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LRK14_ARATH
ID   LRK14_ARATH             Reviewed;         667 AA.
AC   Q9M3D7;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Putative L-type lectin-domain containing receptor kinase I.4;
DE            Short=LecRK-I.4;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   Name=LECRK14; OrderedLocusNames=At3g45420; ORFNames=F18N11.180;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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).
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:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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; AL132953; CAB72491.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78028.1; -; Genomic_DNA.
DR   PIR; T47482; T47482.
DR   RefSeq; NP_190128.1; NM_114411.2.
DR   AlphaFoldDB; Q9M3D7; -.
DR   SMR; Q9M3D7; -.
DR   PaxDb; Q9M3D7; -.
DR   PRIDE; Q9M3D7; -.
DR   ProteomicsDB; 238731; -.
DR   EnsemblPlants; AT3G45420.1; AT3G45420.1; AT3G45420.
DR   GeneID; 823680; -.
DR   Gramene; AT3G45420.1; AT3G45420.1; AT3G45420.
DR   KEGG; ath:AT3G45420; -.
DR   Araport; AT3G45420; -.
DR   TAIR; locus:2078342; AT3G45420.
DR   eggNOG; ENOG502QSJ4; Eukaryota.
DR   HOGENOM; CLU_000288_62_3_1; -.
DR   InParanoid; Q9M3D7; -.
DR   OMA; CTNDVPE; -.
DR   OrthoDB; 416879at2759; -.
DR   PhylomeDB; Q9M3D7; -.
DR   PRO; PR:Q9M3D7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M3D7; baseline and differential.
DR   Genevisible; Q9M3D7; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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: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   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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Glycoprotein; Kinase; Lectin; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..667
FT                   /note="Putative L-type lectin-domain containing receptor
FT                   kinase I.4"
FT                   /id="PRO_0000403073"
FT   TOPO_DOM        22..294
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..667
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          350..625
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          24..257
FT                   /note="Legume-lectin like"
FT   ACT_SITE        474
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         356..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         378
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   667 AA;  74097 MW;  65F2F83FD4A26DBF CRC64;
     MDCRLHLVLF FSCVCLICLS GQQETGFVYN GFHQEDLFID GIAMILPGGL LQLTNASQLK
     IGHAFFKQPF GFDPSSSLSF YTHFVCALVP PKFGAEVGHG MAFVVSPSMN FSHAFPTQYL
     GVFNSSTNVT SSSHLLAIEL DTVETVDFHD LEKAHVGIDV NNPISIESAL PSYFSDALGK
     NISINLVSGE PVQVWIDYDG SLLNVTLAPI EIQKPNRPLI SRDINLSEIF QDKMYIGFSG
     SNGRLTSNQY ILGWSFSKSK EFMQSLDLSK LPQAPIPRNE QAPVPREEKK KLHPLLIGLV
     ILLVIPVLMV LGGVYWYRRK KYAEVKESWE KEYGPHRYSY KSLYKATNGF VKDALVGKGG
     FGKVYKGTLP GGRHIAVKRL SHDAEQGMKQ FVAEVVTMGN IQHRNLVPLL GYCRRKGELL
     LVSEYMSNGS LDQYLFYNQN PSPSWLQRIS ILKDIASALN YLHSGANPAV LHRDIKASNV
     MLDSEYNGRL GDFGMAKFQD PQGNLSATAA VGTIGYMAPE LIRTGTSKET DVYAFGIFLL
     EVTCGRRPFE PELPVQKKYL VKWVCECWKQ ASLLETRDPK LGREFLSEEV EMVLKLGLLC
     TNDVPESRPD MGQVMQYLSQ KQPLPDFSAD SPGIGGFMPV SVEPSSTIGI PDSSMHVTHS
     ILEGYGR
 
 
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