Y1743_ARATH
ID Y1743_ARATH Reviewed; 1106 AA.
AC C0LGJ1; Q9CA77;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g74360;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g74360; ORFNames=F1M20.4;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
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 C0LGJ1; Q9M9S4: At1g14390; NbExp=2; IntAct=EBI-20652666, EBI-16954682;
CC C0LGJ1; Q9SHI2: At1g17230; NbExp=3; IntAct=EBI-20652666, EBI-20651261;
CC C0LGJ1; Q9FL63: At5g24100; NbExp=3; IntAct=EBI-20652666, EBI-20657062;
CC C0LGJ1; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-20652666, EBI-16914444;
CC C0LGJ1; Q9LVI6: RLK902; NbExp=4; IntAct=EBI-20652666, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:14671022}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:14671022}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52362.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011765; AAG52362.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35582.1; -; Genomic_DNA.
DR EMBL; FJ708681; ACN59276.1; -; mRNA.
DR PIR; C96772; C96772.
DR RefSeq; NP_565084.1; NM_106096.4.
DR AlphaFoldDB; C0LGJ1; -.
DR SMR; C0LGJ1; -.
DR BioGRID; 28996; 21.
DR IntAct; C0LGJ1; 26.
DR STRING; 3702.AT1G74360.1; -.
DR PaxDb; C0LGJ1; -.
DR PRIDE; C0LGJ1; -.
DR ProteomicsDB; 242987; -.
DR EnsemblPlants; AT1G74360.1; AT1G74360.1; AT1G74360.
DR GeneID; 843777; -.
DR Gramene; AT1G74360.1; AT1G74360.1; AT1G74360.
DR KEGG; ath:AT1G74360; -.
DR Araport; AT1G74360; -.
DR TAIR; locus:2019255; AT1G74360.
DR eggNOG; ENOG502QQCM; Eukaryota.
DR HOGENOM; CLU_000288_22_9_1; -.
DR InParanoid; C0LGJ1; -.
DR OMA; GECLAMK; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; C0LGJ1; -.
DR PRO; PR:C0LGJ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGJ1; baseline and differential.
DR Genevisible; C0LGJ1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0002215; P:defense response to nematode; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
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; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 12.
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 Mitochondrion; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1106
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g74360"
FT /id="PRO_0000387542"
FT TOPO_DOM 35..736
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 758..1106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 86..109
FT /note="LRR 1"
FT REPEAT 110..134
FT /note="LRR 2"
FT REPEAT 136..156
FT /note="LRR 3"
FT REPEAT 157..182
FT /note="LRR 4"
FT REPEAT 184..204
FT /note="LRR 5"
FT REPEAT 205..226
FT /note="LRR 6"
FT REPEAT 227..250
FT /note="LRR 7"
FT REPEAT 252..275
FT /note="LRR 8"
FT REPEAT 276..299
FT /note="LRR 9"
FT REPEAT 300..323
FT /note="LRR 10"
FT REPEAT 325..346
FT /note="LRR 11"
FT REPEAT 348..371
FT /note="LRR 12"
FT REPEAT 372..396
FT /note="LRR 13"
FT REPEAT 398..419
FT /note="LRR 14"
FT REPEAT 420..443
FT /note="LRR 15"
FT REPEAT 445..468
FT /note="LRR 16"
FT REPEAT 470..492
FT /note="LRR 17"
FT REPEAT 566..593
FT /note="LRR 18"
FT REPEAT 594..617
FT /note="LRR 19"
FT REPEAT 619..640
FT /note="LRR 20"
FT REPEAT 641..664
FT /note="LRR 21"
FT REPEAT 666..690
FT /note="LRR 22"
FT DOMAIN 814..1095
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 941
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 820..828
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 842
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 803
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 811
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 983
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 991
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1106 AA; 121895 MW; AC2A30540EFDCFEF CRC64;
MTMVTRVIMT DDDSQSLCFL CFLLFFFITA IAVAGDSLDS DREVLLSLKS YLESRNPQNR
GLYTEWKMEN QDVVCQWPGI ICTPQRSRVT GINLTDSTIS GPLFKNFSAL TELTYLDLSR
NTIEGEIPDD LSRCHNLKHL NLSHNILEGE LSLPGLSNLE VLDLSLNRIT GDIQSSFPLF
CNSLVVANLS TNNFTGRIDD IFNGCRNLKY VDFSSNRFSG EVWTGFGRLV EFSVADNHLS
GNISASMFRG NCTLQMLDLS GNAFGGEFPG QVSNCQNLNV LNLWGNKFTG NIPAEIGSIS
SLKGLYLGNN TFSRDIPETL LNLTNLVFLD LSRNKFGGDI QEIFGRFTQV KYLVLHANSY
VGGINSSNIL KLPNLSRLDL GYNNFSGQLP TEISQIQSLK FLILAYNNFS GDIPQEYGNM
PGLQALDLSF NKLTGSIPAS FGKLTSLLWL MLANNSLSGE IPREIGNCTS LLWFNVANNQ
LSGRFHPELT RMGSNPSPTF EVNRQNKDKI IAGSGECLAM KRWIPAEFPP FNFVYAILTK
KSCRSLWDHV LKGYGLFPVC SAGSTVRTLK ISAYLQLSGN KFSGEIPASI SQMDRLSTLH
LGFNEFEGKL PPEIGQLPLA FLNLTRNNFS GEIPQEIGNL KCLQNLDLSF NNFSGNFPTS
LNDLNELSKF NISYNPFISG AIPTTGQVAT FDKDSFLGNP LLRFPSFFNQ SGNNTRKISN
QVLGNRPRTL LLIWISLALA LAFIACLVVS GIVLMVVKAS REAEIDLLDG SKTRHDMTSS
SGGSSPWLSG KIKVIRLDKS TFTYADILKA TSNFSEERVV GRGGYGTVYR GVLPDGREVA
VKKLQREGTE AEKEFRAEME VLSANAFGDW AHPNLVRLYG WCLDGSEKIL VHEYMGGGSL
EELITDKTKL QWKKRIDIAT DVARGLVFLH HECYPSIVHR DVKASNVLLD KHGNARVTDF
GLARLLNVGD SHVSTVIAGT IGYVAPEYGQ TWQATTRGDV YSYGVLTMEL ATGRRAVDGG
EECLVEWARR VMTGNMTAKG SPITLSGTKP GNGAEQMTEL LKIGVKCTAD HPQARPNMKE
VLAMLVKISG KAELFNGLSS QGYIEM
