LRK15_ARATH
ID LRK15_ARATH Reviewed; 674 AA.
AC Q9M1G4; A0A1I9LPQ8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable L-type lectin-domain containing receptor kinase I.5;
DE Short=LecRK-I.5;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LECRK15; OrderedLocusNames=At3g45430; ORFNames=F9K21.10;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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=CAB75472.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL138657; CAB75472.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE78029.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64566.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64567.1; -; Genomic_DNA.
DR PIR; T47483; T47483.
DR RefSeq; NP_001326585.1; NM_001339206.1.
DR RefSeq; NP_001326586.1; NM_001339205.1.
DR RefSeq; NP_190129.2; NM_114412.3.
DR AlphaFoldDB; Q9M1G4; -.
DR SMR; Q9M1G4; -.
DR BioGRID; 9001; 2.
DR IntAct; Q9M1G4; 2.
DR PaxDb; Q9M1G4; -.
DR PRIDE; Q9M1G4; -.
DR ProteomicsDB; 238427; -.
DR EnsemblPlants; AT3G45430.1; AT3G45430.1; AT3G45430.
DR EnsemblPlants; AT3G45430.2; AT3G45430.2; AT3G45430.
DR EnsemblPlants; AT3G45430.3; AT3G45430.3; AT3G45430.
DR GeneID; 823681; -.
DR Gramene; AT3G45430.1; AT3G45430.1; AT3G45430.
DR Gramene; AT3G45430.2; AT3G45430.2; AT3G45430.
DR Gramene; AT3G45430.3; AT3G45430.3; AT3G45430.
DR KEGG; ath:AT3G45430; -.
DR Araport; AT3G45430; -.
DR TAIR; locus:2085577; AT3G45430.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9M1G4; -.
DR OMA; GVYYHRK; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9M1G4; -.
DR PRO; PR:Q9M1G4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1G4; baseline and differential.
DR Genevisible; Q9M1G4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IPI:TAIR.
DR GO; GO:0005524; F:ATP binding; IDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IGI:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
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:0140426; P:PAMP-triggered immunity signalling pathway; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
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; 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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..674
FT /note="Probable L-type lectin-domain containing receptor
FT kinase I.5"
FT /id="PRO_0000403074"
FT TOPO_DOM 23..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 344..625
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 25..258
FT /note="Legume-lectin like"
FT REGION 649..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 468
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 350..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 674 AA; 74378 MW; B8C2AF465161BF59 CRC64;
MSKGLFLIWL ISSFHLISFS TSSKDTSFVF NGFGQSNLAL DGSATLLPNG LLQLAKDSQH
QMGHAFIKKP IDFSSSKPLS FSTHFVCALV PKPGFEGGHG ITFVISPTVD FTRAQPTRYM
GIFNASTNGS PSSHLFAVEL DTVRNPDFRE TNNNHIGIDV NNPISVESAP ASYFSKTAQK
NVSINLSSGK PIQVWVDYHG NVLNVSVAPL EAEKPSLPLL SRSMNLSEIF SRRRLFVGFA
AATGTSISYH YLLGWSFSTN RELSQLLDFS KLPQVPRPRA EHKKVQFALI IALPVILAIV
VMAVLAGVYY HRKKKYAEVS EPWEKKYGTH RFSYKSLYIA TKGFHKDRFL GRGGFGEVYR
GDLPLNKTVA VKRVSHDGEQ GMKQFVAEVV SMKSLKHRNL VPLLGYCRRK GELLLVSEYM
PNGSLDQHLF DDQSPVLSWS QRFVILKGIA SALFYLHTEA EQVVLHRDIK ASNVMLDAEL
NGRLGDFGMA RFHDHGGNAA TTAAVGTVGY MAPELITMGA STITDVYAFG VFLLEVACGR
KPVEFGVQVE KRFLIKWVCE CWKKDSLLDA KDPRLGEEFV PEEVELVMKL GLLCTNIVPE
SRPAMGQVVL YLSGNLPLPD FSPYTLGIGS FTPVVVDAAS LTVSFTSRNW SAPSASSSSA
NNSKDHEQPL EFKS
