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   27-MAR-2024, entry version 157.
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.O80939; -.
DR   GlyCosmos; O80939; 6 sites, No reported glycans.
DR   iPTMnet; O80939; -.
DR   PaxDb; 3702-AT2G37710-1; -.
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; AT2G37710; LECRK-IV.1.
DR   eggNOG; ENOG502QSJ4; Eukaryota.
DR   HOGENOM; CLU_000288_62_3_1; -.
DR   InParanoid; O80939; -.
DR   OMA; HGNYNID; -.
DR   OrthoDB; 22648at2759; -.
DR   PhylomeDB; O80939; -.
DR   PRO; PR:O80939; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80939; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR   CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR27007; -; 1.
DR   PANTHER; PTHR27007:SF325; L-TYPE LECTIN-DOMAIN CONTAINING RECEPTOR KINASE IV.1; 1.
DR   Pfam; PF00139; Lectin_legB; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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.
DR   Genevisible; O80939; AT.
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
//