LRL12_ARATH
ID LRL12_ARATH Reviewed; 651 AA.
AC P0C5E2; F4IAQ9; Q5BQ05; Q5Q0G6; Q8RX30; Q9LPQ6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 1.2 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-1.2 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-1.2 {ECO:0000303|PubMed:12805585};
GN Synonyms=LRK10L1 {ECO:0000303|PubMed:25510357};
GN OrderedLocusNames=At1g18390 {ECO:0000312|Araport:AT1G18390};
GN ORFNames=F15H18.11 {ECO:0000312|EMBL:AAF25996.1},
GN F15H18.25 {ECO:0000312|EMBL:AAF25996.1};
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 GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Xiao Y.-L., Underwood B.A., Moskal W.A. Jr., Wang W., Redman J.C., Wu H.C.,
RA Utterback T., Town C.D.;
RT "Reconstruction of cDNA sequences for hypothetical genes in Arabidopsis
RT thaliana from 5' and 3' RACE products.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25533478; DOI=10.1007/s00299-014-1724-2;
RA Lim C.W., Yang S.H., Shin K.H., Lee S.C., Kim S.H.;
RT "The AtLRK10L1.2, Arabidopsis ortholog of wheat LRK10, is involved in ABA-
RT mediated signaling and drought resistance.";
RL Plant Cell Rep. 34:447-455(2015).
RN [9]
RP ALTERNATIVE PROMOTER USAGE, ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
RX PubMed=25510357; DOI=10.1007/s00299-014-1729-x;
RA Shin K.H., Yang S.H., Lee J.Y., Lim C.W., Lee S.C., Brown J.W., Kim S.H.;
RT "Alternative splicing of mini-exons in the Arabidopsis leaf rust receptor-
RT like kinase LRK10 genes affects subcellular localisation.";
RL Plant Cell Rep. 34:495-505(2015).
CC -!- FUNCTION: Probable receptor-like serine/threonine-protein kinase
CC involved in abscisic acid (ABA) signaling. Acts as a positive regulator
CC of abiotic stress response. {ECO:0000269|PubMed:25533478}.
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: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:25510357}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000255}; Single-pass
CC type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Comment=A number of isoforms are produced by alternative splicing of
CC isoform 1. {ECO:0000269|PubMed:25510357};
CC Name=1; Synonyms=AtLRK10L-1.2;
CC IsoId=P0C5E2-1; Sequence=Displayed;
CC Name=2; Synonyms=AtLRK10L-1.1;
CC IsoId=P0C5E2-2; Sequence=VSP_058186;
CC Name=3;
CC IsoId=P0C5E2-3; Sequence=VSP_058186, VSP_058185;
CC -!- DISRUPTION PHENOTYPE: ABA-insensitive and drought stress-semsitive.
CC Late flowering. {ECO:0000269|PubMed:25533478}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:25510357}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 2. May be due to an intron retention. {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=AAF25996.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g18390 and At1g18400.; Evidence={ECO:0000305};
CC Sequence=AAM13983.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAX23748.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE29710.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013354; AAF25996.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29709.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29710.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY924673; AAX23748.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY090931; AAM13983.1; ALT_SEQ; mRNA.
DR EMBL; AY800585; AAV68821.1; -; mRNA.
DR PIR; A86318; A86318.
DR RefSeq; NP_001154349.1; NM_001160877.1.
DR RefSeq; NP_173275.4; NM_101697.6. [P0C5E2-2]
DR AlphaFoldDB; P0C5E2; -.
DR SMR; P0C5E2; -.
DR STRING; 3702.AT1G18390.2; -.
DR iPTMnet; P0C5E2; -.
DR PaxDb; P0C5E2; -.
DR PRIDE; P0C5E2; -.
DR ProteomicsDB; 238527; -. [P0C5E2-1]
DR EnsemblPlants; AT1G18390.1; AT1G18390.1; AT1G18390. [P0C5E2-2]
DR GeneID; 838420; -.
DR Gramene; AT1G18390.1; AT1G18390.1; AT1G18390. [P0C5E2-2]
DR KEGG; ath:AT1G18390; -.
DR Araport; AT1G18390; -.
DR TAIR; locus:2014154; AT1G18390.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_115_3_1; -.
DR InParanoid; P0C5E2; -.
DR OrthoDB; 320088at2759; -.
DR PRO; PR:P0C5E2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0C5E2; baseline and differential.
DR Genevisible; P0C5E2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0071215; P:cellular response to abscisic acid stimulus; IMP:TAIR.
DR GO; GO:0042631; P:cellular response to water deprivation; IMP:TAIR.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP: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 Alternative promoter usage; Alternative splicing; ATP-binding;
KW Cell membrane; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW 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..651
FT /note="LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE
FT PROTEIN KINASE-like 1.2"
FT /id="PRO_0000302049"
FT TOPO_DOM 27..264
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 341..613
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 347..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 415
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 512
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..253
FT /note="MNPSTPSLLYTSIFFYFTIIATQTLSLDPKFKACEPKSCGKGPQISYPFYLS
FT GKQESFCGYPSFELTCDDEEKLPVLGISGEEYVIKNISYLTQSFQVVNSKASHDPCPRP
FT LNNLTLHRTPFFVNPSHINFTILYNCSDHLLEDFRTYPLTCARNTSLLRSFGVFDRKKL
FT GKEKQIASMSCQKLVDVPVLASNESDVMGMTYVEILKRGFVLNWTANSCFRCITSGGRC
FT GTDQQEFVCLCPDGPKLHDTCTNG -> MSIFFFFISFVVFSVADLPSCFSADQQYEEC
FT RSRNLTCGSGHRVFESTTYPFWGGFNKPKFCGHSSFKLSCEGDQNLTLAIGNITLRVVS
FT ANLEDHKISVADDSLLDGGCLNIWNFNGKNQFTLDSNTETIDVFVNCSGVAPLQISCEE
FT SYEDPVTYHVLRSSDSDEGCMKYAEIPMLRSAKDELQRSELTFVEALRKGFDLRYIMED
FT KACRRCIDSGGICGSALDSESFRCLCADRPHNSSCDDNTNQG (in isoform 2
FT and isoform 3)"
FT /id="VSP_058186"
FT VAR_SEQ 254..651
FT /note="Missing (in isoform 3)"
FT /id="VSP_058185"
SQ SEQUENCE 651 AA; 72862 MW; 94E210F4B1271C9D CRC64;
MNPSTPSLLY TSIFFYFTII ATQTLSLDPK FKACEPKSCG KGPQISYPFY LSGKQESFCG
YPSFELTCDD EEKLPVLGIS GEEYVIKNIS YLTQSFQVVN SKASHDPCPR PLNNLTLHRT
PFFVNPSHIN FTILYNCSDH LLEDFRTYPL TCARNTSLLR SFGVFDRKKL GKEKQIASMS
CQKLVDVPVL ASNESDVMGM TYVEILKRGF VLNWTANSCF RCITSGGRCG TDQQEFVCLC
PDGPKLHDTC TNGKNDKRRR VIVKVLIGAS AAVVGLIAAS IFWYVYHRRK TKSYRNSSAL
LPRNISSDPS AKSFDIEKAE ELLVGVHIFS YEELEEATNN FDPSKELGDG GFGTVYYGKL
KDGRSVAVKR LYDNNFKRAE QFRNEVEILT GLRHPNLVAL FGCSSKQSRD LLLVYEYVAN
GTLADHLHGP QANPSSLPWS IRLKIAVETA SALKYLHASK IIHRDVKSNN ILLDQNFNVK
VADFGLSRLF PMDKTHVSTA PQGTPGYVDP DYHLCYQLSN KSDVYSFAVV LMELISSLPA
VDITRPRQEI NLSNMAVVKI QNHELRDMVD PSLGFDTDTR VRQTVIAVAE LAFQCLQSDK
DLRPCMSHVQ DTLTRIQNNG FGSEMDVVDV NKSGPLVAQS PDSVIVKWDS K
