LRL13_ARATH
ID LRL13_ARATH Reviewed; 686 AA.
AC Q8VYG0; Q9FF35;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 1.3 {ECO:0000303|PubMed:12805585};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10L-1.3 {ECO:0000305};
DE Flags: Precursor;
GN Name=LRK10L-1.3 {ECO:0000303|PubMed:12805585};
GN Synonyms=LRK10L3 {ECO:0000303|PubMed:25510357};
GN OrderedLocusNames=At5g38210 {ECO:0000312|Araport:AT5G38210};
GN ORFNames=MXA21.10 {ECO:0000312|EMBL:BAB11288.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [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 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 -!- 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:25510357};
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=BAB11288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005247; BAB11288.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94281.1; -; Genomic_DNA.
DR EMBL; AY072106; AAL59928.1; -; mRNA.
DR EMBL; AY133861; AAM91795.1; -; mRNA.
DR RefSeq; NP_198637.2; NM_123182.4.
DR AlphaFoldDB; Q8VYG0; -.
DR SMR; Q8VYG0; -.
DR IntAct; Q8VYG0; 3.
DR STRING; 3702.AT5G38210.1; -.
DR iPTMnet; Q8VYG0; -.
DR PaxDb; Q8VYG0; -.
DR PRIDE; Q8VYG0; -.
DR ProteomicsDB; 238528; -.
DR EnsemblPlants; AT5G38210.1; AT5G38210.1; AT5G38210.
DR GeneID; 833803; -.
DR Gramene; AT5G38210.1; AT5G38210.1; AT5G38210.
DR KEGG; ath:AT5G38210; -.
DR Araport; AT5G38210; -.
DR TAIR; locus:2176667; AT5G38210.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_115_3_1; -.
DR InParanoid; Q8VYG0; -.
DR PhylomeDB; Q8VYG0; -.
DR PRO; PR:Q8VYG0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VYG0; differential.
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; HDA:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
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; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..686
FT /note="LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE
FT PROTEIN KINASE-like 1.3"
FT /id="PRO_5005941403"
FT TOPO_DOM 34..264
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 358..633
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 657..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 482
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 364..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 432
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 529
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 686 AA; 75294 MW; F65CF37DC1541CA2 CRC64;
MFSPVLFRFS KPNSFLVLLF FLSYIHFLPC AQSQREPCDT LFRCGDLTAG FPFWGVARPQ
PCGHPSLGLH CQKQTNSTSL IISSLMYRVL EVNTTTSTLK LVRQDFSGPF CSASFSGATL
TPELFELLPD YKTLSAYYLC NPSLHYPAKF ICPNKGVGSI HQDDLYHNHC GGIFNITVPI
GYAPEEGALN VTNLESVLKK GFEVKLSIDE RPCQECKTNG GICAYHVATP VCCKTNSSSE
VNCTPMMPSG SSAHAGLSKK GKIGIGFASG FLGATLIGGC LLCIFIRRRK KLATQYTNKG
LSTTTPYSSN YTMSNTPTST TISGSNHSLV PSISNLGNGS VYSGIQVFSY EELEEATENF
SKELGDGGFG TVYYGTLKDG RAVAVKRLFE RSLKRVEQFK NEIDILKSLK HPNLVILYGC
TTRHSRELLL VYEYISNGTL AEHLHGNQAQ SRPICWPARL QIAIETASAL SYLHASGIIH
RDVKTTNILL DSNYQVKVAD FGLSRLFPMD QTHISTAPQG TPGYVDPEYY QCYRLNEKSD
VYSFGVVLSE LISSKEAVDI TRHRHDINLA NMAISKIQND AVHELADLSL GFARDPSVKK
MMSSVAELAF RCLQQERDVR PSMDEIVEVL RVIQKDGISD SKDVVVEIDV NGGDDVGLLK
HGVPPPLSPE TDKTTASSSN TTASSF
