LRL26_ARATH
ID LRL26_ARATH Reviewed; 1118 AA.
AC D7SFH9; Q9FZI0;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein SUPPRESSOR OF NPR1-1 CONSTITUTIVE 4 {ECO:0000303|PubMed:20508139};
DE Includes:
DE RecName: Full=Glycerophosphodiester phosphodiesterase protein kinase domain-containing GDPDL2 {ECO:0000305};
DE EC=3.1.4.46 {ECO:0000250|UniProtKB:Q7Y208};
DE AltName: Full=Glycerophosphodiester phosphodiesterase-like 2 {ECO:0000303|PubMed:21323773};
DE Short=ATGDPDL2 {ECO:0000303|PubMed:21323773};
DE Includes:
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 2.6 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-2.6 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-2.6 {ECO:0000303|PubMed:12805585};
GN Synonyms=GDPDL2 {ECO:0000303|PubMed:21323773},
GN SNC4 {ECO:0000303|PubMed:20508139};
GN OrderedLocusNames=At1g66980 {ECO:0000312|Araport:AT1G66980};
GN ORFNames=F1O19.6 {ECO:0000312|EMBL:AAF98210.1};
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 {ECO:0000312|EMBL:ADI71282.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ALA-850.
RX PubMed=20508139; DOI=10.1104/pp.110.158501;
RA Bi D., Cheng Y.T., Li X., Zhang Y.;
RT "Activation of plant immune responses by a gain-of-function mutation in an
RT atypical receptor-like kinase.";
RL Plant Physiol. 153:1771-1779(2010).
RN [2]
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 [3]
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 [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).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18718934; DOI=10.1093/pcp/pcn120;
RA Hayashi S., Ishii T., Matsunaga T., Tominaga R., Kuromori T., Wada T.,
RA Shinozaki K., Hirayama T.;
RT "The glycerophosphoryl diester phosphodiesterase-like proteins SHV3 and its
RT homologs play important roles in cell wall organization.";
RL Plant Cell Physiol. 49:1522-1535(2008).
RN [7]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21323773; DOI=10.1111/j.1365-313x.2011.04538.x;
RA Cheng Y., Zhou W., El Sheery N.I., Peters C., Li M., Wang X., Huang J.;
RT "Characterization of the Arabidopsis glycerophosphodiester
RT phosphodiesterase (GDPD) family reveals a role of the plastid-localized
RT AtGDPD1 in maintaining cellular phosphate homeostasis under phosphate
RT starvation.";
RL Plant J. 66:781-795(2011).
RN [8]
RP ALTERNATIVE SPLICING.
RX PubMed=25267732; DOI=10.1093/mp/ssu103;
RA Zhang Z., Liu Y., Ding P., Li Y., Kong Q., Zhang Y.;
RT "Splicing of receptor-like kinase-encoding SNC4 and CERK1 is regulated by
RT two conserved splicing factors that are required for plant immunity.";
RL Mol. Plant 7:1766-1775(2014).
CC -!- FUNCTION: Atypical receptor-like kinase involved in disease resistance.
CC {ECO:0000269|PubMed:20508139}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:83408; EC=3.1.4.46;
CC Evidence={ECO:0000250|UniProtKB:Q7Y208};
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:0000269|PubMed:20508139};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. Splicing is regulated by
CC SUA and DRT111. {ECO:0000269|PubMed:25267732};
CC Name=1;
CC IsoId=D7SFH9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in shoots, rosette and cauline leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:21323773}.
CC -!- DOMAIN: The two glycerophosphodiester phosphodiesterase domains are
CC predicted to be extracellular and the kinase domain cytoplasmic.
CC {ECO:0000303|PubMed:20508139}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditons. {ECO:0000269|PubMed:18718934, ECO:0000269|PubMed:20508139}.
CC -!- MISCELLANEOUS: Gain-of-function mutant plants snc4-1D show a dwarf
CC phenotype, express constitutively the defense marker genes PR1, PR2,
CC and PDF1.2, and display enhanced resistance to Hyaloperonospora
CC arabidopsidis isolate NOCO2. {ECO:0000269|PubMed:20508139}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glycerophosphoryl
CC diester phosphodiesterase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98210.1; Type=Erroneous gene model prediction;
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DR EMBL; HM461758; ADI71282.1; -; mRNA.
DR EMBL; AC007152; AAF98210.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34581.1; -; Genomic_DNA.
DR PIR; G96693; G96693.
DR RefSeq; NP_176870.2; NM_105369.3. [D7SFH9-1]
DR AlphaFoldDB; D7SFH9; -.
DR SMR; D7SFH9; -.
DR BioGRID; 28237; 1.
DR STRING; 3702.AT1G66980.1; -.
DR iPTMnet; D7SFH9; -.
DR PaxDb; D7SFH9; -.
DR PRIDE; D7SFH9; -.
DR EnsemblPlants; AT1G66980.1; AT1G66980.1; AT1G66980. [D7SFH9-1]
DR GeneID; 843016; -.
DR Gramene; AT1G66980.1; AT1G66980.1; AT1G66980. [D7SFH9-1]
DR KEGG; ath:AT1G66980; -.
DR Araport; AT1G66980; -.
DR TAIR; locus:2019708; AT1G66980.
DR eggNOG; KOG1187; Eukaryota.
DR eggNOG; KOG2258; Eukaryota.
DR HOGENOM; CLU_006333_0_0_1; -.
DR InParanoid; D7SFH9; -.
DR PRO; PR:D7SFH9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; D7SFH9; baseline and differential.
DR Genevisible; D7SFH9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IBA:GO_Central.
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:0006968; P:cellular defense response; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.20.20.190; -; 2.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
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 Pfam; PF03009; GDPD; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51695; SSF51695; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51704; GP_PDE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycerol metabolism;
KW Glycoprotein; Hydrolase; Immunity; Innate immunity; Kinase; Membrane;
KW Nucleotide-binding; Plant defense; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1118
FT /note="Protein SUPPRESSOR OF NPR1-1 CONSTITUTIVE 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430614"
FT TOPO_DOM 36..751
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..1118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..353
FT /note="GP-PDE 1"
FT /evidence="ECO:0000255"
FT DOMAIN 369..670
FT /note="GP-PDE 2"
FT /evidence="ECO:0000255"
FT DOMAIN 805..1094
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 928
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 811..819
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 833
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 850
FT /note="A->T: In snc4-1D; dwarf phenotype, constitutive
FT expression of defense genes and enhanced disease
FT resistance."
SQ SEQUENCE 1118 AA; 123825 MW; A5610A3E81875795 CRC64;
MNSQQSTRTK QMLQQSSTHL LCGVVLLQLF AAQVDAQRST SPWQTLSGDA PLVIARGGFS
GLFPDSSLAA YQFAMVVSVA DVVLWCDVQL TKDGHGICFP DLNLANASNS EEVYPNRQKS
YPVNGVTTKG WFPIDFSLTE LQKVLFSLIR GILSRSGKFD ENGYSISTVQ NVATQMKPAL
FWLNVQHDEF YEQHNLSMSS FLLSTSRTVS IDFISSPEVN FFRKIAGGFG NNGPSFVFQF
MGKEDFEPTT NRTYGSILSN LSFVKTFASG ILVPKSYILP LDDKQYLLPH TSLVQDAHKA
GLKLYASGFA NDVDIAYNYS WDPVSEYLSF VDNGNFSVDG MLSDFPLTAS ASVDCFSHIG
RNATKQVDFL VISKNGASGE YPGCTKLAYE KAIKDGSDVI DCPVQMSSDG IPFCSSSIDL
VNSTTVGQTH LRNRSIIVPE ISSVAGIFTF SLTWHEIQSL TPAISNPFRE NGMSRNPNER
NSGNLISLYE FLNLAKNSTS LSGILISLEN VVYLREKKGL DVVKVVLNRL TETGYIVGTL
KVMIQSTTRL VLVDFKNQST YKTVYKIKET IGNITDSAIE DIKKFANAVV INKASVFPNS
DSFLTGQTTN VLERLQKFQL PVYVELFQNE FVSQPFDFFA DETVEINAYI FGAGINGTIT
EFPYTAARYK RNRCLGREEV PPYMLPVNPG GVLTLISTSS LPPAQDPNPI FTHDDVTEPP
LPPVIAKSPT STLGTPSTIA KPLRNFLKVI RIVSWSVAGV VLFLVLLTLV FCFHRKRETR
LRQQKLKALI PLEHYTYAQV KRITKSFAEV VGRGGFGIVY KGTLSDGRVV AVKVLKDTKG
NGEDFINEVA TMSRTSHLNI VSLLGFCSEG SKRAIIYEFL ENGSLDKFIL GKTSVNMDWT
ALYRIALGVA HGLEYLHHSC KTRIVHFDIK PQNVLLDDSF CPKVSDFGLA KLCEKKESIL
SMLDTRGTIG YIAPEMISRV YGNVSHKSDV YSYGMLVLEI IGARNKEKAN QACASNTSSM
YFPEWVYRDL ESCKSGRHIE DGINSEEDEL AKKMTLVGLW CIQPSPVDRP AMNRVVEMME
GSLEALEVPP RPVLQQIPIS NLHESSILSE DVSVYTEG
