ETR2_ORYSJ
ID ETR2_ORYSJ Reviewed; 763 AA.
AC Q7XX84; A0A0P0W6W4; Q0JF30; Q5H9Y0; Q944U0;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ethylene receptor 2 {ECO:0000305};
DE Short=OsETR2 {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000305};
DE AltName: Full=OsPK1 {ECO:0000312|EMBL:AAL29304.2};
GN Name=ETR2 {ECO:0000303|PubMed:19417056};
GN OrderedLocusNames=Os04g0169100 {ECO:0000312|EMBL:BAF14057.1},
GN LOC_Os04g08740 {ECO:0000305};
GN ORFNames=P0650D04.3 {ECO:0000312|EMBL:CAI44599.1},
GN SJNBb0089K06.20 {ECO:0000312|EMBL:CAD39679.1};
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], FUNCTION, PHOSPHORYLATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLY-487; GLU-489; ARG-491; PHE-493 AND
RP GLY-501.
RC STRAIN=cv. Lansheng;
RX PubMed=19417056; DOI=10.1105/tpc.108.065391;
RA Wuriyanghan H., Zhang B., Cao W.H., Ma B., Lei G., Liu Y.F., Wei W.,
RA Wu H.J., Chen L.J., Chen H.W., Cao Y.R., He S.J., Zhang W.K., Wang X.J.,
RA Chen S.Y., Zhang J.S.;
RT "The ethylene receptor ETR2 delays floral transition and affects starch
RT accumulation in rice.";
RL Plant Cell 21:1473-1494(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP INDUCTION BY WATER DEFICIENCY.
RX PubMed=16169685; DOI=10.1016/j.gene.2005.07.017;
RA Lin T., He X.W., Yang L., Shou H.X., Wu P.;
RT "Identification and characterization of a novel water-deficit-suppressed
RT gene OsARD encoding an aci-reductone-dioxygenase-like protein in rice.";
RL Gene 360:27-34(2005).
CC -!- FUNCTION: Ethylene receptor related to bacterial two-component
CC regulators. Acts as negative regulator of ethylene signaling. May delay
CC the transition from the vegetative stage to the floral stage by up-
CC regulating GI (GIGANTEA) and RCN1 and cause starch accumulation in
CC stems by down-regulating the alpha-amylase AMY3D.
CC {ECO:0000269|PubMed:19417056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P49333};
CC Note=Binds 1 copper ion per dimer. {ECO:0000250|UniProtKB:P49333};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P49333}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by water deficiency. {ECO:0000269|PubMed:16169685}.
CC -!- PTM: Autophosphorylated on serine, threonine and tyrosine residues.
CC {ECO:0000269|PubMed:19417056}.
CC -!- DISRUPTION PHENOTYPE: Enhanced ethylene sensitivity and early
CC flowering. {ECO:0000269|PubMed:19417056}.
CC -!- MISCELLANEOUS: Plants over-expressing ETR2 display reduced ethylene
CC sensitivity, delayed floral transition and reduced seed set.
CC {ECO:0000269|PubMed:19417056}.
CC -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF14057.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF420319; AAL29304.2; -; mRNA.
DR EMBL; AL663013; CAD39679.1; -; Genomic_DNA.
DR EMBL; CR933497; CAI44599.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF14057.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS87896.1; -; Genomic_DNA.
DR EMBL; AK111748; BAG99395.1; -; mRNA.
DR RefSeq; XP_015636406.1; XM_015780920.1.
DR AlphaFoldDB; Q7XX84; -.
DR STRING; 4530.OS04T0169100-02; -.
DR PaxDb; Q7XX84; -.
DR PRIDE; Q7XX84; -.
DR EnsemblPlants; Os04t0169100-02; Os04t0169100-02; Os04g0169100.
DR GeneID; 4335058; -.
DR Gramene; Os04t0169100-02; Os04t0169100-02; Os04g0169100.
DR KEGG; osa:4335058; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_114_48_1; -.
DR InParanoid; Q7XX84; -.
DR OMA; LNAWTYY; -.
DR OrthoDB; 253193at2759; -.
DR PlantReactome; R-OSA-5225756; Ethylene mediated signaling.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q7XX84; baseline and differential.
DR Genevisible; Q7XX84; OS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051740; F:ethylene binding; IEA:InterPro.
DR GO; GO:0038199; F:ethylene receptor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:CACAO.
DR GO; GO:2000904; P:regulation of starch metabolic process; IMP:CACAO.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0009723; P:response to ethylene; IMP:CACAO.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR014525; ETR.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF026389; Ethyln_sen_HK; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Copper; Disulfide bond; Endoplasmic reticulum;
KW Ethylene signaling pathway; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..763
FT /note="Ethylene receptor 2"
FT /id="PRO_0000433865"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 190..339
FT /note="GAF"
FT /evidence="ECO:0000305"
FT DOMAIN 382..615
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 641..760
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 97
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT BINDING 101
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT MOD_RES 692
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DISULFID 31
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT MUTAGEN 487
FT /note="G->A: Loss of kinase activity; when associated with
FT Q-489, Q-491, A-493 and A-501."
FT /evidence="ECO:0000269|PubMed:19417056"
FT MUTAGEN 489
FT /note="E->Q: Loss of kinase activity; when associated with
FT A-487, Q-491, A-493 and A-501."
FT /evidence="ECO:0000269|PubMed:19417056"
FT MUTAGEN 491
FT /note="R->Q: Loss of kinase activity; when associated with
FT A-487, Q-489, A-493 and A-501."
FT /evidence="ECO:0000269|PubMed:19417056"
FT MUTAGEN 493
FT /note="F->A: Loss of kinase activity; when associated with
FT A-487, Q-489, Q-491 and A-501."
FT /evidence="ECO:0000269|PubMed:19417056"
FT MUTAGEN 501
FT /note="G->A: Loss of kinase activity; when associated with
FT A-487, Q-489, Q-491 and A-493."
FT /evidence="ECO:0000269|PubMed:19417056"
FT CONFLICT 516
FT /note="V -> A (in Ref. 1; AAL29304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 763 AA; 84832 MW; 323F342696E07C1C CRC64;
MPPIPSLWIR VFFSWLLLSL PAAAAADFSH CGGCDDGDGG GGIWSTDNIL QCQRVSDFLI
AMAYFSIPLE LLYFATCSDL FPLKWIVLQF GAFIVLCGLT HLITMFTYEP HSFHVVLALT
VAKFLTALVS FATAITLLTL IPQLLRVKVR ENFLRIKARE LDREVGMMKR QEEASWHVRM
LTHEIRKSLD RHTILYTTMV ELSKTLELQN CAVWMPSESG SEMILTHQLR QMETEDSNSL
SIAMDNPDVL EIKATKDAKV LAADSALGIA SRGKLEAGPV AAIRMPMLKA SNFKGGTPEV
METSYAILVL VLPEDGSLGW GEEELEIVEV VADQVAVALS HAAVLEESQL MREKLAAQHR
DLLRAKHETT MATEARNSFQ TAMYDGMRRP MHSILGLVSM MQQENMNPEQ RLVMDAIVKT
SSVASTLMND VMQTSTVNRE YLSLVRRAFN LHSLVKEAIS VVRCLTGCKG IDFEFEVDNS
LPERVVGDEK RVFHIVLHMV GTLIQRCNAG CLSLYVNTYN EKEERHNQDW MLRRANFSGS
YVCVKFEIRI RESRGNLLSS SSSRRLQGPN STSSEMGLSF NMCKKIVQMM NGNIWSVSDS
KGLGETIMLA LQFQLQHVTP VSGASSDLFR SAPIPNFNGL QVILVDSDDT NRAVTHKLLE
KLGCLVLSVT SGIQCINSFA SAESSFQLVV LDLTMRTMDG FDVALAIRKF RGNCWPPLIV
ALAASTDDTV RDRCQQAGIN GLIQKPVTLA ALGDELYRVL QNN
