LRK41_ARATH
ID LRK41_ARATH Reviewed; 675 AA.
AC O80939; Q39139;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=L-type lectin-domain containing receptor kinase IV.1;
DE Short=Arabidopsis thaliana lectin-receptor kinase e;
DE Short=AthlecRK-e;
DE Short=LecRK-IV.1;
DE EC=2.7.11.1;
DE AltName: Full=Lectin Receptor Kinase 1;
DE Flags: Precursor;
GN Name=LECRK41; Synonyms=LECRKE, LRK1; OrderedLocusNames=At2g37710;
GN ORFNames=F13M22.21;
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 [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RA Swarup R., Dumas C., Cock J.M.;
RT "A new class of receptor-like protein kinase gene from Arabidopsis thaliana
RT possessing a domain with similarity to plant lectin genes.";
RL (er) Plant Gene Register PGR96-022(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY.
RX PubMed=10350082; DOI=10.1023/a:1006136701595;
RA Herve C., Serres J., Dabos P., Canut H., Barre A., Rouge P., Lescure B.;
RT "Characterization of the Arabidopsis lecRK-a genes: members of a
RT superfamily encoding putative receptors with an extracellular domain
RT homologous to legume lectins.";
RL Plant Mol. Biol. 39:671-682(1999).
RN [6]
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 [7]
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: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
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=CAA65153.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X95909; CAA65153.1; ALT_FRAME; mRNA.
DR EMBL; AC004684; AAC23641.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09438.1; -; Genomic_DNA.
DR EMBL; AY091070; AAM13890.1; -; mRNA.
DR PIR; T02537; T02537.
DR PIR; T50661; T50661.
DR RefSeq; NP_181307.1; NM_129327.4.
DR AlphaFoldDB; O80939; -.
DR SMR; O80939; -.
DR BioGRID; 3692; 5.
DR STRING; 3702.AT2G37710.1; -.
DR iPTMnet; O80939; -.
DR PaxDb; O80939; -.
DR PRIDE; O80939; -.
DR ProteomicsDB; 238499; -.
DR EnsemblPlants; AT2G37710.1; AT2G37710.1; AT2G37710.
DR GeneID; 818348; -.
DR Gramene; AT2G37710.1; AT2G37710.1; AT2G37710.
DR KEGG; ath:AT2G37710; -.
DR Araport; AT2G37710; -.
DR TAIR; locus:2040681; AT2G37710.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; O80939; -.
DR OMA; RDKWRGE; -.
DR OrthoDB; 418528at2759; -.
DR PhylomeDB; O80939; -.
DR PRO; PR:O80939; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80939; baseline and differential.
DR Genevisible; O80939; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 GO; GO:0009751; P:response to salicylic acid; IEP: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; Glycoprotein; Kinase; Lectin; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..675
FT /note="L-type lectin-domain containing receptor kinase
FT IV.1"
FT /id="PRO_0000403085"
FT TOPO_DOM 23..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 347..624
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 25..261
FT /note="Legume-lectin like"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 353..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 376
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 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 12
FT /note="Missing (in Ref. 1; CAA65153)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="I -> S (in Ref. 1; CAA65153)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..130
FT /note="LA -> IT (in Ref. 1; CAA65153)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..302
FT /note="LFLI -> QFFF (in Ref. 1; CAA65153)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="G -> R (in Ref. 1; CAA65153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 75541 MW; C3F2437E6ABA9967 CRC64;
MFLKLLTIFF FFFFNLIFQS SSQSLNFAYN NGFNPPTDLS IQGITTVTPN GLLKLTNTTV
QKTGHAFYTK PIRFKDSPNG TVSSFSTSFV FAIHSQIAIL SGHGIAFVVA PNASLPYGNP
SQYIGLFNLA NNGNETNHVF AVELDTILST EFNDTNDNHV GIDINSLKSV QSSPAGYWDE
KGQFKNLTLI SRKPMQVWVD YDGRTNKIDV TMAPFNEDKP TRPLVTAVRD LSSVLLQDMY
VGFSSATGSV LSEHYILGWS FGLNEKAPPL ALSRLPKLPR FEPKRISEFY KIGMPLISLF
LIFSFIFLVC YIVRRRRKFA EELEEWEKEF GKNRFRFKDL YYATKGFKEK GLLGTGGFGS
VYKGVMPGTK LEIAVKRVSH ESRQGMKEFV AEIVSIGRMS HRNLVPLLGY CRRRGELLLV
YDYMPNGSLD KYLYNTPEVT LNWKQRIKVI LGVASGLFYL HEEWEQVVIH RDVKASNVLL
DGELNGRLGD FGLARLYDHG SDPQTTHVVG TLGYLAPEHT RTGRATMATD VFAFGAFLLE
VACGRRPIEF QQETDETFLL VDWVFGLWNK GDILAAKDPN MGSECDEKEV EMVLKLGLLC
SHSDPRARPS MRQVLHYLRG DAKLPELSPL DLSGSGMMFG VHDGFSELGM SYSSSVFKGF
TGGSSIADSQ LSGGR
