LRK22_ARATH
ID LRK22_ARATH Reviewed; 694 AA.
AC Q9FIF0; F4KHU6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative L-type lectin-domain containing receptor kinase II.2;
DE Short=LecRK-II.2;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LECRK22; OrderedLocusNames=At5g59270; ORFNames=MNC17.20;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 GENE FAMILY.
RX DOI=10.1080/0735-260291044287;
RA Barre A., Herve C., Lescure B., Rouge P.;
RT "Lectin receptor kinases in plants.";
RL Crit. Rev. Plant Sci. 21:379-399(2002).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19773388; DOI=10.1093/jxb/erp277;
RA Bouwmeester K., Govers F.;
RT "Arabidopsis L-type lectin receptor kinases: phylogeny, classification, and
RT expression profiles.";
RL J. Exp. Bot. 60:4383-4396(2009).
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: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the leguminous lectin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED97164.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB09772.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB09772.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB016890; BAB09772.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97164.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_200735.1; NM_125317.2.
DR AlphaFoldDB; Q9FIF0; -.
DR SMR; Q9FIF0; -.
DR PaxDb; Q9FIF0; -.
DR PeptideAtlas; Q9FIF0; -.
DR PRIDE; Q9FIF0; -.
DR ProteomicsDB; 238394; -.
DR GeneID; 836045; -.
DR KEGG; ath:AT5G59270; -.
DR Araport; AT5G59270; -.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR InParanoid; Q9FIF0; -.
DR PRO; PR:Q9FIF0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIF0; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0002229; P:defense response to oomycetes; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Lectin; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..694
FT /note="Putative L-type lectin-domain containing receptor
FT kinase II.2"
FT /id="PRO_0000403082"
FT TOPO_DOM 25..318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..694
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 375..650
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 27..272
FT /note="Legume-lectin like"
FT REGION 283..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..311
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 500
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 381..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 694 AA; 77085 MW; 0275283338F0D65E CRC64;
MAGVLRSLRF WMIICVQVLS LVLAQDRDEF VYHDFSQADL HLDGMASIDD GRLHLTNNTT
KSTGHAFWKI PMNFTTSPSS SLSFSTEFVF AIFPLLGDGQ GMAFVVAPFM DIRYSGDAAS
YLGLFNRKND NKTENHILAV ELDTNSSPEA IEDSDNHVGI DINSIISEDS ANASYFSGTE
GKNISFRLAS EKSILVWIDY NGTEKLLNVT VAPVPTPKPA LPYLSSSIKP RKPLLSRFIN
ISEIFNGTMF VGFSGSTGTV KSDQYILGWS FKKGGQAESL DLSKILDPPN RPPPPSSPPP
PPPPPPTPPT SRSKDSKNII IICVTVTSIA FLLMLGGFLY LYKKKKYAEV LEHWENEYSP
QRYSFRNLYK AIRGFRENRL LGAGGFGKVY KGELPSGTQI AVKRVYHNAE QGMKQYAAEI
ASMGRLRHKN LVQLLGYCRR KGELLLVYDY MPNGSLDDYL FNKNKLKDLT WSQRVNIIKG
VASALLYLHE EWEQVVLHRD IKASNILLDA DLNGRLGDFG LARFHDRGEN LQATRVVGTI
GYMAPELTAM GVATTKTDIY AFGSFILEVV CGRRPVEPDR PPEQMHLLKW VATCGKRDTL
MDVVDSKLGD FKAKEAKLLL KLGMLCSQSN PESRPSMRHI IQYLEGNATI PSISFDTAGF
GIPNISNETI TQMTATSSSA NFSFEDVTIL FGGR
