ID LRK51_ARATH Reviewed; 666 AA.
AC O04534;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 164.
DE RecName: Full=Putative L-type lectin-domain containing receptor kinase V.1;
DE Short=Arabidopsis thaliana lectin-receptor kinase b2;
DE Short=AthlecRK-b2;
DE Short=LecRK-V.1;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LECRK51; Synonyms=LECRKB2; OrderedLocusNames=At1g70110;
GN ORFNames=F20P5.16;
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; AAB61103.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35021.1; -; Genomic_DNA.
DR PIR; H96723; H96723.
DR RefSeq; NP_177168.1; NM_105679.2.
DR AlphaFoldDB; O04534; -.
DR SMR; O04534; -.
DR STRING; 3702.O04534; -.
DR GlyCosmos; O04534; 6 sites, No reported glycans.
DR PaxDb; 3702-AT1G70110-1; -.
DR EnsemblPlants; AT1G70110.1; AT1G70110.1; AT1G70110.
DR GeneID; 843347; -.
DR Gramene; AT1G70110.1; AT1G70110.1; AT1G70110.
DR KEGG; ath:AT1G70110; -.
DR Araport; AT1G70110; -.
DR TAIR; AT1G70110; LECRK-V.1.
DR eggNOG; ENOG502QTAM; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; O04534; -.
DR OMA; WIEYESK; -.
DR OrthoDB; 22648at2759; -.
DR PhylomeDB; O04534; -.
DR PRO; PR:O04534; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04534; baseline and differential.
DR Genevisible; O04534; AT.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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:SF275; L-TYPE LECTIN-DOMAIN CONTAINING RECEPTOR KINASE V.1-RELATED; 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; 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 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..666
FT /note="Putative L-type lectin-domain containing receptor
FT kinase V.1"
FT /id="PRO_0000403089"
FT TOPO_DOM 19..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 344..625
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 27..257
FT /note="Legume-lectin like"
FT ACT_SITE 469
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 350..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 666 AA; 74578 MW; 7C5F79D4D1B2A233 CRC64;
MVLLLFLVLF FVPESVVCQR PNPNGVEFNT SGNMYTSGSA YINNNGLIRL TNSTPQTTGQ
VFYNDQLRFK NSVNGTVSSF STTFVFSIEF HNGIYGGYGI AFVICPTRDL SPTFPTTYLG
LFNRSNMGDP KNHIVAVELD TKVDQQFEDK DANHVGIDIN TLVSDTVALA GYYMDNGTFR
SLLLNSGQPM QIWIEYDSKQ KQINVTLHPL YVPKPKIPLL SLEKDLSPYL LELMYVGFTS
TTGDLTASHY ILGWTFKMNG TTPDIDPSRL PKIPRYNQPW IQSPNGILTI SLTVSGVIIL
IILSLSLWLF LKRKKLLEVL EDWEVQFGPH RFAFKDLHIA TKGFKDTEVL GKGGFGKVYK
GTLPVSNVEI AVKMVSHDSR QGMREFIAEI ATIGRLRHPN LVRLQGYCRH KGELYLVYDC
MAKGSLDKFL YHQQTGNLDW SQRFKIIKDV ASGLYYLHQQ WVQVIIHRDI KPANILLDAN
MNAKLGDFGL AKLCDHGTDP QTSHVAGTLG YISPELSRTG KASTRSDVFA FGIVMLEIAC
GRKPILPRAS QREMVLTDWV LECWENEDIM QVLDHKIGQE YVEEQAALVL KLGLFCSHPV
AAIRPNMSSV IQLLDSVAQL PHNLLDIVQT REVHRGTEIS GEAADSPESC SIAPLTFTES
FVSHGR
//
