LRL27_ARATH
ID LRL27_ARATH Reviewed; 883 AA.
AC F4HQ23; A0A1P8AQB9; Q9C622; Q9FZI5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 3.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 2.7 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-2.7 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-2.7 {ECO:0000303|PubMed:12805585};
GN Synonyms=LRK10L2 {ECO:0000303|PubMed:25510357};
GN OrderedLocusNames=At1g66930 {ECO:0000312|Araport:AT1G66930};
GN ORFNames=F1O19.1 {ECO:0000312|EMBL:AAF98207.1},
GN T4O24.2 {ECO:0000312|EMBL:AAG50593.1};
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).
RN [5]
RP IDENTIFICATION.
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: Membrane {ECO:0000255}; Single-pass type I
CC 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=AAF98207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50593.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE34573.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007152; AAF98207.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC083891; AAG50593.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34573.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; ANM58817.1; -; Genomic_DNA.
DR PIR; B96693; B96693.
DR RefSeq; NP_001321228.1; NM_001334256.1.
DR RefSeq; NP_176865.1; NM_105364.2.
DR AlphaFoldDB; F4HQ23; -.
DR SMR; F4HQ23; -.
DR STRING; 3702.AT1G66930.1; -.
DR iPTMnet; F4HQ23; -.
DR PaxDb; F4HQ23; -.
DR PRIDE; F4HQ23; -.
DR ProteomicsDB; 238392; -.
DR EnsemblPlants; AT1G66930.2; AT1G66930.2; AT1G66930.
DR GeneID; 843011; -.
DR Gramene; AT1G66930.2; AT1G66930.2; AT1G66930.
DR KEGG; ath:AT1G66930; -.
DR Araport; AT1G66930; -.
DR TAIR; locus:2019688; AT1G66930.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_115_3_1; -.
DR InParanoid; F4HQ23; -.
DR OMA; FQCANIP; -.
DR OrthoDB; 403686at2759; -.
DR PRO; PR:F4HQ23; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HQ23; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR045874; LRK10-like.
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; IPR032872; WAK_assoc_C.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27009; PTHR27009; 1.
DR Pfam; PF13947; GUB_WAK_bind; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF14380; WAK_assoc; 2.
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 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; 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..883
FT /note="LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE
FT PROTEIN KINASE-like 2.7"
FT /id="PRO_0000435872"
FT TOPO_DOM 27..491
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..883
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 555..846
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 679
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 561..569
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 546
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 628
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 716
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 719
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 883 AA; 98898 MW; 67B1584A9463AC53 CRC64;
MSYMPTSCLV LFFLLFLFHP LPWALSKEDL GWCEALFQCG NNTAGFPFWG GNRAKPCGHP
LLELRCLNNI TSLNISNHEY NVFHIDQTSN TLRLARTDLL GSFCSAEFNT PTFPREIFKL
FPTYKSLTVL YNCDPKLSYR SSYTCPDLGL FSMSQSLDYQ NSCQDSFKVN VPTSFVPEEK
EMNLTHLESA LRKGFEVKLV IDEIPCQECS SSRGICGFNS TTQICCNVTS LSGGVTCVPQ
HQPSADELRR RCSERFSCGN QRNLYYPFWI PGREYCGHPD FKLDCSGGFA ELNIASVNFR
ILNMSYDSSN KRLARSDYLN DLCPPNPLND EPLIETVLQF SADTELLTLY YDCQLNSSAT
SPFPSSYFGE LGCDEGRSYY VTRNLSSPLL DRFRGVLNNL REMCKRKVSV PASGPALNTL
QTNPNSNNLK MALEHGFELQ DNSNCSMCVL SGGSCGYNQN SSLFVCYCKD GPQDNQCDIN
LDDIIGNRIV AIIIGIFVAL CTIGGFIAFL VLLCPCCKVR IFRNRKTSDD RRQEKLKALI
PLKHYTYAQV KRMTKSFAEV VGRGGFGIVY RGTLCDGRMV AVKVLKESKG NNSEDFINEV
SSMSQTSHVN IVSLLGFCSE GSRRAIIYEF LENGSLDKFI SEKTSVILDL TALYGIALGV
ARGLEYLHYG CKTRIVHFDI KPQNVLLDDN LSPKVSDFGL AKLCEKKESV MSLMDTRGTI
GYIAPEMISR VYGSVSHKSD VYSYGMLVFE MIGARKKERF GQNSANGSSM YFPEWIYKDL
EKADNGDLEH IEIGISSEEE EIAKKMTLVG LWCIQSSPSD RPPMNKVVEM MEGSLDALEV
PPRPVLQQIH VGPLLESSWI TEESSSISEI ENRNLQVCEK ILS
