EREC1_ORYSJ
ID EREC1_ORYSJ Reviewed; 978 AA.
AC Q69SP5;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase ER1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305|PubMed:26280413};
DE AltName: Full=ERECTA homolog 1 {ECO:0000303|PubMed:26280413};
DE Short=ER homolog 1 {ECO:0000303|PubMed:26280413};
DE Short=OsER1 {ECO:0000303|PubMed:26280413};
DE AltName: Full=Receptor-like cytoplasmic kinase 204 {ECO:0000303|PubMed:19825577};
DE Short=OsRLCK204 {ECO:0000303|PubMed:19825577};
DE Flags: Precursor;
GN Name=ER1 {ECO:0000303|PubMed:26280413};
GN Synonyms=RLCK204 {ECO:0000303|PubMed:19825577};
GN OrderedLocusNames=Os06g0203800 {ECO:0000312|EMBL:BAF19001.1},
GN LOC_Os06g10230 {ECO:0000305};
GN ORFNames=OSJNBa0016O19.39 {ECO:0000312|EMBL:BAD35990.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825577; DOI=10.1093/mp/ssn047;
RA Vij S., Giri J., Dansana P.K., Kapoor S., Tyagi A.K.;
RT "The receptor-like cytoplasmic kinase (OsRLCK) gene family in rice:
RT organization, phylogenetic relationship, and expression during development
RT and stress.";
RL Mol. Plant 1:732-750(2008).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26280413; DOI=10.1038/nbt.3321;
RA Shen H., Zhong X., Zhao F., Wang Y., Yan B., Li Q., Chen G., Mao B.,
RA Wang J., Li Y., Xiao G., He Y., Xiao H., Li J., He Z.;
RT "Overexpression of receptor-like kinase ERECTA improves thermotolerance in
RT rice and tomato.";
RL Nat. Biotechnol. 33:996-1003(2015).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29692796; DOI=10.3389/fpls.2018.00473;
RA Zhang Y., Li S., Xue S., Yang S., Huang J., Wang L.;
RT "Phylogenetic and CRISPR/Cas9 studies in deciphering the evolutionary
RT trajectory and phenotypic impacts of rice ERECTA genes.";
RL Front. Plant Sci. 9:473-473(2018).
CC -!- FUNCTION: Receptor kinase involved in the regulation of thermotolerance
CC (PubMed:26280413). Functions as positive regulator of heat tolerance
CC (PubMed:26280413). May be involved in the regulation of cell
CC proliferation and cell growth (PubMed:29692796).
CC {ECO:0000269|PubMed:26280413, ECO:0000269|PubMed:29692796}.
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 Evidence={ECO:0000305|PubMed:26280413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:26280413};
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; Evidence={ECO:0000305|PubMed:26280413};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:26280413};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants cannot survive when grown under heat
CC conditions (42 degres Celsius during the day and 35 degres Celsius
CC during the night) (PubMed:26280413). Reduced plant height and reduced
CC panicle length (PubMed:29692796). {ECO:0000269|PubMed:26280413,
CC ECO:0000269|PubMed:29692796}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AP004991; BAD35990.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19001.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96679.1; -; Genomic_DNA.
DR RefSeq; XP_015642019.1; XM_015786533.1.
DR AlphaFoldDB; Q69SP5; -.
DR SMR; Q69SP5; -.
DR STRING; 4530.OS06T0203800-01; -.
DR PaxDb; Q69SP5; -.
DR PRIDE; Q69SP5; -.
DR EnsemblPlants; Os06t0203800-01; Os06t0203800-01; Os06g0203800.
DR GeneID; 4340427; -.
DR Gramene; Os06t0203800-01; Os06t0203800-01; Os06g0203800.
DR KEGG; osa:4340427; -.
DR eggNOG; ENOG502QTEP; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q69SP5; -.
DR OMA; VYEDIMT; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0033612; F:receptor serine/threonine kinase binding; IBA:GO_Central.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 5.
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; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 13.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Growth regulation; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Stress response; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..978
FT /note="LRR receptor-like serine/threonine-protein kinase
FT ER1"
FT /id="PRO_5013532859"
FT TOPO_DOM 25..577
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..978
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 66..87
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 88..112
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 114..136
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 137..159
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 160..184
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 186..208
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 209..232
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 233..257
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 259..278
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 279..302
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 304..327
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 328..350
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 352..375
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 377..399
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 400..423
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 424..447
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 449..470
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 471..494
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 496..518
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 519..543
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 645..916
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 771
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 651..659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 673
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 978 AA; 106746 MW; 9F0485366B705BD2 CRC64;
MTPAPAAASY RALVALLLVA VAVADDGSTL LEIKKSFRNV DNVLYDWAGG DYCSWRGVLC
DNVTFAVAAL NLSGLNLGGE ISPAVGRLKG IVSIDLKSNG LSGQIPDEIG DCSSLKTLDL
SFNSLDGDIP FSVSKLKHIE SLILKNNQLI GVIPSTLSQL PNLKILDLAQ NKLSGEIPRL
IYWNEVLQYL GLRGNNLEGS ISPDICQLTG LWYFDVKNNS LTGPIPETIG NCTSFQVLDL
SYNKLSGSIP FNIGFLQVAT LSLQGNMFTG PIPSVIGLMQ ALAVLDLSYN QLSGPIPSIL
GNLTYTEKLY MQGNKLTGPI PPELGNMSTL HYLELNDNQL SGFIPPEFGK LTGLFDLNLA
NNNFEGPIPD NISSCVNLNS FNAYGNRLNG TIPPSLHKLE SMTYLNLSSN FLSGSIPIEL
SRINNLDTLD LSCNMITGPI PSTIGSLEHL LRLNLSNNGL VGFIPAEIGN LRSIMEIDMS
NNHLGGLIPQ ELGMLQNLML LNLKNNNITG DVSSLMNCFS LNILNVSYNN LAGVVPTDNN
FSRFSPDSFL GNPGLCGYWL GSSCRSSGHQ QKPLISKAAI LGIAVGGLVI LLMILVAVCR
PHSPPVFKDV SVSKPVSNVP PKLVILHMNL SLLVYEDIMT MTENLSEKYI IGYGASSTVY
KCVSKNRKPV AVKKLYAHYP QSFKEFETEL ETVGSIKHRN LVSLQGYSLS PVGNLLFYDY
MENGSLWDVL HEGPTKKKKL DWETRLRIAL GAAQGLAYLH HDCSPRIIHR DVKSKNILLD
KDYEAHLTDF GIAKSLCVSK THTSTYVMGT IGYIDPEYAR TSRLNEKSDV YSYGIVLLEL
LTGKKPVDNE CNLHHLILSK TANNAVMETV DPDIADTCKD LGEVKKVFQL ALLCTKRQPS
DRPTMHEVVR VLDCLVRPDP PPKSAQQLAM PQRPAVPSYI NEYVSLRGTS VLSCANSSCT
SDAELFLKFG EVISQNTE
