ETR2_ARATH
ID ETR2_ARATH Reviewed; 773 AA.
AC Q0WPQ2; O82429; Q9LTD5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ethylene receptor 2 {ECO:0000303|PubMed:9576967};
DE Short=AtETR2 {ECO:0000303|PubMed:9576967};
DE EC=2.7.11.-;
DE AltName: Full=Protein ETHYLENE RESPONSE 2 {ECO:0000303|PubMed:9576967};
DE AltName: Full=Protein ETR2 {ECO:0000303|PubMed:9576967};
GN Name=ETR2 {ECO:0000303|PubMed:9576967};
GN OrderedLocusNames=At3g23150 {ECO:0000312|Araport:AT3G23150};
GN ORFNames=K14B15.9 {ECO:0000312|EMBL:BAA95726.1};
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 [GENOMIC DNA], MUTAGENESIS OF PRO-66, INDUCTION BY
RP ETHYLENE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9576967; DOI=10.1073/pnas.95.10.5812;
RA Sakai H., Hua J., Chen Q.G., Chang C., Medrano L.J., Bleecker A.B.,
RA Meyerowitz E.M.;
RT "ETR2 is an ETR1-like gene involved in ethylene signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:5812-5817(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9707532; DOI=10.2307/3870643;
RA Hua J., Sakai H., Nourizadeh S., Chen Q.G., Bleecker A.B., Ecker J.R.,
RA Meyerowitz E.M.;
RT "EIN4 and ERS2 are members of the putative ethylene receptor gene family in
RT Arabidopsis.";
RL Plant Cell 10:1321-1332(1998).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=15358768; DOI=10.1074/jbc.m403100200;
RA Moussatche P., Klee H.J.;
RT "Autophosphorylation activity of the Arabidopsis ethylene receptor
RT multigene family.";
RL J. Biol. Chem. 279:48734-48741(2004).
RN [7]
RP FUNCTION.
RX PubMed=15703053; DOI=10.1111/j.1365-313x.2004.02331.x;
RA O'Malley R.C., Rodriguez F.I., Esch J.J., Binder B.M., O'Donnell P.,
RA Klee H.J., Bleecker A.B.;
RT "Ethylene-binding activity, gene expression levels, and receptor system
RT output for ethylene receptor family members from Arabidopsis and tomato.";
RL Plant J. 41:651-659(2005).
RN [8]
RP INDUCTION BY ETHYLENE, SUBCELLULAR LOCATION, AND DEGRADATION.
RX PubMed=17595158; DOI=10.1074/jbc.m704419200;
RA Chen Y.-F., Shakeel S.N., Bowers J., Zhao X.-C., Etheridge N.,
RA Schaller G.E.;
RT "Ligand-induced degradation of the ethylene receptor ETR2 through a
RT proteasome-dependent pathway in Arabidopsis.";
RL J. Biol. Chem. 282:24752-24758(2007).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-751, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [10]
RP INTERACTION WITH ETR1, AND INDUCTION BY ETHYLENE.
RX PubMed=18577522; DOI=10.1074/jbc.m800641200;
RA Gao Z., Wen C.-K., Binder B.M., Chen Y.-F., Chang J., Chiang Y.-H.,
RA Kerris R.J. III, Chang C., Schaller G.E.;
RT "Heteromeric interactions among ethylene receptors mediate signaling in
RT Arabidopsis.";
RL J. Biol. Chem. 283:23801-23810(2008).
RN [11]
RP INTERACTION WITH MRF3/ECIP1.
RC STRAIN=cv. Columbia;
RX PubMed=21631530; DOI=10.1111/j.1365-3040.2011.02363.x;
RA Lei G., Shen M., Li Z.G., Zhang B., Duan K.X., Wang N., Cao Y.R.,
RA Zhang W.K., Ma B., Ling H.Q., Chen S.Y., Zhang J.S.;
RT "EIN2 regulates salt stress response and interacts with a MA3 domain-
RT containing protein ECIP1 in Arabidopsis.";
RL Plant Cell Environ. 34:1678-1692(2011).
RN [12]
RP RETRACTED PAPER.
RX PubMed=26207341; DOI=10.1038/srep12477;
RA Li Z.G., Chen H.W., Li Q.T., Tao J.J., Bian X.H., Ma B., Zhang W.K.,
RA Chen S.Y., Zhang J.S.;
RT "Three SAUR proteins SAUR76, SAUR77 and SAUR78 promote plant growth in
RT Arabidopsis.";
RL Sci. Rep. 5:12477-12477(2015).
RN [13]
RP RETRACTION NOTICE OF PUBMED:26207341.
RX PubMed=35105927; DOI=10.1038/s41598-022-06178-8;
RA Li Z.G., Chen H.W., Li Q.T., Tao J.J., Bian X.H., Ma B., Zhang W.K.,
RA Chen S.Y., Zhang J.S.;
RL Sci. Rep. 12:1994-1994(2022).
CC -!- FUNCTION: Ethylene receptor related to bacterial two-component
CC regulators. Acts as a redundant negative regulator of ethylene
CC signaling. {ECO:0000269|PubMed:15703053}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per dimer. {ECO:0000250};
CC -!- SUBUNIT: Heteromer with ETR1 (PubMed:18577522). Binds to MRF3/ECIP1
CC (PubMed:21631530). {ECO:0000269|PubMed:18577522,
CC ECO:0000269|PubMed:21631530}.
CC -!- INTERACTION:
CC Q0WPQ2; Q05609: CTR1; NbExp=2; IntAct=EBI-1787533, EBI-1606697;
CC Q0WPQ2; P49333: ETR1; NbExp=2; IntAct=EBI-1787533, EBI-1606682;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17595158}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17595158}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, flowers,
CC mature siliques, shoot apical meristems, leaf primordia, inflorescence
CC meristems, young floral meristems, developing petals, carpels and
CC ovules. Low expression in stamens. {ECO:0000269|PubMed:9576967,
CC ECO:0000269|PubMed:9707532}.
CC -!- INDUCTION: By ethylene. {ECO:0000269|PubMed:17595158,
CC ECO:0000269|PubMed:18577522, ECO:0000269|PubMed:9576967}.
CC -!- DOMAIN: The GAF domain is sufficient to mediate heteromerization.
CC -!- PTM: Autophosphorylated predominantly on Ser residues.
CC {ECO:0000269|PubMed:15358768}.
CC -!- MISCELLANEOUS: ETR2 is degraded by a proteasome-dependent pathway in
CC response to ethylene binding.
CC -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
CC -!- CAUTION: The article by Li et al was retracted by the editors after
CC publication. Concerns were raised regarding a number of figure panels,
CC such as partial overlap between the panels and duplication of protein
CC gel analysis. {ECO:0000305|PubMed:35105927}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95726.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF047975; AAC62208.1; -; Genomic_DNA.
DR EMBL; AB025608; BAA95726.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76724.1; -; Genomic_DNA.
DR EMBL; AK229010; BAF00897.1; -; mRNA.
DR RefSeq; NP_001326955.1; NM_001338618.1.
DR RefSeq; NP_188956.1; NM_113216.3.
DR AlphaFoldDB; Q0WPQ2; -.
DR SMR; Q0WPQ2; -.
DR BioGRID; 7223; 30.
DR IntAct; Q0WPQ2; 14.
DR STRING; 3702.AT3G23150.1; -.
DR iPTMnet; Q0WPQ2; -.
DR PaxDb; Q0WPQ2; -.
DR PRIDE; Q0WPQ2; -.
DR ProteomicsDB; 222327; -.
DR EnsemblPlants; AT3G23150.1; AT3G23150.1; AT3G23150.
DR GeneID; 821891; -.
DR Gramene; AT3G23150.1; AT3G23150.1; AT3G23150.
DR KEGG; ath:AT3G23150; -.
DR Araport; AT3G23150; -.
DR TAIR; locus:2086208; AT3G23150.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_114_48_1; -.
DR InParanoid; Q0WPQ2; -.
DR OMA; YCAVWMP; -.
DR OrthoDB; 253193at2759; -.
DR PRO; PR:Q0WPQ2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WPQ2; baseline and differential.
DR Genevisible; Q0WPQ2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0038199; F:ethylene receptor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; TAS:TAIR.
DR CDD; cd00082; HisKA; 1.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
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; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 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; Isopeptide bond; Kinase; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system;
KW Ubl conjugation.
FT CHAIN 1..773
FT /note="Ethylene receptor 2"
FT /id="PRO_0000378141"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 187..331
FT /note="GAF"
FT DOMAIN 374..614
FT /note="Histidine kinase"
FT DOMAIN 647..766
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 94
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT MOD_RES 702
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DISULFID 32
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CROSSLNK 751
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT MUTAGEN 66
FT /note="P->L: In etr2-1; ehtylene insensitivity."
FT /evidence="ECO:0000269|PubMed:9576967"
FT CONFLICT 488
FT /note="I -> M (in Ref. 1; AAC62208)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="N -> Y (in Ref. 4; BAF00897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 85613 MW; 1E93F80F0CC9E9B2 CRC64;
MVKEIASWLL ILSMVVFVSP VLAINGGGYP RCNCEDEGNS FWSTENILET QRVSDFLIAV
AYFSIPIELL YFVSCSNVPF KWVLFEFIAF IVLCGMTHLL HGWTYSAHPF RLMMAFTVFK
MLTALVSCAT AITLITLIPL LLKVKVREFM LKKKAHELGR EVGLILIKKE TGFHVRMLTQ
EIRKSLDRHT ILYTTLVELS KTLGLQNCAV WMPNDGGTEM DLTHELRGRG GYGGCSVSME
DLDVVRIRES DEVNVLSVDS SIARASGGGG DVSEIGAVAA IRMPMLRVSD FNGELSYAIL
VCVLPGGTPR DWTYQEIEIV KVVADQVTVA LDHAAVLEES QLMREKLAEQ NRALQMAKRD
ALRASQARNA FQKTMSEGMR RPMHSILGLL SMIQDEKLSD EQKMIVDTMV KTGNVMSNLV
GDSMDVPDGR FGTEMKPFSL HRTIHEAACM ARCLCLCNGI RFLVDAEKSL PDNVVGDERR
VFQVILHIVG SLVKPRKRQE GSSLMFKVLK ERGSLDRSDH RWAAWRSPAS SADGDVYIRF
EMNVENDDSS SQSFASVSSR DQEVGDVRFS GGYGLGQDLS FGVCKKVVQL IHGNISVVPG
SDGSPETMSL LLRFRRRPSI SVHGSSESPA PDHHAHPHSN SLLRGLQVLL VDTNDSNRAV
TRKLLEKLGC DVTAVSSGFD CLTAIAPGSS SPSTSFQVVV LDLQMAEMDG YEVAMRIRSR
SWPLIVATTV SLDEEMWDKC AQIGINGVVR KPVVLRAMES ELRRVLLQAD QLL
