Y3475_ARATH
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 03-AUG-2022, entry version 88.
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.AT3G47570.1; -.
DR iPTMnet; C0LGP4; -.
DR PaxDb; C0LGP4; -.
DR PRIDE; C0LGP4; -.
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; locus:2079142; AT3G47570.
DR eggNOG; ENOG502QPYS; Eukaryota.
DR HOGENOM; CLU_000288_22_0_1; -.
DR InParanoid; C0LGP4; -.
DR OMA; FQLKPCL; -.
DR OrthoDB; 335055at2759; -.
DR PhylomeDB; C0LGP4; -.
DR PRO; PR:C0LGP4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; C0LGP4; baseline and differential.
DR Genevisible; C0LGP4; 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; -; 4.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
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 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
