LRL11_ARATH
ID LRL11_ARATH Reviewed; 629 AA.
AC Q9C6K9; Q941D0;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 1.1 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-1.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-1.1 {ECO:0000303|PubMed:12805585};
GN Synonyms=LRK10L4 {ECO:0000303|PubMed:25510357};
GN OrderedLocusNames=At1g25390 {ECO:0000312|Araport:AT1G25390};
GN ORFNames=F2J7.14 {ECO:0000312|EMBL:AAG50813.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
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).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=25510357; DOI=10.1007/s00299-014-1729-x;
RA Shin K.H., Yang S.H., Lee J.Y., Lim C.W., Lee S.C., Brown J.W., Kim S.H.;
RT "Alternative splicing of mini-exons in the Arabidopsis leaf rust receptor-
RT like kinase LRK10 genes affects subcellular localisation.";
RL Plant Cell Rep. 34:495-505(2015).
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:0000269|PubMed:25510357};
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=AAK97715.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC079281; AAG50813.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30616.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60432.1; -; Genomic_DNA.
DR EMBL; AY052245; AAK97715.1; ALT_FRAME; mRNA.
DR PIR; H86383; H86383.
DR RefSeq; NP_001322718.1; NM_001332678.1.
DR RefSeq; NP_173910.1; NM_102350.3.
DR AlphaFoldDB; Q9C6K9; -.
DR SMR; Q9C6K9; -.
DR STRING; 3702.AT1G25390.1; -.
DR iPTMnet; Q9C6K9; -.
DR PaxDb; Q9C6K9; -.
DR PRIDE; Q9C6K9; -.
DR ProteomicsDB; 238735; -.
DR EnsemblPlants; AT1G25390.1; AT1G25390.1; AT1G25390.
DR EnsemblPlants; AT1G25390.2; AT1G25390.2; AT1G25390.
DR GeneID; 839125; -.
DR Gramene; AT1G25390.1; AT1G25390.1; AT1G25390.
DR Gramene; AT1G25390.2; AT1G25390.2; AT1G25390.
DR KEGG; ath:AT1G25390; -.
DR Araport; AT1G25390; -.
DR TAIR; locus:2031230; AT1G25390.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_115_3_1; -.
DR InParanoid; Q9C6K9; -.
DR OMA; FITIHRM; -.
DR OrthoDB; 573754at2759; -.
DR PhylomeDB; Q9C6K9; -.
DR PRO; PR:Q9C6K9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6K9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR044652; LRK10L-1.1/1.2/1.3/1.4.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR46008; PTHR46008; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 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;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..629
FT /note="LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE
FT PROTEIN KINASE-like 1.1"
FT /id="PRO_5005942625"
FT TOPO_DOM 20..225
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 291..565
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 609..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 297..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 365
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 463
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 629 AA; 70856 MW; D361F8369965639D CRC64;
METVSVLLFF FLFLLAAEAR STKRTGCKDF TCGEHDFKFP FFRTDMPSRC GLFKLNCSAN
IPEIQLEKDG KWYTVKSVSQ ANTITIIDPR LNQSLTTGGC SDLSSFSLPD SPWLKLNTLY
KCNNSSRKNG FSYANCRGEG SSLYYNLGDD HDVSGCSPIK TPESWVTPKN GNLSDVNATF
SLHIELPGNC FRCHNNGGEC TKVKNNYRCV GANTEPNNYH AEMRLGLGIG GSVILIIILV
ALFAVIHRNY RRKDGSELSR DNSKSDVEFS QVFFKIPIFS YKELQAATDN FSKDRLLGDG
GFGTVYYGKV RDGREVAVKR LYEHNYRRLE QFMNEIEILT RLHHKNLVSL YGCTSRRSRE
LLLVYEFIPN GTVADHLYGE NTPHQGFLTW SMRLSIAIET ASALAYLHAS DIIHRDVKTT
NILLDRNFGV KVADFGLSRL LPSDVTHVST APQGTPGYVD PEYHRCYHLT DKSDVYSFGV
VLVELISSKP AVDISRCKSE INLSSLAINK IQNHATHELI DQNLGYATNE GVRKMTTMVA
ELAFQCLQQD NTMRPTMEQV VHELKGIQNE EQKCPTYDYR EETIIPHPSP PDWGEAALLK
NMKFPRSPVS VTDQWTSKST TPNTSAYEF
