LRK16_ARATH
ID LRK16_ARATH Reviewed; 669 AA.
AC Q9M1G3; A0A1I9LTM5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable L-type lectin-domain containing receptor kinase I.6;
DE Short=LecRK-I.6;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LECRK16; OrderedLocusNames=At3g45440; ORFNames=F9K21.20;
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=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}.
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DR EMBL; AL138657; CAB75473.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78030.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65933.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65935.1; -; Genomic_DNA.
DR PIR; T47484; T47484.
DR RefSeq; NP_001327866.1; NM_001339208.1.
DR RefSeq; NP_001327868.1; NM_001339209.1.
DR RefSeq; NP_190130.1; NM_114413.2.
DR AlphaFoldDB; Q9M1G3; -.
DR SMR; Q9M1G3; -.
DR BioGRID; 9002; 5.
DR IntAct; Q9M1G3; 5.
DR STRING; 3702.AT3G45440.1; -.
DR iPTMnet; Q9M1G3; -.
DR PaxDb; Q9M1G3; -.
DR EnsemblPlants; AT3G45440.1; AT3G45440.1; AT3G45440.
DR EnsemblPlants; AT3G45440.3; AT3G45440.3; AT3G45440.
DR EnsemblPlants; AT3G45440.4; AT3G45440.4; AT3G45440.
DR GeneID; 823682; -.
DR Gramene; AT3G45440.1; AT3G45440.1; AT3G45440.
DR Gramene; AT3G45440.3; AT3G45440.3; AT3G45440.
DR Gramene; AT3G45440.4; AT3G45440.4; AT3G45440.
DR KEGG; ath:AT3G45440; -.
DR Araport; AT3G45440; -.
DR TAIR; locus:2085587; AT3G45440.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9M1G3; -.
DR OMA; WEMASLL; -.
DR PhylomeDB; Q9M1G3; -.
DR PRO; PR:Q9M1G3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1G3; baseline and differential.
DR Genevisible; Q9M1G3; AT.
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; 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 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..669
FT /note="Probable L-type lectin-domain containing receptor
FT kinase I.6"
FT /id="PRO_0000403075"
FT TOPO_DOM 23..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 342..614
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..257
FT /note="Legume-lectin like"
FT ACT_SITE 466
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 348..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 669 AA; 73499 MW; 69F1A70C5EAA1433 CRC64;
MAQGLHLIWV IFCLHLICIS SQQETEFIFN GFGQADLYTD GVAKILPNGL LQLTDGSGQK
MGHAFFKKPF EFKSPRSFSF STHFVCALVP KPGFIGGHGI AFVLSASMDL TQADATQFLG
LFNISTQGSP SSHLVAVELD TALSAEFDDI DANHVGIDVN SLMSIASTPA AYFSEIDGEN
KSIKLLSGDP IQVWVDYGGN VLNVTLAPLK IQKPSRPLLS RSINLSETFP DRKFFLGFSG
ATGTLISYQY ILGWSLSRNK VSLQTLDVTK LPRVPRHRAK NKGPSVVLIV LLILLAIIVF
LALGAAYVYR RRKYAEIREE WEKEYGPHRF SYKDLYIATN GFNKDGLLGK GGFGKVYKGT
LPSKGQIAVK RVSHDAEEGM KQFVAEIVSM GNLKHKNMVP LLGYCRRKGE LLLVSEYMPN
GSLDQYLFND EKPPFSWRRR LLIIKDIATA LNYMHTGAPQ VVLHRDIKAS NVMLDTEFNG
RLGDFGMARF HDHGKDPATT AAVGTIGYMA PELATVGACT ATDVYGFGAF LLEVTCGRRP
VEPGLSAERW YIVKWVCECW KMASLLGARD PRMRGEISAE EVEMVLKLGL LCTNGVPDLR
PSMEDIVQYL NGSLELPDIS PNSPGIGSFT PLIIGSNPPV SPSTKTFYTS SSANDSTFVT
HSIIHGDGR
