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RecName: Full=L-type lectin-domain containing receptor kinase VII.1; Short=LecRK-VII.1; Flags: Precursor

UniProtKB/Swiss-Prot: Q9S9U1.1

Identical Proteins FASTA Graphics 

LOCUS       LRK71_ARATH              686 aa            linear   PLN 27-NOV-2024
DEFINITION  RecName: Full=L-type lectin-domain containing receptor kinase
            VII.1; Short=LecRK-VII.1; Flags: Precursor.
ACCESSION   Q9S9U1
VERSION     Q9S9U1.1
DBSOURCE    UniProtKB: locus LRK71_ARATH, accession Q9S9U1;
            class: standard.
            extra accessions:Q56WH7,Q7Y206
            created: Jan 11, 2011.
            sequence updated: May 1, 2000.
            annotation updated: Nov 27, 2024.
            xrefs: AF162444.1, AAD48977.1, AL161502.2, CAB81038.1, CP002687.1,
            AEE82450.1, BT008663.1, AAP40475.1, AK222063.1, BAD94865.1,
            AK229495.1, BAF01352.1, D85062, NP_567277.1
            xrefs (non-sequence databases): AlphaFoldDB:Q9S9U1, SMR:Q9S9U1,
            STRING:3702.Q9S9U1, GlyCosmos:Q9S9U1, PaxDb:3702-AT4G04960.1,
            ProteomicsDB:238676, EnsemblPlants:AT4G04960.1,
            EnsemblPlants:AT4G04960.1, EnsemblPlants:AT4G04960, GeneID:825837,
            Gramene:AT4G04960.1, KEGG:ath:AT4G04960, Araport:AT4G04960,
            TAIR:AT4G04960, eggNOG:ENOG502QRZ3, HOGENOM:CLU_000288_62_3_1,
            InParanoid:Q9S9U1, OrthoDB:22648at2759, PhylomeDB:Q9S9U1,
            PRO:PR:Q9S9U1, Proteomes:UP000006548, ExpressionAtlas:Q9S9U1,
            GO:0005886, GO:0005524, GO:0030246, GO:0044024, GO:0106310,
            GO:0006468, CDD:cd06899, CDD:cd14066, FunFam:1.10.510.10:FF:000108,
            FunFam:2.60.120.200:FF:000086, FunFam:3.30.200.20:FF:000621,
            Gene3D:2.60.120.200, Gene3D:1.10.510.10, InterPro:IPR013320,
            InterPro:IPR011009, InterPro:IPR050528, InterPro:IPR001220,
            InterPro:IPR000719, InterPro:IPR017441, InterPro:IPR008271,
            PANTHER:PTHR27007, PANTHER:PTHR27007:SF193, Pfam:PF00139,
            Pfam:PF00069, SMART:SM00220, SUPFAM:SSF49899, SUPFAM:SSF56112,
            PROSITE:PS00107, PROSITE:PS50011, PROSITE:PS00108
KEYWORDS    ATP-binding; Cell membrane; Glycoprotein; Kinase; Lectin; Membrane;
            Nucleotide-binding; Receptor; Reference proteome;
            Serine/threonine-protein kinase; Signal; Transferase;
            Transmembrane; Transmembrane helix.
SOURCE      Arabidopsis thaliana (thale cress)
  ORGANISM  Arabidopsis thaliana
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
            Pentapetalae; rosids; malvids; Brassicales; Brassicaceae;
            Camelineae; Arabidopsis.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Mayer,K., Schuller,C., Wambutt,R., Murphy,G., Volckaert,G.,
            Pohl,T., Dusterhoft,A., Stiekema,W., Entian,K.D., Terryn,N.,
            Harris,B., Ansorge,W., Brandt,P., Grivell,L., Rieger,M.,
            Weichselgartner,M., de Simone,V., Obermaier,B., Mache,R.,
            Muller,M., Kreis,M., Delseny,M., Puigdomenech,P., Watson,M.,
            Schmidtheini,T., Reichert,B., Portatelle,D., Perez-Alonso,M.,
            Boutry,M., Bancroft,I., Vos,P., Hoheisel,J., Zimmermann,W.,
            Wedler,H., Ridley,P., Langham,S.A., McCullagh,B., Bilham,L.,
            Robben,J., Van der Schueren,J., Grymonprez,B., Chuang,Y.J.,
            Vandenbussche,F., Braeken,M., Weltjens,I., Voet,M., Bastiaens,I.,
            Aert,R., Defoor,E., Weitzenegger,T., Bothe,G., Ramsperger,U.,
            Hilbert,H., Braun,M., Holzer,E., Brandt,A., Peters,S., van
            Staveren,M., Dirske,W., Mooijman,P., Klein Lankhorst,R., Rose,M.,
            Hauf,J., Kotter,P., Berneiser,S., Hempel,S., Feldpausch,M.,
            Lamberth,S., Van den Daele,H., De Keyser,A., Buysshaert,C.,
            Gielen,J., Villarroel,R., De Clercq,R., Van Montagu,M., Rogers,J.,
            Cronin,A., Quail,M., Bray-Allen,S., Clark,L., Doggett,J., Hall,S.,
            Kay,M., Lennard,N., McLay,K., Mayes,R., Pettett,A.,
            Rajandream,M.A., Lyne,M., Benes,V., Rechmann,S., Borkova,D.,
            Blocker,H., Scharfe,M., Grimm,M., Lohnert,T.H., Dose,S., de
            Haan,M., Maarse,A., Schafer,M., Muller-Auer,S., Gabel,C., Fuchs,M.,
            Fartmann,B., Granderath,K., Dauner,D., Herzl,A., Neumann,S.,
            Argiriou,A., Vitale,D., Liguori,R., Piravandi,E., Massenet,O.,
            Quigley,F., Clabauld,G., Mundlein,A., Felber,R., Schnabl,S.,
            Hiller,R., Schmidt,W., Lecharny,A., Aubourg,S., Chefdor,F.,
            Cooke,R., Berger,C., Montfort,A., Casacuberta,E., Gibbons,T.,
            Weber,N., Vandenbol,M., Bargues,M., Terol,J., Torres,A.,
            Perez-Perez,A., Purnelle,B., Bent,E., Johnson,S., Tacon,D.,
            Jesse,T., Heijnen,L., Schwarz,S., Scholler,P., Heber,S., Francs,P.,
            Bielke,C., Frishman,D., Haase,D., Lemcke,K., Mewes,H.W.,
            Stocker,S., Zaccaria,P., Bevan,M., Wilson,R.K., de la Bastide,M.,
            Habermann,K., Parnell,L., Dedhia,N., Gnoj,L., Schutz,K., Huang,E.,
            Spiegel,L., Sehkon,M., Murray,J., Sheet,P., Cordes,M.,
            Abu-Threideh,J., Stoneking,T., Kalicki,J., Graves,T., Harmon,G.,
            Edwards,J., Latreille,P., Courtney,L., Cloud,J., Abbott,A.,
            Scott,K., Johnson,D., Minx,P., Bentley,D., Fulton,B., Miller,N.,
            Greco,T., Kemp,K., Kramer,J., Fulton,L., Mardis,E., Dante,M.,
            Pepin,K., Hillier,L., Nelson,J., Spieth,J., Ryan,E., Andrews,S.,
            Geisel,C., Layman,D., Du,H., Ali,J., Berghoff,A., Jones,K.,
            Drone,K., Cotton,M., Joshu,C., Antonoiu,B., Zidanic,M., Strong,C.,
            Sun,H., Lamar,B., Yordan,C., Ma,P., Zhong,J., Preston,R., Vil,D.,
            Shekher,M., Matero,A., Shah,R., Swaby,I.K., O'Shaughnessy,A.,
            Rodriguez,M., Hoffmann,J., Till,S., Granat,S., Shohdy,N.,
            Hasegawa,A., Hameed,A., Lodhi,M., Johnson,A., Chen,E., Marra,M.,
            Martienssen,R. and McCombie,W.R.
  TITLE     Sequence and analysis of chromosome 4 of the plant Arabidopsis
            thaliana
  JOURNAL   Nature 402 (6763), 769-777 (1999)
   PUBMED   10617198
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
            STRAIN=cv. Columbia
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Cheng,C.Y., Krishnakumar,V., Chan,A.P., Thibaud-Nissen,F.,
            Schobel,S. and Town,C.D.
  TITLE     Araport11: a complete reannotation of the Arabidopsis thaliana
            reference genome
  JOURNAL   Plant J 89 (4), 789-804 (2017)
   PUBMED   27862469
  REMARK    GENOME REANNOTATION.;
            STRAIN=cv. Columbia
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Yamada,K., Lim,J., Dale,J.M., Chen,H., Shinn,P., Palm,C.J.,
            Southwick,A.M., Wu,H.C., Kim,C., Nguyen,M., Pham,P., Cheuk,R.,
            Karlin-Newmann,G., Liu,S.X., Lam,B., Sakano,H., Wu,T., Yu,G.,
            Miranda,M., Quach,H.L., Tripp,M., Chang,C.H., Lee,J.M., Toriumi,M.,
            Chan,M.M., Tang,C.C., Onodera,C.S., Deng,J.M., Akiyama,K.,
            Ansari,Y., Arakawa,T., Banh,J., Banno,F., Bowser,L., Brooks,S.,
            Carninci,P., Chao,Q., Choy,N., Enju,A., Goldsmith,A.D., Gurjal,M.,
            Hansen,N.F., Hayashizaki,Y., Johnson-Hopson,C., Hsuan,V.W.,
            Iida,K., Karnes,M., Khan,S., Koesema,E., Ishida,J., Jiang,P.X.,
            Jones,T., Kawai,J., Kamiya,A., Meyers,C., Nakajima,M., Narusaka,M.,
            Seki,M., Sakurai,T., Satou,M., Tamse,R., Vaysberg,M.,
            Wallender,E.K., Wong,C., Yamamura,Y., Yuan,S., Shinozaki,K.,
            Davis,R.W., Theologis,A. and Ecker,J.R.
  TITLE     Empirical analysis of transcriptional activity in the Arabidopsis
            genome
  JOURNAL   Science 302 (5646), 842-846 (2003)
   PUBMED   14593172
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=cv. Columbia
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Totoki,Y., Seki,M., Ishida,J., Nakajima,M., Enju,A., Kamiya,A.,
            Narusaka,M., Shin-i,T., Nakagawa,M., Sakamoto,N., Oishi,K.,
            Kohara,Y., Kobayashi,M., Toyoda,A., Sakaki,Y., Sakurai,T., Iida,K.,
            Akiyama,K., Satou,M., Toyoda,T., Konagaya,A., Carninci,P.,
            Kawai,J., Hayashizaki,Y. and Shinozaki,K.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-JUL-2006) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=cv. Columbia
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Barre,A., Herve,C., Lescure,B. and Rouge,P.
  TITLE     Lectin receptor kinases in plants
  JOURNAL   Crit. Rev. Plant Sci. 21, 379-399 (2002)
  REMARK    GENE FAMILY.
            DOI: 10.1080/0735-260291044287
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Bouwmeester,K. and Govers,F.
  TITLE     Arabidopsis L-type lectin receptor kinases: phylogeny,
            classification, and expression profiles
  JOURNAL   J Exp Bot 60 (15), 4383-4396 (2009)
   PUBMED   19773388
  REMARK    GENE FAMILY, AND NOMENCLATURE.
COMMENT     On or before Jan 11, 2011 this sequence version replaced
            gi:75217671, gi:75327691, gi:25387046.
            [CATALYTIC ACTIVITY] Reaction=L-seryl-[protein] + ATP =
            O-phospho-L-seryl-[protein] + ADP + H(+); Xref=Rhea:RHEA:17989,
            Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378,
            ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
            ChEBI:CHEBI:456216; EC=2.7.11.1.
            [CATALYTIC ACTIVITY] Reaction=L-threonyl-[protein] + ATP =
            O-phospho-L-threonyl-[protein] + ADP + H(+); Xref=Rhea:RHEA:46608,
            Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378,
            ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
            ChEBI:CHEBI:456216; EC=2.7.11.1.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000250}; Single-pass
            type I membrane protein {ECO:0000250}.
            [SIMILARITY] In the C-terminal section; belongs to the protein
            kinase superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
            [SIMILARITY] In the N-terminal section; belongs to the leguminous
            lectin family. {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Arabidopsis thaliana"
                     /db_xref="taxon:3702"
     gene            1..686
                     /gene="LECRK71"
                     /locus_tag="At4g04960"
                     /gene_synonym="T32N4.9"
     Protein         1..686
                     /product="L-type lectin-domain containing receptor kinase
                     VII.1"
                     /EC_number="2.7.11.1"
                     /note="LecRK-VII.1"
                     /UniProtKB_evidence="Evidence at transcript level"
     Region          1..20
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          21..686
                     /region_name="Mature chain"
                     /note="L-type lectin-domain containing receptor kinase
                     VII.1. /id=PRO_0000403099."
     Region          21..286
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000255."
     Region          21..256
                     /region_name="Region of interest in the sequence"
                     /note="Legume-lectin like."
     Region          21..253
                     /region_name="lectin_legume_LecRK_Arcelin_ConA"
                     /note="legume lectins, lectin-like receptor kinases,
                     arcelin, concanavalinA, and alpha-amylase inhibitor;
                     cd06899"
                     /db_xref="CDD:173887"
     Site            order(21..22,24,34,63,66,169,194,203,205..207,216..218,
                     220,232)
                     /site_type="other"
                     /note="homotetramer interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:173887"
     Site            order(21..22,24,34,63,66,232)
                     /site_type="other"
                     /note="homodimer interaction site [polypeptide binding]"
                     /db_xref="CDD:173887"
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            64
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            123
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            123
                     /site_type="other"
                     /note="N-linked glycosylation site"
                     /db_xref="CDD:173887"
     Site            order(138,140,154)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:173887"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            224
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          287..307
                     /region_name="Transmembrane region"
                     /note="Helical. /evidence=ECO:0000255."
     Region          308..686
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000255."
     Region          347..628
                     /region_name="Domain"
                     /note="Protein kinase.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00159."
     Region          353..622
                     /region_name="STKc_IRAK"
                     /note="Catalytic domain of the Serine/Threonine kinases,
                     Interleukin-1 Receptor Associated Kinases and related
                     STKs; cd14066"
                     /db_xref="CDD:270968"
     Site            order(353..357,361,374,376,405,422..425,429,431,475,477,
                     479..480,482,493,496,513..516)
                     /site_type="active"
                     /db_xref="CDD:270968"
     Site            order(353..357,361,374,376,405,422..425,429,475,477,
                     479..480,482,493)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270968"
     Site            order(357,429,431,475,477,479,496,513..516)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270968"
     Region          445
                     /region_name="Conflict"
                     /note="S -> R (in Ref. 3; AAP40475 and 4; BAF01352).
                     /evidence=ECO:0000305."
     Site            475
                     /site_type="active"
                     /note="Proton acceptor.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00159,
                     ECO:0000255|PROSITE-ProRule:PRU10027."
     Site            order(492..499,509..516)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270968"
ORIGIN      
        1 mkallflltl flilpnpisa idfifngfnd sssnvslfgi atieskiltl tnqtsfatgr
       61 alynrtirtk dpitssvlpf stsfiftmap ykntlpghgi vflfapstgi ngsssaqhlg
      121 lfnltnngnp snhifgvefd vfanqefsdi danhvgidvn slhsvysnts gywsddgvvf
      181 kplklndgrn yqvwidyrdf vvnvtmqvag kirpkiplls tslnlsdvve demfvgftaa
      241 tgrlvqshki lawsfsnsnf slsnslittg lpsfvlpkds ivkakwfvfv lvlicflvva
      301 lvglvlfavv rkrlerarkr almedwemey wphripyeei esgtkgfdek nvigiggngk
      361 vykgllqggv vevavkrisq essdgmrefv aeisslgrlk hrnlvslrgw ckkevgsfml
      421 vydymengsl drwifendek ittlsceeri rilkgvasgi lylhegwesk vlhrdikasn
      481 vlldrdmipr lsdfglarvh gheqpvrttr vvgtagylap evvktgrast qtdvfaygil
      541 vlevmcgrrp ieegkkplmd wvwglmerge ilngldpqmm mtqgvtevid eaervlqlgl
      601 lcahpdpakr psmrqvvqvf egdkaeifea essedveswm lmkmgsrgss refwygsssh
      661 ptieqirlqs lsvslsswns silegr
//
1..686
/gene="LECRK71"
/locus_tag="At4g04960"
/gene_synonym="T32N4.9"
Feature Q9S9U1 : 1 segment
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