LRK63_ARATH
ID LRK63_ARATH Reviewed; 688 AA.
AC Q9M020;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Lectin-domain containing receptor kinase VI.3;
DE Short=LecRK-VI.3;
DE EC=2.7.11.1;
DE AltName: Full=Lectin receptor kinase A4.2;
DE Flags: Precursor;
GN Name=LECRK63; Synonyms=LECRKA4.2; OrderedLocusNames=At5g01550;
GN ORFNames=F7A7.70;
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 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 [4]
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 [5]
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 LECRKA4.3.
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}.
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DR EMBL; AL161946; CAB82271.1; -; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T48176; T48176.
DR AlphaFoldDB; Q9M020; -.
DR SMR; Q9M020; -.
DR BioGRID; 16976; 7.
DR IntAct; Q9M020; 7.
DR STRING; 3702.AT5G01550.1; -.
DR iPTMnet; Q9M020; -.
DR PaxDb; Q9M020; -.
DR PRIDE; Q9M020; -.
DR EnsemblPlants; AT5G01550.1; AT5G01550.1; AT5G01550.
DR Gramene; AT5G01550.1; AT5G01550.1; AT5G01550.
DR Araport; AT5G01550; -.
DR TAIR; locus:2149795; AT5G01550.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR HOGENOM; CLU_000288_62_3_1; -.
DR InParanoid; Q9M020; -.
DR PhylomeDB; Q9M020; -.
DR PRO; PR:Q9M020; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M020; baseline and differential.
DR Genevisible; Q9M020; 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..14
FT /evidence="ECO:0000255"
FT CHAIN 15..688
FT /note="Lectin-domain containing receptor kinase VI.3"
FT /id="PRO_0000364130"
FT TOPO_DOM 15..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 361..640
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 22..271
FT /note="Legume-lectin like"
FT REGION 662..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 490
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 367..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 688 AA; 75985 MW; DDAFFA86F8947EC3 CRC64;
MLVLFLLLTI PTRAQRTTTE TPKTEFIFRG FSGNQSNIVT TGAATIKLDG LLRLTDRNSN
VTGTSFYHKP VRLLETNTSS TNSTIRSFST SFVFVIIPTS SSNGGFGFTF TLSPTPDRTG
AESAQYLGLL NKANDGNSTN HVFAVEFDTV QGFKDGADRT GNHIGLNFNS LTSDVQEPVV
YYDNEDPNRK EDFPLQSGDP IRAILDYDGP TQTLNLTVYP ANLKSRPVRP LISRPVPKLS
QIVQEEMYVG FTAATGRDQS SAHYVMGWSF SSGGDLLTED TLDLLELPRP PPNTAKKRGY
NSQVLALIVA LSGVTVILLA LLFFFVMYKK RLQQGEVLED WEINHPHRLR YKDLYAATDG
FKENRIVGTG GFGTVFRGNL SSPSSDQIAV KKITPNSMQG VREFIAEIES LGRLRHKNLV
NLQGWCKQKN DLLLIYDYIP NGSLDSLLYS RPRQSGVVLS WNARFKIAKG IASGLLYLHE
EWEKVVIHRD IKPSNVLIED DMNPRLGDFG LARLYERGSQ SNTTVVVGTI GYMAPELARN
GKSSSASDVF AFGVLLLEIV SGRRPTDSGT FFLADWVMEL HARGEILHAV DPRLGFGYDG
VEARLALVVG LLCCHQRPTS RPSMRTVLRY LNGDDDVPEI DNDWGYSDSS RSDLGSNFEG
YVSSDRASSS VPSFSVTRVS SSSVISGR
