Y2267_ARATH
ID Y2267_ARATH Reviewed; 658 AA.
AC O48788; Q949V3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Probable inactive receptor kinase At2g26730;
DE Flags: Precursor;
GN OrderedLocusNames=At2g26730; ORFNames=F18A8.10;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637 AND SER-640, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637 AND SER-640, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
CC -!- INTERACTION:
CC O48788; P25854: CAM4; NbExp=2; IntAct=EBI-1239029, EBI-1235664;
CC O48788; P59220: CAM7; NbExp=2; IntAct=EBI-1239029, EBI-1236031;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC003105; AAB95307.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07880.1; -; Genomic_DNA.
DR EMBL; AY050870; AAK92807.1; -; mRNA.
DR EMBL; BT021127; AAX22262.1; -; mRNA.
DR PIR; B84664; B84664.
DR RefSeq; NP_180241.1; NM_128230.3.
DR AlphaFoldDB; O48788; -.
DR SMR; O48788; -.
DR BioGRID; 2566; 32.
DR IntAct; O48788; 20.
DR STRING; 3702.AT2G26730.1; -.
DR iPTMnet; O48788; -.
DR SwissPalm; O48788; -.
DR PaxDb; O48788; -.
DR PRIDE; O48788; -.
DR ProteomicsDB; 242536; -.
DR EnsemblPlants; AT2G26730.1; AT2G26730.1; AT2G26730.
DR GeneID; 817214; -.
DR Gramene; AT2G26730.1; AT2G26730.1; AT2G26730.
DR KEGG; ath:AT2G26730; -.
DR Araport; AT2G26730; -.
DR TAIR; locus:2043858; AT2G26730.
DR eggNOG; ENOG502QT13; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; O48788; -.
DR OMA; FDAHMDA; -.
DR OrthoDB; 714922at2759; -.
DR PhylomeDB; O48788; -.
DR PRO; PR:O48788; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48788; baseline and differential.
DR Genevisible; O48788; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; -; 2.
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 Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..658
FT /note="Probable inactive receptor kinase At2g26730"
FT /id="PRO_0000305194"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 65..89
FT /note="LRR 1"
FT REPEAT 90..113
FT /note="LRR 2"
FT REPEAT 115..138
FT /note="LRR 3"
FT REPEAT 139..164
FT /note="LRR 4"
FT REPEAT 166..183
FT /note="LRR 5"
FT REPEAT 184..207
FT /note="LRR 6"
FT DOMAIN 351..619
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 289..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 357..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 374
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 520
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 403
FT /note="H -> R (in Ref. 3; AAK92807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 658 AA; 71752 MW; 2B951D45A40485B4 CRC64;
MASISWVLNS LFSILLLTQR VNSESTAEKQ ALLTFLQQIP HENRLQWNES DSACNWVGVE
CNSNQSSIHS LRLPGTGLVG QIPSGSLGRL TELRVLSLRS NRLSGQIPSD FSNLTHLRSL
YLQHNEFSGE FPTSFTQLNN LIRLDISSNN FTGSIPFSVN NLTHLTGLFL GNNGFSGNLP
SISLGLVDFN VSNNNLNGSI PSSLSRFSAE SFTGNVDLCG GPLKPCKSFF VSPSPSPSLI
NPSNRLSSKK SKLSKAAIVA IIVASALVAL LLLALLLFLC LRKRRGSNEA RTKQPKPAGV
ATRNVDLPPG ASSSKEEVTG TSSGMGGETE RNKLVFTEGG VYSFDLEDLL RASAEVLGKG
SVGTSYKAVL EEGTTVVVKR LKDVMASKKE FETQMEVVGK IKHPNVIPLR AYYYSKDEKL
LVFDFMPTGS LSALLHGSRG SGRTPLDWDN RMRIAITAAR GLAHLHVSAK LVHGNIKASN
ILLHPNQDTC VSDYGLNQLF SNSSPPNRLA GYHAPEVLET RKVTFKSDVY SFGVLLLELL
TGKSPNQASL GEEGIDLPRW VLSVVREEWT AEVFDVELMR YHNIEEEMVQ LLQIAMACVS
TVPDQRPVMQ EVLRMIEDVN RSETTDDGLR QSSDDPSKGS EGQTPPGESR TPPRSVTP
