Y1723_ARATH
ID Y1723_ARATH Reviewed; 1101 AA.
AC Q9SHI2; Q8GX06;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Leucine-rich repeat receptor-like serine/threonine-protein kinase At1g17230;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g17230; ORFNames=F20D23.7;
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] OF 213-1101.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 Q9SHI2; C0LGE0: At1g07650; NbExp=3; IntAct=EBI-20651261, EBI-16954597;
CC Q9SHI2; C0LGJ1: At1g74360; NbExp=3; IntAct=EBI-20651261, EBI-20652666;
CC Q9SHI2; C0LGK9: At2g24230; NbExp=3; IntAct=EBI-20651261, EBI-16965118;
CC Q9SHI2; Q9LT96: At5g49770; NbExp=3; IntAct=EBI-20651261, EBI-17123993;
CC Q9SHI2; Q9ZPS9: BRL2; NbExp=4; IntAct=EBI-20651261, EBI-2292728;
CC Q9SHI2; C0LGF4: FEI1; NbExp=2; IntAct=EBI-20651261, EBI-16896366;
CC Q9SHI2; C0LGN2: LRR-RLK; NbExp=3; IntAct=EBI-20651261, EBI-20652801;
CC Q9SHI2; P43298: TMK1; NbExp=3; IntAct=EBI-20651261, EBI-2023970;
CC Q9SHI2; Q9FYK0: TMK2; NbExp=4; IntAct=EBI-20651261, EBI-20652836;
CC Q9SHI2; Q9SIT1: TMK3; NbExp=4; IntAct=EBI-20651261, EBI-16896864;
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=BAC43119.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC43119.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC43119.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AC007651; AAD50027.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29561.1; -; Genomic_DNA.
DR EMBL; AK118516; BAC43119.1; ALT_SEQ; mRNA.
DR PIR; E86308; E86308.
DR RefSeq; NP_001322898.1; NM_001332283.1.
DR RefSeq; NP_173166.2; NM_101584.4.
DR AlphaFoldDB; Q9SHI2; -.
DR SMR; Q9SHI2; -.
DR BioGRID; 23534; 14.
DR IntAct; Q9SHI2; 24.
DR STRING; 3702.AT1G17230.1; -.
DR PaxDb; Q9SHI2; -.
DR PRIDE; Q9SHI2; -.
DR ProteomicsDB; 242444; -.
DR EnsemblPlants; AT1G17230.1; AT1G17230.1; AT1G17230.
DR GeneID; 838294; -.
DR Gramene; AT1G17230.1; AT1G17230.1; AT1G17230.
DR KEGG; ath:AT1G17230; -.
DR Araport; AT1G17230; -.
DR TAIR; locus:2020417; AT1G17230.
DR eggNOG; ENOG502QPT1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9SHI2; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9SHI2; -.
DR PRO; PR:Q9SHI2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SHI2; differential.
DR Genevisible; Q9SHI2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; -; 3.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1101
FT /note="Leucine-rich repeat receptor-like serine/threonine-
FT protein kinase At1g17230"
FT /id="PRO_0000403348"
FT TOPO_DOM 24..734
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 756..1101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 66..90
FT /note="LRR 1"
FT REPEAT 91..115
FT /note="LRR 2"
FT REPEAT 117..137
FT /note="LRR 3"
FT REPEAT 138..162
FT /note="LRR 4"
FT REPEAT 163..186
FT /note="LRR 5"
FT REPEAT 188..210
FT /note="LRR 6"
FT REPEAT 211..234
FT /note="LRR 7"
FT REPEAT 235..258
FT /note="LRR 8"
FT REPEAT 260..282
FT /note="LRR 9"
FT REPEAT 283..306
FT /note="LRR 10"
FT REPEAT 308..329
FT /note="LRR 11"
FT REPEAT 330..354
FT /note="LRR 12"
FT REPEAT 355..379
FT /note="LRR 13"
FT REPEAT 381..402
FT /note="LRR 14"
FT REPEAT 403..426
FT /note="LRR 15"
FT REPEAT 427..450
FT /note="LRR 16"
FT REPEAT 451..474
FT /note="LRR 17"
FT REPEAT 476..498
FT /note="LRR 18"
FT REPEAT 499..522
FT /note="LRR 19"
FT REPEAT 524..546
FT /note="LRR 20"
FT REPEAT 548..569
FT /note="LRR 21"
FT REPEAT 570..593
FT /note="LRR 22"
FT REPEAT 595..618
FT /note="LRR 23"
FT REPEAT 619..643
FT /note="LRR 24"
FT REPEAT 644..667
FT /note="LRR 25"
FT REPEAT 669..692
FT /note="LRR 26"
FT DOMAIN 799..1081
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1076..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 926
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 805..813
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 827
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 788
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 796
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 874
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 913
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 968
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 975
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 976
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
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 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1101 AA; 122100 MW; B1ECEFC99967320B CRC64;
MRGRICFLAI VILCSFSFIL VRSLNEEGRV LLEFKAFLND SNGYLASWNQ LDSNPCNWTG
IACTHLRTVT SVDLNGMNLS GTLSPLICKL HGLRKLNVST NFISGPIPQD LSLCRSLEVL
DLCTNRFHGV IPIQLTMIIT LKKLYLCENY LFGSIPRQIG NLSSLQELVI YSNNLTGVIP
PSMAKLRQLR IIRAGRNGFS GVIPSEISGC ESLKVLGLAE NLLEGSLPKQ LEKLQNLTDL
ILWQNRLSGE IPPSVGNISR LEVLALHENY FTGSIPREIG KLTKMKRLYL YTNQLTGEIP
REIGNLIDAA EIDFSENQLT GFIPKEFGHI LNLKLLHLFE NILLGPIPRE LGELTLLEKL
DLSINRLNGT IPQELQFLPY LVDLQLFDNQ LEGKIPPLIG FYSNFSVLDM SANSLSGPIP
AHFCRFQTLI LLSLGSNKLS GNIPRDLKTC KSLTKLMLGD NQLTGSLPIE LFNLQNLTAL
ELHQNWLSGN ISADLGKLKN LERLRLANNN FTGEIPPEIG NLTKIVGFNI SSNQLTGHIP
KELGSCVTIQ RLDLSGNKFS GYIAQELGQL VYLEILRLSD NRLTGEIPHS FGDLTRLMEL
QLGGNLLSEN IPVELGKLTS LQISLNISHN NLSGTIPDSL GNLQMLEILY LNDNKLSGEI
PASIGNLMSL LICNISNNNL VGTVPDTAVF QRMDSSNFAG NHGLCNSQRS HCQPLVPHSD
SKLNWLINGS QRQKILTITC IVIGSVFLIT FLGLCWTIKR REPAFVALED QTKPDVMDSY
YFPKKGFTYQ GLVDATRNFS EDVVLGRGAC GTVYKAEMSG GEVIAVKKLN SRGEGASSDN
SFRAEISTLG KIRHRNIVKL YGFCYHQNSN LLLYEYMSKG SLGEQLQRGE KNCLLDWNAR
YRIALGAAEG LCYLHHDCRP QIVHRDIKSN NILLDERFQA HVGDFGLAKL IDLSYSKSMS
AVAGSYGYIA PEYAYTMKVT EKCDIYSFGV VLLELITGKP PVQPLEQGGD LVNWVRRSIR
NMIPTIEMFD ARLDTNDKRT VHEMSLVLKI ALFCTSNSPA SRPTMREVVA MITEARGSSS
LSSSSITSET PLEEANSSKE I
