Y2278_ARATH
ID Y2278_ARATH Reviewed; 742 AA.
AC C0LGJ9; O64505; Q84WD0;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At2g02780;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g02780; ORFNames=T20F6.8;
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=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-742.
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).
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 -!- INTERACTION:
CC C0LGJ9; C0LGE4: At1g12460; NbExp=2; IntAct=EBI-20651541, EBI-17126713;
CC C0LGJ9; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-20651541, EBI-20651385;
CC C0LGJ9; A0A178VQN9: At2g42290; NbExp=2; IntAct=EBI-20651541, EBI-20655829;
CC C0LGJ9; Q9LRT1: At3g28040; NbExp=2; IntAct=EBI-20651541, EBI-16956175;
CC C0LGJ9; C0LGS2: At4g36180; NbExp=2; IntAct=EBI-20651541, EBI-16955302;
CC C0LGJ9; C0LGS3: At4g37250; NbExp=2; IntAct=EBI-20651541, EBI-16955335;
CC C0LGJ9; A0A1P8B6S7: At4g39270; NbExp=2; IntAct=EBI-20651541, EBI-20661308;
CC C0LGJ9; Q0WR59: At5g10020; NbExp=2; IntAct=EBI-20651541, EBI-16945916;
CC C0LGJ9; C0LGU1: At5g37450; NbExp=2; IntAct=EBI-20651541, EBI-20661217;
CC C0LGJ9; A0A178UFM8: AXX17_At5g50380; NbExp=2; IntAct=EBI-20651541, EBI-20653342;
CC C0LGJ9; A0A178UAF6: AXX17_At5g67350; NbExp=2; IntAct=EBI-20651541, EBI-20661274;
CC C0LGJ9; Q9M2Z1: BAM2; NbExp=2; IntAct=EBI-20651541, EBI-16933791;
CC C0LGJ9; C0LGF4: FEI1; NbExp=2; IntAct=EBI-20651541, EBI-16896366;
CC C0LGJ9; C0LGL9: FEI2; NbExp=2; IntAct=EBI-20651541, EBI-16921113;
CC C0LGJ9; C0LGN2: LRR-RLK; NbExp=2; IntAct=EBI-20651541, EBI-20652801;
CC C0LGJ9; C0LGN7: LRR-RLK; NbExp=2; IntAct=EBI-20651541, EBI-20651518;
CC C0LGJ9; Q8GY50: LRR-RLK; NbExp=2; IntAct=EBI-20651541, EBI-20658163;
CC C0LGJ9; Q9FRI1: LRR-RLK; NbExp=2; IntAct=EBI-20651541, EBI-17071528;
CC C0LGJ9; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-20651541, EBI-17121474;
CC C0LGJ9; Q9FZ59: PEPR2; NbExp=2; IntAct=EBI-20651541, EBI-20652612;
CC C0LGJ9; Q9LPT1: PRK5; NbExp=2; IntAct=EBI-20651541, EBI-16914400;
CC C0LGJ9; Q9LZV7: PXC2; NbExp=2; IntAct=EBI-20651541, EBI-1238200;
CC C0LGJ9; F4I2N7-2: RLK7; NbExp=2; IntAct=EBI-20651541, EBI-20651307;
CC C0LGJ9; O82318: SKM1; NbExp=2; IntAct=EBI-20651541, EBI-20661246;
CC C0LGJ9; Q9SKB2: SOBIR1; NbExp=2; IntAct=EBI-20651541, EBI-16905883;
CC C0LGJ9; P43298: TMK1; NbExp=2; IntAct=EBI-20651541, EBI-2023970;
CC C0LGJ9; Q9FYK0: TMK2; NbExp=2; IntAct=EBI-20651541, EBI-20652836;
CC C0LGJ9; Q9SIT1: TMK3; NbExp=2; IntAct=EBI-20651541, EBI-16896864;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC 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=AAC05344.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002521; AAC05344.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05623.1; -; Genomic_DNA.
DR EMBL; FJ708689; ACN59284.1; -; mRNA.
DR EMBL; BT003963; AAO42008.1; -; mRNA.
DR PIR; T00850; T00850.
DR RefSeq; NP_178381.3; NM_126333.4.
DR AlphaFoldDB; C0LGJ9; -.
DR SMR; C0LGJ9; -.
DR BioGRID; 209; 47.
DR IntAct; C0LGJ9; 74.
DR STRING; 3702.AT2G02780.1; -.
DR PaxDb; C0LGJ9; -.
DR PRIDE; C0LGJ9; -.
DR ProteomicsDB; 243188; -.
DR EnsemblPlants; AT2G02780.1; AT2G02780.1; AT2G02780.
DR GeneID; 814807; -.
DR Gramene; AT2G02780.1; AT2G02780.1; AT2G02780.
DR KEGG; ath:AT2G02780; -.
DR Araport; AT2G02780; -.
DR TAIR; locus:2058872; AT2G02780.
DR eggNOG; ENOG502QTFC; Eukaryota.
DR HOGENOM; CLU_000288_108_0_1; -.
DR InParanoid; C0LGJ9; -.
DR OMA; HESSMKA; -.
DR OrthoDB; 496522at2759; -.
DR PhylomeDB; C0LGJ9; -.
DR PRO; PR:C0LGJ9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; C0LGJ9; baseline and differential.
DR Genevisible; C0LGJ9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase 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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR045272; ANXUR1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR27003; PTHR27003; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..742
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At2g02780"
FT /id="PRO_0000387549"
FT TOPO_DOM 26..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 74..96
FT /note="LRR 1"
FT REPEAT 104..128
FT /note="LRR 2"
FT REPEAT 130..154
FT /note="LRR 3"
FT REPEAT 156..177
FT /note="LRR 4"
FT REPEAT 178..204
FT /note="LRR 5"
FT REPEAT 206..223
FT /note="LRR 6"
FT REPEAT 224..247
FT /note="LRR 7"
FT REPEAT 249..271
FT /note="LRR 8"
FT REPEAT 273..294
FT /note="LRR 9"
FT DOMAIN 426..720
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 386..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 742 AA; 82002 MW; 637D7BC29DB8660D CRC64;
MQISLQIHLS SFTFLLLIFL LPVLSESQVA SSESQTLLEI QKQLQYPQVL QSWTDTTNFC
HIRPSPSLRI ICLHGHVTEL TVTGNRTSKL SGSFHKLFTL LTQLSSLKTL SLTSLGISGS
LSPKIITKLS PSLESLNLSS NFISGKIPEE IVSLKNLKSL VLRDNMFWGF VSDDLRGLSN
LQELDLGGNK LGPEVPSLPS KLTTVSLKNN SFRSKIPEQI KKLNNLQSLD LSSNEFTGSI
PEFLFSIPSL QILSLDQNLL SGSLPNSSCT SSKIITLDVS HNLLTGKLPS CYSSKSFSNQ
TVLFSFNCLS LIGTPNAKYQ RPLSFCQNQA SKAIAVEPIP KAKDKDSARI KLGLVILIII
GVIILAAILV LLVLIALKRR RSRSEDDPFE VNNSNNERHA SDKVSVCSTT TASSKSLPDS
RRVPQTMRSA VIGLPPYRVF SLEELEEATN DFDAASLFCE QLYRGCLREG IPVTVRVIKL
KQKSLPQSLA QQMEVLSKLR HMHLVSVLGH SIASNQDHNQ HAGHTIFIVQ EYISSGSLRD
FLTNCRKKEV LKWPQRMAIA IGVARGIQFL HMGVAPGIFG NNLKIENIML DETLTVKISG
YTIPLPSKVG EERPQAKKPR SNEDREKEDV YQFGVILLQI ITGKVVAAGS SEMGSLKLQL
ENGLRDEPSV LSSLADPSVK GSYAYESLRT TVEFAINCLC EDQSKRPSIE DVVWNLQYTI
QVQQGWRPSS GNHESSMKAI YE
