LRL21_ARATH
ID LRL21_ARATH Reviewed; 638 AA.
AC Q9FF31;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 2.1 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-2.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-2.1 {ECO:0000303|PubMed:12805585};
GN OrderedLocusNames=At5g38260 {ECO:0000312|Araport:AT5G38260};
GN ORFNames=MXA21.5 {ECO:0000312|EMBL:BAB11292.1};
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}.
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DR EMBL; AB005247; BAB11292.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94287.1; -; Genomic_DNA.
DR RefSeq; NP_198642.1; NM_123187.1.
DR AlphaFoldDB; Q9FF31; -.
DR SMR; Q9FF31; -.
DR STRING; 3702.AT5G38260.1; -.
DR PaxDb; Q9FF31; -.
DR PRIDE; Q9FF31; -.
DR EnsemblPlants; AT5G38260.1; AT5G38260.1; AT5G38260.
DR GeneID; 833808; -.
DR Gramene; AT5G38260.1; AT5G38260.1; AT5G38260.
DR KEGG; ath:AT5G38260; -.
DR Araport; AT5G38260; -.
DR TAIR; locus:2176717; AT5G38260.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_115_3_1; -.
DR InParanoid; Q9FF31; -.
DR OMA; ENGEDTW; -.
DR OrthoDB; 403686at2759; -.
DR PhylomeDB; Q9FF31; -.
DR PRO; PR:Q9FF31; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF31; 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; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF14380; WAK_assoc; 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 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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..638
FT /note="LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE
FT PROTEIN KINASE-like 2.1"
FT /id="PRO_5005942896"
FT TOPO_DOM 30..264
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 321..609
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 444
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 327..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 393
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 484
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 638 AA; 71411 MW; BE493A9BB2F5EA30 CRC64;
MINLSLYQTN SLSYTIIWML FVIPSCVLSV DERQKHCSPT FRCGKQTDLY YPFWSPDREE
CGHPVFKVNC SGDFAEFTIS TVKFHVLEMN YESRIIRLVR TEYLNNLCPW HPENRSINQE
VLPFLQDTEL GTFYYNCSGP TVDELANGYI RQLGCDEEVG GKSYFVSSPS HPGNRAILDG
LSASCERNVD IPVSRSAMET TATNQSLEAI KKVLDVGFEL GFNSDCSLCV ASKGACGFNQ
SSKAFVCYCK DEPHEHTCGK MGIGIGLGCG FLGATLITVC LLCFFFQKRR TSHHLRPRDN
NLKGLVQLKQ YSYAEVRKIT KLFSHTLGKG GFGTVYGGNL CDGRKVAVKI LKDFKSNGED
FINEVASMSQ TSHVNIVSLL GFCYEGSKRA IVYEFLENGS LDQFLSEKKS LNLDVSTLYR
IALGVARGLD YLHHGCKTRI VHFDIKPQNI LLDDTFCPKV SDFGLAKLCE KRESILSLLD
ARGTIGYIAP EVFSGMYGRV SHKSDVYSYG MLVLEMIGAK NKEIEETAAS NSSSAYFPDW
IYKNLENGED TWKFGDEISR EDKEVAKKMT LVGLWCIQPS PLNRPPMNRI VEMMEGSLDV
LEVPPKPSIH YSAEPLPQLS SFSEENSIYT EVFIGSTS
