LRK52_ARATH
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 03-AUG-2022, entry version 155.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 iPTMnet; O04533; -.
DR PaxDb; O04533; -.
DR PRIDE; O04533; -.
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; locus:2020593; AT1G70130.
DR eggNOG; ENOG502QTAM; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; O04533; -.
DR OMA; ITSKTQG; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O04533; -.
DR PRO; PR:O04533; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04533; baseline and differential.
DR Genevisible; O04533; 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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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
