LRL15_ARATH
ID LRL15_ARATH Reviewed; 636 AA.
AC F4I3V3; Q9CAS4;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 1.5 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-1.5 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-1.5 {ECO:0000303|PubMed:12805585};
GN OrderedLocusNames=At1g69910 {ECO:0000312|Araport:AT1G69910};
GN ORFNames=T17F3.6 {ECO:0000312|EMBL:AAG52555.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 PubMed=11526204; DOI=10.1073/pnas.181141598;
RA Shiu S.H., Bleecker A.B.;
RT "Receptor-like kinases from Arabidopsis form a monophyletic gene family
RT related to animal receptor kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10763-10768(2001).
RN [4]
RP GENE FAMILY.
RX PubMed=12805585; DOI=10.1104/pp.103.021964;
RA Shiu S.H., Bleecker A.B.;
RT "Expansion of the receptor-like kinase/Pelle gene family and receptor-like
RT proteins in Arabidopsis.";
RL Plant Physiol. 132:530-543(2003).
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|UniProtKB:P0C5E2};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52555.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010675; AAG52555.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34997.1; -; Genomic_DNA.
DR PIR; E96721; E96721.
DR RefSeq; NP_177149.2; NM_105659.3.
DR AlphaFoldDB; F4I3V3; -.
DR SMR; F4I3V3; -.
DR IntAct; F4I3V3; 1.
DR STRING; 3702.AT1G69910.1; -.
DR PaxDb; F4I3V3; -.
DR PRIDE; F4I3V3; -.
DR ProteomicsDB; 238433; -.
DR EnsemblPlants; AT1G69910.1; AT1G69910.1; AT1G69910.
DR GeneID; 843327; -.
DR Gramene; AT1G69910.1; AT1G69910.1; AT1G69910.
DR KEGG; ath:AT1G69910; -.
DR Araport; AT1G69910; -.
DR TAIR; locus:2196754; AT1G69910.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_115_3_1; -.
DR InParanoid; F4I3V3; -.
DR OMA; NCSHCPW; -.
DR OrthoDB; 684563at2759; -.
DR PRO; PR:F4I3V3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I3V3; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR045274; WAK-like.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..636
FT /note="LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE
FT PROTEIN KINASE-like 1.5"
FT /id="PRO_5003316225"
FT TOPO_DOM 27..257
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 324..628
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 458
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 330..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 636 AA; 70530 MW; A9C09604CF7E63F0 CRC64;
MSQPPWRCFS LLIFVLTIFS TKPSSASTSC SSSFHCPPFN SSPPYPFSAS PGCGHPNFQI
QCSSSRATIT IKNLTFSILH YSSISSSLTL SPITNTNRNT NNCSSLRFSS SPNRFIDLTG
SPFRVSDSSC SRLSLLRPCS PFTLPNCSRC PWDCKLLKNP GRILHGCEST HGSLSEQGCQ
GDLLGFLQDF FTRFGFEVEW DESQDPYFIK CRDCQIKNGV CGFNSTHPNQ DFICFHKSRS
ELVTQRDNNK RVNHIAVLSL IFALTCLLLV FSVAVAIFRS RRASFLSSIN EEDPAALFLR
HHRSAALLPP VFTFEELESA TNKFDPKRKI GDGGFGSVYL GQLSDGQLLA VKFLHHHHGA
TAAATEHCKA FSMKSFCNEI LILSSINHPN LVKLHGYCSD PRGLLLVHDY VTNGTLADHL
HGRGPKMTWR VRLDIALQTA LAMEYLHFDI VPPVVHRDIT SSNIFVEKDM KIKVGDFGLS
RLLVFSETTV NSATSSDYVC TGPQGTPGYL DPDYHRSFRL TEKSDVYSYG VVLMELITGM
KAVDQRREKR DMALADLVVS KIQMGLLDQV IDPLLALDGD DVAAVSDGFG VAAVAELAFR
CVATDKDDRP DAKEIVQELR RIRSHTRVAD DDVAKN
