(data stored in ACNUC13479 zone)

SWISSPROT: LRK62_ARATH

ID   LRK62_ARATH             Reviewed;         682 AA.
AC   Q9M021;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   30-AUG-2017, entry version 118.
DE   RecName: Full=L-type lectin-domain containing receptor kinase VI.2 {ECO:0000303|PubMed:19773388};
DE            Short=LecRK-VI.2 {ECO:0000303|PubMed:19773388};
DE            EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE   AltName: Full=Lectin receptor kinase A4.1 {ECO:0000303|Ref.4};
DE   Flags: Precursor;
GN   Name=LECRK62 {ECO:0000303|PubMed:19773388};
GN   Synonyms=LECRKA4.1 {ECO:0000303|Ref.4};
GN   OrderedLocusNames=At5g01540 {ECO:0000312|Araport:AT5G01540};
GN   ORFNames=F7A7.60 {ECO:0000312|EMBL:CAB82270.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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,
RT   classification, and expression profiles.";
RL   J. Exp. Bot. 60:4383-4396(2009).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   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).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=25083911; DOI=10.1094/MPMI-06-14-0191-R;
RA   Wang Y., Bouwmeester K., Beseh P., Shan W., Govers F.;
RT   "Phenotypic analyses of Arabidopsis T-DNA insertion lines and
RT   expression profiling reveal that multiple L-type lectin receptor
RT   kinases are involved in plant immunity.";
RL   Mol. Plant Microbe Interact. 27:1390-1402(2014).
CC   -!- FUNCTION: Involved in negative regulation of abscisic acid
CC       response in seed germination. {ECO:0000269|PubMed:18987212}.
CC   -!- FUNCTION: Involved in resistance response to the pathogenic
CC       bacteria Pseudomonas syringae. {ECO:0000269|PubMed:25083911}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18987212};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in the vascular system and
CC       trichomes of the leaves. Also expressed in guard cells, anthers,
CC       stigmas and germinating seeds, but not found in petals or roots.
CC       Increased susceptibility to the bacteria Pseudomonas syringae,
CC       characterized by stronger necrotic symptoms and higher bacterial
CC       proliferation (PubMed:25083911). {ECO:0000269|PubMed:18987212,
CC       ECO:0000269|PubMed:25083911}.
CC   -!- DISRUPTION PHENOTYPE: Slight enhancement in abscisic acid-
CC       inhibited germination. Redundant with LECRKA4.2 and LECRKA4.3.
CC       {ECO:0000269|PubMed:18987212}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the protein
CC       kinase superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the leguminous
CC       lectin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
DR   EMBL; AL161946; CAB82270.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90358.1; -; Genomic_DNA.
DR   EMBL; AF361597; AAK32765.1; -; mRNA.
DR   EMBL; BT000489; AAN18058.1; -; mRNA.
DR   PIR; T48175; T48175.
DR   RefSeq; NP_195774.1; NM_120232.2.
DR   UniGene; At.28701; -.
DR   ProteinModelPortal; Q9M021; -.
DR   SMR; Q9M021; -.
DR   BioGrid; 16998; 25.
DR   STRING; 3702.AT5G01540.1; -.
DR   PaxDb; Q9M021; -.
DR   PRIDE; Q9M021; -.
DR   EnsemblPlants; AT5G01540.1; AT5G01540.1; AT5G01540.
DR   GeneID; 831722; -.
DR   Gramene; AT5G01540.1; AT5G01540.1; AT5G01540.
DR   KEGG; ath:AT5G01540; -.
DR   Araport; AT5G01540; -.
DR   TAIR; locus:2149780; AT5G01540.
DR   eggNOG; ENOG410IKU3; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116555; -.
DR   InParanoid; Q9M021; -.
DR   OMA; NTDRIGN; -.
DR   OrthoDB; EOG093605JV; -.
DR   PhylomeDB; Q9M021; -.
DR   PRO; PR:Q9M021; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q9M021; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR   GO; GO:0052033; P:pathogen-associated molecular pattern dependent induction by symbiont of host innate immune response; IMP:TAIR.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR   GO; GO:0009845; P:seed germination; IMP:TAIR.
DR   CDD; cd06899; lectin_legume_LecRK_Arcelin_Co; 1.
DR   InterPro; IPR013320; ConA-like_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
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;
DR   PRODOM; Q9M021.
DR   SWISS-2DPAGE; Q9M021.
KW   ATP-binding; Cell membrane; Complete proteome; Kinase; Lectin;
KW   Membrane; Nucleotide-binding; Plant defense; Receptor;
KW   Reference proteome; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    682       L-type lectin-domain containing receptor
FT                                kinase VI.2.
FT                                /FTId=PRO_0000364129.
FT   TOPO_DOM     27    310       Extracellular. {ECO:0000255}.
FT   TRANSMEM    311    331       Helical. {ECO:0000255}.
FT   TOPO_DOM    332    682       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      367    641       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     373    381       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION       29    277       Legume-lectin like. {ECO:0000255}.
FT   COMPBIAS    104    107       Poly-Ser. {ECO:0000255}.
FT   COMPBIAS    294    298       Poly-Pro. {ECO:0000255}.
FT   ACT_SITE    494    494       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   BINDING     395    395       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
SQ   SEQUENCE   682 AA;  75868 MW;  C19750EC2E8E470F CRC64;
     MGTQRSMFIV SFLFKLFLFL SVHVRAQRTT TNFAFRGFNG NQSKIRIEGA AMIKPDGLLR
     LTDRKSNVTG TAFYHKPVRL LNRNSTNVTI RSFSTSFVFV IIPSSSSNKG FGFTFTLSPT
     PYRLNAGSAQ YLGVFNKENN GDPRNHVFAV EFDTVQGSRD DNTDRIGNDI GLNYNSRTSD
     LQEPVVYYNN DDHNKKEDFQ LESGNPIQAL LEYDGATQML NVTVYPARLG FKPTKPLISQ
     HVPKLLEIVQ EEMYVGFTAS TGKGQSSAHY VMGWSFSSGG ERPIADVLIL SELPPPPPNK
     AKKEGLNSQV IVMIVALSAV MLVMLVLLFF FVMYKKRLGQ EETLEDWEID HPRRLRYRDL
     YVATDGFKKT GIIGTGGFGT VFKGKLPNSD PIAVKKIIPS SRQGVREFVA EIESLGKLRH
     KNLVNLQGWC KHKNDLLLIY DYIPNGSLDS LLYTVPRRSG AVLSWNARFQ IAKGIASGLL
     YLHEEWEKIV IHRDVKPSNV LIDSKMNPRL GDFGLARLYE RGTLSETTAL VGTIGYMAPE
     LSRNGNPSSA SDVFAFGVLL LEIVCGRKPT DSGTFFLVDW VMELHANGEI LSAIDPRLGS
     GYDGGEARLA LAVGLLCCHQ KPASRPSMRI VLRYLNGEEN VPEIDDEWGY SKSSRSEFGS
     KLVGYVSSTS ITRVSSTSRI SQ
//

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