSSWNHS FPLCNWKGVT
     CGRKNKRVTH LELGRLQLGG VISPSIGNLS FLVSLDLYEN FFGGTIPQEV GQLSRLEYLD
     MGINYLRGPI PLGLYNCSRL LNLRLDSNRL GGSVPSELGS LTNLVQLNLY GNNMRGKLPT
     SLGNLTLLEQ LALSHNNLEG EIPSDVAQLT QIWSLQLVAN NFSGVFPPAL YNLSSLKLLG
     IGYNHFSGRL RPDLGILLPN LLSFNMGGNY FTGSIPTTLS NISTLERLGM NENNLTGSIP
     TFGNVPNLKL LFLHTNSLGS DSSRDLEFLT SLTNCTQLET LGIGRNRLGG DLPISIANLS
     AKLVTLDLGG TLISGSIPYD IGNLINLQKL ILDQNMLSGP LPTSLGKLLN LRYLSLFSNR
     LSGGIPAFIG NMTMLETLDL SNNGFEGIVP TSLGNCSHLL ELWIGDNKLN GTIPLEIMKI
     QQLLRLDMSG NSLIGSLPQD IGALQNLGTL SLGDNKLSGK LPQTLGNCLT MESLFLEGNL
     FYGDIPDLKG LVGVKEVDLS NNDLSGSIPE YFASFSKLEY LNLSFNNLEG KVPVKGIFEN
     ATTVSIVGNN DLCGGIMGFQ LKPCLSQAPS VVKKHSSRLK KVVIGVSVGI TLLLLLFMAS
     VTLIWLRKRK KNKETNNPTP STLEVLHEKI SYGDLRNATN GFSSSNMVGS GSFGTVYKAL
     LLTEKKVVAV KVLNMQRRGA MKSFMAECES LKDIRHRNLV KLLTACSSID FQGNEFRALI
     YEFMPNGSLD MWLHPEEVEE IHRPSRTLTL LERLNIAIDV ASVLDYLHVH CHEPIAHCDL
     KPSNVLLDDD LTAHVSDFGL ARLLLKFDEE SFFNQLSSAG VRGTIGYAAP EYGVGGQPSI
     NGDVYSFGIL LLEMFTGKRP TNELFGGNFT LNSYTKSALP ERILDIVDES ILHIGLRVGF
     PVVECLTMVF EVGLRCCEES PMNRLATSIV VKELISIRER FFKASRTTWR
//