Y1848_ARATH
ID Y1848_ARATH Reviewed; 655 AA.
AC Q9LP77; B9DHQ4; Q9ZT08;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable inactive receptor kinase At1g48480;
DE Flags: Precursor;
GN Name=RKL1; OrderedLocusNames=At1g48480; ORFNames=T1N15.9;
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 [GENOMIC DNA] OF 11-655, TISSUE SPECIFICITY, AND LACK
RP OF INDUCTION.
RX PubMed=11100776; DOI=10.1093/pcp/pcd028;
RA Ohtake Y., Takahashi T., Komeda Y.;
RT "Salicylic acid induces the expression of a number of receptor-like kinase
RT genes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 41:1038-1044(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-655.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15388970; DOI=10.1271/bbb.68.1935;
RA Tarutani Y., Morimoto T., Sasaki A., Yasuda M., Nakashita H., Yoshida S.,
RA Yamaguchi I., Suzuki Y.;
RT "Molecular characterization of two highly homologous receptor-like kinase
RT genes, RLK902 and RKL1, in Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 68:1935-1941(2004).
CC -!- INTERACTION:
CC Q9LP77; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-1544507, EBI-20654480;
CC Q9LP77; Q9LT96: At5g49770; NbExp=3; IntAct=EBI-1544507, EBI-17123993;
CC Q9LP77; C0LGN2: LRR-RLK; NbExp=3; IntAct=EBI-1544507, EBI-20652801;
CC Q9LP77; Q8GX94: LRR-RLK; NbExp=2; IntAct=EBI-1544507, EBI-16955556;
CC Q9LP77; Q9FRI1: LRR-RLK; NbExp=2; IntAct=EBI-1544507, EBI-17071528;
CC Q9LP77; F4K6B8: RGI4; NbExp=2; IntAct=EBI-1544507, EBI-1238236;
CC Q9LP77; Q9LP77: RKL1; NbExp=2; IntAct=EBI-1544507, EBI-1544507;
CC Q9LP77; Q9FYK0: TMK2; NbExp=3; IntAct=EBI-1544507, EBI-20652836;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings and leaves. Lower
CC expression in roots, stems, flowers and siliques. Detected in the
CC vascular tissues of roots, in the trichomes of young rosettes leaves
CC and hydathodes, in the floral abscission zones, in filament apex and
CC stomata cells of anthers, in inflorescence stems and in sepals.
CC {ECO:0000269|PubMed:11100776, ECO:0000269|PubMed:15388970}.
CC -!- INDUCTION: By not induced by salicylic acid.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Probably due to the
CC redundancy with other receptor-like kinases.
CC {ECO:0000269|PubMed:15388970}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; AF084034; AAC95351.1; -; Genomic_DNA.
DR EMBL; AC020889; AAF79696.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32298.1; -; Genomic_DNA.
DR EMBL; AK317608; BAH20271.1; -; mRNA.
DR PIR; G96524; G96524.
DR RefSeq; NP_564528.1; NM_103744.2.
DR AlphaFoldDB; Q9LP77; -.
DR SMR; Q9LP77; -.
DR BioGRID; 26494; 28.
DR IntAct; Q9LP77; 36.
DR STRING; 3702.AT1G48480.1; -.
DR iPTMnet; Q9LP77; -.
DR SwissPalm; Q9LP77; -.
DR PaxDb; Q9LP77; -.
DR PRIDE; Q9LP77; -.
DR ProteomicsDB; 232384; -.
DR EnsemblPlants; AT1G48480.1; AT1G48480.1; AT1G48480.
DR GeneID; 841269; -.
DR Gramene; AT1G48480.1; AT1G48480.1; AT1G48480.
DR KEGG; ath:AT1G48480; -.
DR Araport; AT1G48480; -.
DR TAIR; locus:2198090; AT1G48480.
DR eggNOG; ENOG502QSFF; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9LP77; -.
DR OMA; ILMVLCR; -.
DR OrthoDB; 287580at2759; -.
DR PhylomeDB; Q9LP77; -.
DR PRO; PR:Q9LP77; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LP77; baseline and differential.
DR Genevisible; Q9LP77; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..655
FT /note="Probable inactive receptor kinase At1g48480"
FT /id="PRO_0000324843"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 71..95
FT /note="LRR 1"
FT REPEAT 98..120
FT /note="LRR 2"
FT REPEAT 122..144
FT /note="LRR 3"
FT REPEAT 146..169
FT /note="LRR 4"
FT REPEAT 170..192
FT /note="LRR 5"
FT REPEAT 194..215
FT /note="LRR 6"
FT DOMAIN 371..646
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 234..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 377..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 622
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CONFLICT 483
FT /note="D -> N (in Ref. 3; AAC95351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 71131 MW; 734B4A7D2E956456 CRC64;
MRVFFFPNSS MAILSVFLSL LLLSLPLPST QDLNADRTAL LSLRSAVGGR TFRWNIKQTS
PCNWAGVKCE SNRVTALRLP GVALSGDIPE GIFGNLTQLR TLSLRLNALS GSLPKDLSTS
SNLRHLYLQG NRFSGEIPEV LFSLSHLVRL NLASNSFTGE ISSGFTNLTK LKTLFLENNQ
LSGSIPDLDL PLVQFNVSNN SLNGSIPKNL QRFESDSFLQ TSLCGKPLKL CPDEETVPSQ
PTSGGNRTPP SVEGSEEKKK KNKLSGGAIA GIVIGCVVGF ALIVLILMVL CRKKSNKRSR
AVDISTIKQQ EPEIPGDKEA VDNGNVYSVS AAAAAAMTGN GKASEGNGPA TKKLVFFGNA
TKVFDLEDLL RASAEVLGKG TFGTAYKAVL DAVTVVAVKR LKDVMMADKE FKEKIELVGA
MDHENLVPLR AYYFSRDEKL LVYDFMPMGS LSALLHGNRG AGRSPLNWDV RSRIAIGAAR
GLDYLHSQGT STSHGNIKSS NILLTKSHDA KVSDFGLAQL VGSSATNPNR ATGYRAPEVT
DPKRVSQKGD VYSFGVVLLE LITGKAPSNS VMNEEGVDLP RWVKSVARDE WRREVFDSEL
LSLATDEEEM MAEMVQLGLE CTSQHPDQRP EMSEVVRKME NLRPYSGSDQ VNEAD
