LRL24_ARATH
ID LRL24_ARATH Reviewed; 617 AA.
AC F4HQ22; Q9C621;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 2.4 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-2.4 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-2.4 {ECO:0000303|PubMed:12805585};
GN OrderedLocusNames=At1g66920 {ECO:0000312|Araport:AT1G66920};
GN ORFNames=T4O24.7 {ECO:0000312|EMBL:AAG50589.1};
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: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4HQ22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HQ22-2; Sequence=VSP_058195;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC083891; AAG50589.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34571.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34572.1; -; Genomic_DNA.
DR PIR; A96693; A96693.
DR RefSeq; NP_001185332.1; NM_001198403.2. [F4HQ22-1]
DR RefSeq; NP_176864.1; NM_105363.2. [F4HQ22-2]
DR AlphaFoldDB; F4HQ22; -.
DR SMR; F4HQ22; -.
DR IntAct; F4HQ22; 1.
DR STRING; 3702.AT1G66920.2; -.
DR PaxDb; F4HQ22; -.
DR PRIDE; F4HQ22; -.
DR ProteomicsDB; 238390; -. [F4HQ22-1]
DR EnsemblPlants; AT1G66920.1; AT1G66920.1; AT1G66920. [F4HQ22-2]
DR EnsemblPlants; AT1G66920.2; AT1G66920.2; AT1G66920. [F4HQ22-1]
DR GeneID; 843010; -.
DR Gramene; AT1G66920.1; AT1G66920.1; AT1G66920. [F4HQ22-2]
DR Gramene; AT1G66920.2; AT1G66920.2; AT1G66920. [F4HQ22-1]
DR KEGG; ath:AT1G66920; -.
DR Araport; AT1G66920; -.
DR TAIR; locus:2204475; AT1G66920.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; F4HQ22; -.
DR OMA; GFSEINI; -.
DR PRO; PR:F4HQ22; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HQ22; 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; IPR025287; WAK_GUB.
DR PANTHER; PTHR27009; PTHR27009; 2.
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 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; 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..617
FT /note="LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE
FT PROTEIN KINASE-like 2.4"
FT /id="PRO_5003309388"
FT TOPO_DOM 27..243
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 307..594
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 431
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 313..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 380
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 468
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 471
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 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 237..245
FT /note="RLSSEAKIA -> P (in isoform 2)"
FT /id="VSP_058195"
SQ SEQUENCE 617 AA; 69276 MW; 080ACBB49BB08627 CRC64;
MYYLPSSCLV LFLFFSLFYH LPCASSKQTL GWCESQFQCG NITAGFPFWG GNRPEVCGHP
LLELHCLDNI TSLTISDHLY HVLSINHTYN TLRVARTDFL QSICLSPFPF ANATLPPEIF
DILPTYKSVT LYRCYPVIPD LARYGCPAIG SVSVSDNLEN PVSCEARFTV NIPTSFVPNE
KRLNITSLVR DVRNGFEVRL RIDENSCQEC SSSHKYCGFT GTLPLETKCR PLNLPTRLSS
EAKIATIAGV SLLPFLVLTL VVHIIRKQKT SNDKGQQDLK EHIPKPRIKA LIQLKQYSYE
QVKRITNSFA EVVGRGGFGI VYRGTLSDGR MVAVKVLKDL KGNNGEDFIN EVASMSQTSH
VNIVTLLGFC SEGYKRAIIY EFMENGSLDK FISSKKSSTM DWRELYGIAL GVARGLEYLH
HGCRTRIVHF DIKPQNVLLD DNLSPKVSDF GLAKLCERKE SILSLMDTRG TIGYIAPEVF
SRVYGSVSHK SDVYSYGMLV LDIIGARNKT STEDTTSSTS SMYFPEWIYK DLEKGDNGRL
IVNRSEEDEI AKKMTLVGLW CIQPWPLDRP AMNRVVEMME GNLDALEVPP RPVLQCSVVP
HLDSSWISEE NSISSEI
