EREC2_ORYSJ
ID EREC2_ORYSJ Reviewed; 986 AA.
AC I1Z695; Q0DX34; Q6ZGC7;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase ER2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305|PubMed:29692796};
DE AltName: Full=ERECTA homolog 2 {ECO:0000303|PubMed:29692796};
DE Short=ER homolog 2 {ECO:0000303|PubMed:29692796};
DE Short=OsER2 {ECO:0000303|PubMed:29692796};
DE AltName: Full=Receptor-like cytoplasmic kinase 85 {ECO:0000303|PubMed:19825577};
DE Short=OsRLCK85 {ECO:0000303|PubMed:19825577};
DE Flags: Precursor;
GN Name=ER2 {ECO:0000303|PubMed:29692796};
GN Synonyms=RLCK85 {ECO:0000303|PubMed:19825577};
GN OrderedLocusNames=Os02g0777400 {ECO:0000312|PROSITE:PS51450},
GN LOC_Os02g53720 {ECO:0000305};
GN ORFNames=OJ1534_E09.14 {ECO:0000312|EMBL:BAD16970.1};
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 [MRNA].
RA Liu J., Xie X.;
RT "Cloning of ERECTA-like genes from japonica rice.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 540-986.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, 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 that may be involved in the regulation of
CC cell proliferation and cell growth. {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:29692796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:29692796};
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:29692796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:29692796};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant height, reduced panicle length and
CC reduced seed set. {ECO:0000269|PubMed:29692796}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD16970.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF10204.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAG87384.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAS81182.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JN991005; AFJ14786.1; -; mRNA.
DR EMBL; AP004140; BAD16970.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008208; BAF10204.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; BAS81182.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK060260; BAG87384.1; ALT_INIT; mRNA.
DR RefSeq; XP_015623966.1; XM_015768480.1.
DR AlphaFoldDB; I1Z695; -.
DR SMR; I1Z695; -.
DR STRING; 4530.OS02T0777400-01; -.
DR EnsemblPlants; Os02t0777400-01; Os02t0777400-01; Os02g0777400.
DR GeneID; 4330905; -.
DR Gramene; Os02t0777400-01; Os02t0777400-01; Os02g0777400.
DR KEGG; osa:4330905; -.
DR eggNOG; ENOG502QTEP; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
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: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; 2.
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; 14.
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 Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..986
FT /note="LRR receptor-like serine/threonine-protein kinase
FT ER2"
FT /id="PRO_5003655149"
FT TOPO_DOM 22..581
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..986
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 68..89
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 90..114
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 116..138
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 139..161
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 162..186
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 188..210
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 211..233
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 234..259
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 261..280
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 281..304
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 306..329
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 330..352
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 354..377
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 379..401
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 402..425
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 427..449
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 450..472
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 473..498
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 500..520
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 521..545
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 653..934
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 779
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 659..667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 986 AA; 107717 MW; 025F3948ACDD8895 CRC64;
MTTTTTTRLL LAAILLAVAA ADDDGQTLLE IKKSFRNVDN VLYDWAGDGA PRRYCSWRGV
LCDNVTFAVA ALNLSGLNLG GEISPAIGNL KSVESIDLKS NELSGQIPDE IGDCTSLKTL
DLSSNNLGGD IPFSISKLKH LENLILKNNQ LVGMIPSTLS QLPNLKILDL AQNKLNGEIP
RLIYWNEVLQ YLGLRSNNLE GSLSPEMCQL TGLWYFDVKN NSLTGIIPDT IGNCTSFQVL
DLSYNRLTGE IPFNIGFLQV ATLSLQGNNF SGPIPSVIGL MQALAVLDLS FNQLSGPIPS
ILGNLTYTEK LYLQGNRLTG SIPPELGNMS TLHYLELNDN QLTGFIPPEL GKLTGLFDLN
LANNNLEGPI PDNISSCMNL ISFNAYGNKL NGTVPRSLHK LESITYLNLS SNYLSGAIPI
ELAKMKNLDT LDLSCNMVAG PIPSAIGSLE HLLRLNFSNN NLVGYIPAEF GNLRSIMEID
LSSNHLGGLI PQEVGMLQNL ILLKLESNNI TGDVSSLINC FSLNVLNVSY NNLAGIVPTD
NNFSRFSPDS FLGNPGLCGY WLGSSCYSTS HVQRSSVSRS AILGIAVAGL VILLMILAAA
CWPHWAQVPK DVSLCKPDIH ALPSSNVPPK LVILHMNMAF LVYEDIMRMT ENLSEKYIIG
YGASSTVYKC VLKNCKPVAI KKLYAHYPQS LKEFETELET VGSIKHRNLV SLQGYSLSPA
GNLLFYDYLE NGSLWDVLHA GSSKKQKLDW EARLRIALGA AQGLAYLHHD CNPRIIHRDV
KSKNILLDKD YEAHLADFGI AKSLCTSKTH TSTYVMGTIG YIDPEYACTS RLNEKSDVYS
YGIVLLELLT GKKPVDNECN LHHLILSKAA DNTVMEMVDP DIADTCKDLG EVKKVFQLAL
LCSKRQPSDR PTMHEVVRVL DCLVYPDPPS KPALPPALPQ SSTVPSYVNE YVSLRGGSTL
SCENSSSASD AELFLKFGEV ISQNTE
