ID LRL22_ARATH Reviewed; 624 AA.
AC F4KA50; Q9FF33;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 2.2 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-2.2 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-2.2 {ECO:0000303|PubMed:12805585};
GN OrderedLocusNames=At5g38240 {ECO:0000312|Araport:AT5G38240};
GN ORFNames=MXA21.7 {ECO:0000312|EMBL:BAB11290.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11290.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005247; BAB11290.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; ANM70965.1; -; Genomic_DNA.
DR RefSeq; NP_001332532.1; NM_001344236.1.
DR AlphaFoldDB; F4KA50; -.
DR SMR; F4KA50; -.
DR STRING; 3702.F4KA50; -.
DR GlyCosmos; F4KA50; 6 sites, No reported glycans.
DR ProteomicsDB; 238573; -.
DR EnsemblPlants; AT5G38240.2; AT5G38240.2; AT5G38240.
DR GeneID; 833806; -.
DR Gramene; AT5G38240.2; AT5G38240.2; AT5G38240.
DR KEGG; ath:AT5G38240; -.
DR Araport; AT5G38240; -.
DR TAIR; AT5G38240; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_115_3_1; -.
DR InParanoid; F4KA50; -.
DR OMA; MSNCEDF; -.
DR PRO; PR:F4KA50; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KA50; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PTHR47974; OS07G0415500 PROTEIN; 1.
DR PANTHER; PTHR47974:SF24; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 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; Protein kinase-like (PK-like); 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; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..624
FT /note="LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE
FT PROTEIN KINASE-like 2.2"
FT /id="PRO_5003315620"
FT TOPO_DOM 31..263
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 317..599
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 587..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 434
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 323..331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 624 AA; 69565 MW; B80E6FA1BD1FAA86 CRC64;
MDYLSSMGSQ TARFCLILLF LFYYLPCALS QDDLWGCGTP FRCGNITAGF PFLGGIRGEV
CGHHSLKLNC NKHSNTTSLI FSGHNYTVLY IDNNNNSVTL GLSRQDFSGP FCSASFSSTL
LSSGLFQNLP SYKSLTVFYA CDPRRHFLGN FTCPVKGLGS IIQNSTYGIL CDGSFSVPVP
TSFVSEEEVL DLTHLESVLR KGFEVKLNID EIPCPLECFS SRANCLFLAG SCCKYHDRTT
TCGGDTGDLL REIIPNTRSI LITIGQVVGF HVFIIVVMII AFLFWRRKKV NDLRKQNLEA
LVTSRRYSYR QIKKITKSFT EVVGRGGFGT VYKGNLRDGR KVAVKILKDS NGNCEDFINE
VASISQTSHV NIVSLLGFCF EKSKRAIVYE FLENGSLDQS SNLDVSTLYG IALGVARGIE
YLHFGCKKRI VHFDIKPQNV LLDENLKPKV ADFGLAKLCE KQESILSLLD TRGTIGYIAP
ELFSRVYGNV SHKSDVYSYG MLVLEMTGAR NKERVQNADS NNSSAYFPDW IFKDLENGDY
VKLLADGLTR EEEDIAKKMI LVGLWCIQFR PSDRPSMNKV VGMMEGNLDS LDPPPKPLLH
MPMQNNNAES SQPSEEDSSI YSEV
//
