LRL14_ARATH
ID LRL14_ARATH Reviewed; 663 AA.
AC F4HQ17; Q9C617; Q9C9P0;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 1.4 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-1.4 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-1.4 {ECO:0000303|PubMed:12805585};
GN OrderedLocusNames=At1g66880 {ECO:0000312|Araport:AT1G66880};
GN ORFNames=F4N21.1 {ECO:0000312|EMBL:AAG60067.1},
GN T4O24.5 {ECO:0000312|EMBL:AAG50588.1};
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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).
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:0000250|UniProtKB:P0C5E2};
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=AAG50588.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG60067.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE34567.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013288; AAG60067.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC083891; AAG50588.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34567.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX814972; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; E96692; E96692.
DR RefSeq; NP_176860.2; NM_105359.3.
DR AlphaFoldDB; F4HQ17; -.
DR SMR; F4HQ17; -.
DR PaxDb; F4HQ17; -.
DR PeptideAtlas; F4HQ17; -.
DR PRIDE; F4HQ17; -.
DR ProteomicsDB; 238736; -.
DR GeneID; 843006; -.
DR KEGG; ath:AT1G66880; -.
DR Araport; AT1G66880; -.
DR TAIR; locus:2204465; AT1G66880.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_115_3_1; -.
DR InParanoid; F4HQ17; -.
DR OrthoDB; 700616at2759; -.
DR PRO; PR:F4HQ17; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HQ17; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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:0071456; P:cellular response to hypoxia; HEP:TAIR.
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; IPR032872; WAK_assoc_C.
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 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..663
FT /note="LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE
FT PROTEIN KINASE-like 1.4"
FT /id="PRO_0000435826"
FT TOPO_DOM 26..241
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 334..609
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 282..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 458
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 340..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 663 AA; 74127 MW; C1D820C571A137EE CRC64;
MYYPLSSSLM FFILFSLFYH LPCESSKCES LFQCGNITAS FPFWGGDRHK HCGHPLLELR
CDQNKSTSLF ISDQEFFVLH VDQTSYSLTL ARPDLLHSFC SLTFTNTTLP PEIFELSPAY
KSVTFYHCYP VLPDLSNYTC PVIGPISVSG NPEDHETCFP NFAANVPTSF VTKEKKLNIA
NLESVLEKGF EVNMNVIMKA CQACSYSNES CGFDENFPFE VKCKPHHSPT DTSLSIGAKA
GIAVASVSGL AILLLAGLFL CIRRRRKTQD AQYTSKSLPI TSYSSRDTSR NPTSTTISSS
SNHSLLPSIS NLANRSDYCG VQVFSYEELE EATENFSREL GDGGFGTVYY GVLKDGRAVA
VKRLYERSLK RVEQFKNEIE ILKSLKHPNL VILYGCTSRH SRELLLVYEY ISNGTLAEHL
HGNRAEARPL CWSTRLNIAI ETASALSFLH IKGIIHRDIK TTNILLDDNY QVKVADFGLS
RLFPMDQTHI STAPQGTPGY VDPEYYQCYQ LNEKSDVYSF GVVLTELISS KEAVDITRHR
HDINLANMAV SKIQNNALHE LVDSSLGYDN DPEVRRKMMA VAELAFRCLQ QERDVRPAMD
EIVEILRGIK DDEKKRVLVK SPDVVDIECG GGDDVGLLRN SVPPPISPET DKWTSSSDTA
ASL
