(data stored in ACNUC13479 zone)

SWISSPROT: 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   30-AUG-2017, entry version 116.
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; 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   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,
RT   classification, and 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
CC       response in seed germination. {ECO:0000269|PubMed:18987212}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type I membrane protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Slight enhancement in abscisic acid-
CC       inhibited germination. Redundant with LECRKA4.1 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; CAB82271.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90359.1; -; Genomic_DNA.
DR   PIR; T48176; T48176.
DR   RefSeq; NP_195775.2; NM_120233.2.
DR   UniGene; At.49414; -.
DR   ProteinModelPortal; Q9M020; -.
DR   SMR; Q9M020; -.
DR   BioGrid; 16976; 7.
DR   STRING; 3702.AT5G01550.1; -.
DR   iPTMnet; Q9M020; -.
DR   PaxDb; Q9M020; -.
DR   GeneID; 831700; -.
DR   KEGG; ath:AT5G01550; -.
DR   Araport; AT5G01550; -.
DR   TAIR; locus:2149795; AT5G01550.
DR   eggNOG; ENOG410IKU3; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116555; -.
DR   InParanoid; Q9M020; -.
DR   OMA; KQEMYVG; -.
DR   OrthoDB; EOG093605O2; -.
DR   PhylomeDB; Q9M020; -.
DR   PRO; PR:Q9M020; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q9M020; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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; Q9M020.
DR   SWISS-2DPAGE; Q9M020.
KW   ATP-binding; Cell membrane; Complete proteome; Kinase; Lectin;
KW   Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     14       {ECO:0000255}.
FT   CHAIN        15    688       Lectin-domain containing receptor kinase
FT                                VI.3.
FT                                /FTId=PRO_0000364130.
FT   TOPO_DOM     15    306       Extracellular. {ECO:0000255}.
FT   TRANSMEM    307    327       Helical. {ECO:0000255}.
FT   TOPO_DOM    328    688       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      361    640       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     367    375       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION       22    271       Legume-lectin like.
FT   COMPBIAS    647    686       Ser-rich.
FT   ACT_SITE    490    490       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     391    391       ATP. {ECO:0000255|PROSITE-
FT                                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
//

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