LRK64_ARATH
ID LRK64_ARATH Reviewed; 691 AA.
AC Q66GN2; Q9M019;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Lectin-domain containing receptor kinase VI.4;
DE Short=LecRK-VI.4;
DE EC=2.7.11.1;
DE AltName: Full=Lectin receptor kinase A4.3;
DE Flags: Precursor;
GN Name=LECRK64; Synonyms=LECRKA4.3; OrderedLocusNames=At5g01560;
GN ORFNames=F7A7.80;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18987212; DOI=10.1104/pp.108.130583;
RA Xin Z., Wang A., Yang G., Gao P., Zheng Z.-L.;
RT "The Arabidopsis a4 subfamily of lectin receptor kinases negatively
RT regulates abscisic acid response in seed germination.";
RL Plant Physiol. 149:434-444(2009).
CC -!- FUNCTION: Involved in negative regulation of abscisic acid response in
CC seed germination. {ECO:0000269|PubMed:18987212}.
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:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Slight enhancement in abscisic acid-inhibited
CC germination. Redundant with LECRKA4.1 and LECRKA4.2.
CC {ECO:0000269|PubMed:18987212}.
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=CAB82272.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL161946; CAB82272.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED90360.1; -; Genomic_DNA.
DR EMBL; BT015370; AAU05493.1; -; mRNA.
DR PIR; T48177; T48177.
DR RefSeq; NP_195776.2; NM_120234.4.
DR AlphaFoldDB; Q66GN2; -.
DR SMR; Q66GN2; -.
DR STRING; 3702.AT5G01560.1; -.
DR iPTMnet; Q66GN2; -.
DR PaxDb; Q66GN2; -.
DR PRIDE; Q66GN2; -.
DR ProteomicsDB; 238723; -.
DR EnsemblPlants; AT5G01560.1; AT5G01560.1; AT5G01560.
DR GeneID; 830345; -.
DR Gramene; AT5G01560.1; AT5G01560.1; AT5G01560.
DR KEGG; ath:AT5G01560; -.
DR Araport; AT5G01560; -.
DR TAIR; locus:2149810; AT5G01560.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q66GN2; -.
DR OMA; RTPMISQ; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q66GN2; -.
DR PRO; PR:Q66GN2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q66GN2; baseline and differential.
DR Genevisible; Q66GN2; AT.
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:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
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:0009845; P:seed germination; IMP: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; Cell membrane; Kinase; Lectin; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..691
FT /note="Lectin-domain containing receptor kinase VI.4"
FT /id="PRO_0000364131"
FT TOPO_DOM 20..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 363..641
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 26..273
FT /note="Legume-lectin like"
FT ACT_SITE 491
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 369..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 691 AA; 76735 MW; B5CBCEDC8ACEE226 CRC64;
MGRAKSMVSL LLVLFLVRAH VATTETTTEF IFHGFKGNQS EIHMQGDSTI TSNGLLRLTD
RNSDVVGTAF YHKPVRLLDS NSTNTTVRSF STSFIFIIPS SSTSNGGFGF TFTLSPTPNR
TDADPEQYMG LLNERNDGNS SNHVFAVEFD TVQGFKDGTN RIGNHIGLNF NSLSSDVQEP
VAYFNNNDSQ KEEFQLVSGE PIQVFLDYHG PTKTLNLTVY PTRLGYKPRI PLISREVPKL
SDIVVDEMFV GFTAATGRHG QSSAHYVMGW SFASGGEHPL AAMLDISQLP PPPPNKAKKR
GYNGKVIALI VALSTVISIM LVLLFLFMMY KKRMQQEEIL EDWEIDHPHR FRYRDLYKAT
EGFKENRVVG TGGFGIVYRG NIRSSSDQIA VKKITPNSMQ GVREFVAEIE SLGRLRHKNL
VNLQGWCKHR NDLLLIYDYI PNGSLDSLLY SKPRRSGAVL SWNARFQIAK GIASGLLYLH
EEWEQIVIHR DVKPSNVLID SDMNPRLGDF GLARLYERGS QSCTTVVVGT IGYMAPELAR
NGNSSSASDV FAFGVLLLEI VSGRKPTDSG TFFIADWVME LQASGEILSA IDPRLGSGYD
EGEARLALAV GLLCCHHKPE SRPLMRMVLR YLNRDEDVPE IHDNWGYSDS SRTDLGSKLV
GYISSDRASS SHSHTSSSLT RISSTSLISG R
