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
//