ID Y5169_ARATH Reviewed; 866 AA.
AC C0LGT5; Q9LFL1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At5g16900;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g16900; ORFNames=F2K13.50;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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).
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 C0LGT5; Q8W4S5: At5g63710; NbExp=2; IntAct=EBI-16954237, EBI-16934827;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01703.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391141; CAC01703.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92356.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70370.1; -; Genomic_DNA.
DR EMBL; FJ708779; ACN59370.1; -; mRNA.
DR PIR; T51545; T51545.
DR RefSeq; NP_001318574.1; NM_001343470.1.
DR RefSeq; NP_197192.2; NM_121696.3.
DR AlphaFoldDB; C0LGT5; -.
DR SMR; C0LGT5; -.
DR BioGRID; 16829; 38.
DR IntAct; C0LGT5; 39.
DR STRING; 3702.C0LGT5; -.
DR PaxDb; 3702-AT5G16900-1; -.
DR EnsemblPlants; AT5G16900.1; AT5G16900.1; AT5G16900.
DR EnsemblPlants; AT5G16900.3; AT5G16900.3; AT5G16900.
DR GeneID; 831553; -.
DR Gramene; AT5G16900.1; AT5G16900.1; AT5G16900.
DR Gramene; AT5G16900.3; AT5G16900.3; AT5G16900.
DR KEGG; ath:AT5G16900; -.
DR Araport; AT5G16900; -.
DR TAIR; AT5G16900; -.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; C0LGT5; -.
DR OrthoDB; 5551317at2759; -.
DR PhylomeDB; C0LGT5; -.
DR PRO; PR:C0LGT5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGT5; baseline and differential.
DR Genevisible; C0LGT5; AT.
DR GO; GO:0016020; C: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 CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025875; Leu-rich_rpt_4.
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 PANTHER; PTHR45631:SF183; BNAC02G06920D PROTEIN; 1.
DR PANTHER; PTHR45631; OS07G0107800 PROTEIN-RELATED; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
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.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..866
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At5g16900"
FT /id="PRO_0000387561"
FT TOPO_DOM 21..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 415..438
FT /note="LRR 1"
FT REPEAT 439..461
FT /note="LRR 2"
FT REPEAT 463..485
FT /note="LRR 3"
FT DOMAIN 573..846
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 698
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 579..587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 646
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 733
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 738
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 746
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
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 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
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 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 866 AA; 97252 MW; 01BBFB19555F0CFF CRC64;
MEDRHRYLFF IFAIIHYVQA QQGFISLDCG LPSNEPPYIE PVTGLVFSSD ADHIPSGISG
RIQKNLEAVH IKPYLFLRYF PDGLRNCYTL DVLQNRRYMI KAVFVYGNYD GYNDYPSFDL
YLGPNKWVRV DLEGKVNGSV EEIIHIPSSN SLQICLVKTG NSLPFISALE LRLLRNDTYV
VQDVSLKHLF RRYYRQSDRL IRYPDDVYDR VWSPFFLPEW TQITTSLDVN NSNNYEPPKA
ALTSAATPGD NGTRLTIIWT LDNPDEQIHL YVHFAELEPV GENTDEALRT LFTRTFYFVV
NGKISYDESI TPLDLAVSTV ETVVNKCDGG NCSLQLVRSE ASPGVRVPLV NAMEAFTAIK
FPHSETNPDD VISIKVIQAT YELSRVDWQG DPCLPQQFLW TGLNCSYMNM STSPRIISLD
LSSHKLTGKI VPDIQNLTQL QKLDLSNNKL TGGVPEFLAN MKSLLFINLS NNNLVGSIPQ
ALLDRKNLKL EFEGNPKLCA TGPCNSSSGN KETTVIAPVA AAIAIFIAVL VLIIVFIKKR
PSSIRALHPS RANLSLENKK RRITYSEILL MTNNFERVIG EGGFGVVYHG YLNDSEQVAV
KVLSPSSSQG YKEFKAEVEL LLRVHHINLV SLVGYCDEQA HLALIYEYMA NGDLKSHLSG
KHGDCVLKWE NRLSIAVETA LGLEYLHSGC KPLMVHRDVK SMNILLDEHF QAKLADFGLS
RSFSVGEESH VSTGVVGTPG YLDPEYYRTY RLTEKSDVYS FGIVLLEIIT NQPVLEQANE
NRHIAERVRT MLTRSDISTI VDPNLIGEYD SGSVRKALKL AMSCVDPSPV ARPDMSHVVQ
ELKQCIKSEN LRLRTGLNQV IDSKSS
//
