ID   LRK52_ARATH             Reviewed;         656 AA.
AC   O04533;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Putative L-type lectin-domain containing receptor kinase V.2;
DE            Short=Arabidopsis thaliana lectin-receptor kinase b1;
DE            Short=AthlecRK-b1;
DE            Short=LecRK-V.2;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   Name=LECRK52; Synonyms=LECRKB1; OrderedLocusNames=At1g70130;
GN   ORFNames=F20P5.15;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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   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   [4]
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   [5]
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; AC002062; AAB61102.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35023.1; -; Genomic_DNA.
DR   PIR; A96724; A96724.
DR   RefSeq; NP_177170.1; NM_105681.2.
DR   AlphaFoldDB; O04533; -.
DR   SMR; O04533; -.
DR   STRING; 3702.O04533; -.
DR   GlyCosmos; O04533; 5 sites, No reported glycans.
DR   iPTMnet; O04533; -.
DR   PaxDb; 3702-AT1G70130-1; -.
DR   ProteomicsDB; 238721; -.
DR   EnsemblPlants; AT1G70130.1; AT1G70130.1; AT1G70130.
DR   GeneID; 843349; -.
DR   Gramene; AT1G70130.1; AT1G70130.1; AT1G70130.
DR   KEGG; ath:AT1G70130; -.
DR   Araport; AT1G70130; -.
DR   TAIR; AT1G70130; LECRK-V.2.
DR   eggNOG; ENOG502QTAM; Eukaryota.
DR   HOGENOM; CLU_000288_62_3_1; -.
DR   InParanoid; O04533; -.
DR   OMA; ITSKTQG; -.
DR   OrthoDB; 22648at2759; -.
DR   PhylomeDB; O04533; -.
DR   PRO; PR:O04533; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O04533; baseline and differential.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0098542; P:defense response to other organism; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27007; -; 1.
DR   PANTHER; PTHR27007:SF241; L-TYPE LECTIN-DOMAIN CONTAINING RECEPTOR KINASE V.2-RELATED; 1.
DR   Pfam; PF00139; Lectin_legB; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 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; O04533; AT.
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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..656
FT                   /note="Putative L-type lectin-domain containing receptor
FT                   kinase V.2"
FT                   /id="PRO_0000403090"
FT   TOPO_DOM        24..276
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..656
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          334..615
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          29..248
FT                   /note="Legume-lectin like"
FT   ACT_SITE        459
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         340..348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   656 AA;  72455 MW;  F438795FA65C9A12 CRC64;
     MSLLLKMLLF SLFFFYMASI SQCSDPTGGQ FSFNGYLYTD GVADLNPDGL FKLITSKTQG
     GAGQVLYQFP LQFKNSPNGT VSSFSTTFVF AIVAVRKTIA GCGLSFNISP TKGLNSVPNI
     DHSNHSVSVG FHTAKSDKPD GEDVNLVGIN IDSSKMDRNC SAGYYKDDGR LVNLDIASGK
     PIQVWIEYNN STKQLDVTMH SIKISKPKIP LLSMRKDLSP YLHEYMYIGF TSVGSPTSSH
     YILGWSFNNK GAVSDINLSR LPKVPDEDQE RSLSSKILAI SLSISGVTLV IVLILGVMLF
     LKRKKFLEVI EDWEVQFGPH KFTYKDLFIA TKGFKNSEVL GKGGFGKVFK GILPLSSIPI
     AVKKISHDSR QGMREFLAEI ATIGRLRHPD LVRLLGYCRR KGELYLVYDF MPKGSLDKFL
     YNQPNQILDW SQRFNIIKDV ASGLCYLHQQ WVQVIIHRDI KPANILLDEN MNAKLGDFGL
     AKLCDHGIDS QTSNVAGTFG YISPELSRTG KSSTSSDVFA FGVFMLEITC GRRPIGPRGS
     PSEMVLTDWV LDCWDSGDIL QVVDEKLGHR YLAEQVTLVL KLGLLCSHPV AATRPSMSSV
     IQFLDGVATL PHNLLDLVNS RIINEGFDTL GVTTESMEAS SNVSLVMTES FLSSGR
//