Y5596_ARATH
ID Y5596_ARATH Reviewed; 887 AA.
AC Q9FN93;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At5g59680;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g59680; ORFNames=MTH12.14;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 Q9FN93; C0LGS3: At4g37250; NbExp=2; IntAct=EBI-20653513, EBI-16955335;
CC Q9FN93; Q9FRI1: LRR-RLK; NbExp=2; IntAct=EBI-20653513, EBI-17071528;
CC Q9FN93; Q94AG2: SERK1; NbExp=2; IntAct=EBI-20653513, EBI-1555537;
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}.
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DR EMBL; AB006705; BAB09506.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97219.1; -; Genomic_DNA.
DR EMBL; FJ708808; ACN59399.1; -; mRNA.
DR RefSeq; NP_200776.2; NM_125360.3.
DR AlphaFoldDB; Q9FN93; -.
DR SMR; Q9FN93; -.
DR BioGRID; 21333; 32.
DR IntAct; Q9FN93; 35.
DR STRING; 3702.AT5G59680.1; -.
DR PaxDb; Q9FN93; -.
DR PRIDE; Q9FN93; -.
DR ProteomicsDB; 243165; -.
DR EnsemblPlants; AT5G59680.1; AT5G59680.1; AT5G59680.
DR GeneID; 836089; -.
DR Gramene; AT5G59680.1; AT5G59680.1; AT5G59680.
DR KEGG; ath:AT5G59680; -.
DR Araport; AT5G59680; -.
DR TAIR; locus:2174304; AT5G59680.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; Q9FN93; -.
DR OMA; SNKLQVC; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FN93; -.
DR PRO; PR:Q9FN93; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN93; baseline and differential.
DR Genevisible; Q9FN93; 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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF00069; Pkinase; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..887
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At5g59680"
FT /id="PRO_0000387566"
FT TOPO_DOM 25..510
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 411..434
FT /note="LRR 1"
FT REPEAT 435..457
FT /note="LRR 2"
FT REPEAT 459..481
FT /note="LRR 3"
FT DOMAIN 580..853
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 705
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 586..594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 608
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 571
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 653
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 740
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 745
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 753
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 887 AA; 98369 MW; 945AA8FD1E76583C CRC64;
MERSLELLLL LIRTLAIIHI SQAQSQQGFI SLDCGLPANE PSPYTEPRTG LQFSSDAAFI
QSGKIGRIQA NLEADFLKPS TTMRYFPDGK RNCYNLNVEK GRNHLIRARF VYGNYDGRDT
GPKFDLYLGP NPWATIDLAK QVNGTRPEIM HIPTSNKLQV CLVKTGETTP LISVLEVRPM
GSGTYLTKSG SLKLYYREYF SKSDSSLRYP DDIYDRQWTS FFDTEWTQIN TTSDVGNSND
YKPPKVALTT AAIPTNASAP LTNEWSSVNP DEQYYVYAHF SEIQELQANE TREFNMLLNG
KLFFGPVVPP KLAISTILSV SPNTCEGGEC NLQLIRTNRS TLPPLLNAYE VYKVIQFPQL
ETNETDVSAV KNIQATYELS RINWQSDPCV PQQFMWDGLN CSITDITTPP RITTLNLSSS
GLTGTITAAI QNLTTLEKLD LSNNNLTGEV PEFLSNMKSL LVINLSGNDL NGTIPQSLQR
KGLELLYQGN PRLISPGSTE TKSGKSFPVT IVASVGSAAI LIVVLVLVLF LRKKKPSAVE
VVLPRPSRPT MNVPYANSPE PSIEMKKRKF TYSEVTKMTN NFGRVVGEGG FGVVCHGTVN
GSEQVAVKLL SQSSTQGYKE FKAEVDLLLR VHHTNLVSLV GYCDEGDHLA LIYEFVPNGD
LRQHLSGKGG KPIVNWGTRL RIAAEAALGL EYLHIGCTPP MVHRDVKTTN ILLDEHYKAK
LADFGLSRSF PVGGESHVST VIAGTPGYLD PEYYHTSRLS EKSDVYSFGI VLLEMITNQA
VIDRNRRKSH ITQWVGSELN GGDIAKIMDL KLNGDYDSRS AWRALELAMS CADPTSARRP
TMSHVVIELK ECLVSENSRR NMSRGMDTLS SPEVSMIFDA EMIPRAR
