ETR1_ARATH
ID ETR1_ARATH Reviewed; 738 AA.
AC P49333;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Ethylene receptor 1 {ECO:0000303|PubMed:8211181};
DE Short=AtETR1 {ECO:0000303|PubMed:8211181};
DE EC=2.7.13.3 {ECO:0000305};
DE AltName: Full=Protein ETHYLENE RESPONSE 1 {ECO:0000303|PubMed:8211181};
DE AltName: Full=Protein ETR1 {ECO:0000303|PubMed:8211181};
GN Name=ETR1 {ECO:0000303|PubMed:8211181};
GN OrderedLocusNames=At1g66340 {ECO:0000312|Araport:AT1G66340};
GN ORFNames=T27F4.9 {ECO:0000312|EMBL:AAG52169.1};
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], AND MUTANTS ETR1-1; ETR1-2; ETR1-3 AND
RP ETR1-4.
RX PubMed=8211181; DOI=10.1126/science.8211181;
RA Chang C., Kwok S.F., Bleecker A.B., Meyerowitz E.M.;
RT "Arabidopsis ethylene-response gene ETR1: similarity of product to two-
RT component regulators.";
RL Science 262:539-544(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 DISULFIDE BONDS, AND MUTAGENESIS OF CYS-4; CYS-6 AND CYS-99.
RX PubMed=7759498; DOI=10.1074/jbc.270.21.12526;
RA Schaller G.E., Ladd A.N., Lanahan M.B., Spanbauer J.M., Bleecker A.B.;
RT "The ethylene response mediator ETR1 from Arabidopsis forms a disulfide-
RT linked dimer.";
RL J. Biol. Chem. 270:12526-12530(1995).
RN [5]
RP MUTAGENESIS OF CYS-4; CYS-6; CYS-65 AND CYS-99.
RX PubMed=8525372; DOI=10.1126/science.270.5243.1809;
RA Schaller G.E., Bleecker A.B.;
RT "Ethylene-binding sites generated in yeast expressing the Arabidopsis ETR1
RT gene.";
RL Science 270:1809-1811(1995).
RN [6]
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 [7]
RP COFACTOR, AND MUTAGENESIS OF GLU-38; CYS-65; HIS-69; HIS-79; MET-87;
RP MET-104 AND HIS-107.
RX PubMed=9974395; DOI=10.1126/science.283.5404.996;
RA Rodriguez F.I., Esch J.J., Hall A.E., Binder B.M., Schaller G.E.,
RA Bleecker A.B.;
RT "A copper cofactor for the ethylene receptor ETR1 from Arabidopsis.";
RL Science 283:996-998(1999).
RN [8]
RP INTERACTION WITH AHP1; AHP2 AND AHP3.
RX PubMed=10930573; DOI=10.1016/s0014-5793(00)01860-3;
RA Urao T., Miyata S., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Possible His to Asp phosphorelay signaling in an Arabidopsis two-component
RT system.";
RL FEBS Lett. 478:227-232(2000).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11916973; DOI=10.1074/jbc.m201286200;
RA Chen Y.-F., Randlett M.D., Findell J.L., Schaller G.E.;
RT "Localization of the ethylene receptor ETR1 to the endoplasmic reticulum of
RT Arabidopsis.";
RL J. Biol. Chem. 277:19861-19866(2002).
RN [10]
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 [11]
RP FUNCTION.
RX PubMed=15466228; DOI=10.1104/pp.104.047126;
RA Qu X., Schaller G.E.;
RT "Requirement of the histidine kinase domain for signal transduction by the
RT ethylene receptor ETR1.";
RL Plant Physiol. 136:2961-2970(2004).
RN [12]
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 [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=17224067; DOI=10.1186/1471-2229-7-3;
RA Qu X., Hall B.P., Gao Z., Schaller G.E.;
RT "A strong constitutive ethylene-response phenotype conferred on Arabidopsis
RT plants containing null mutations in the ethylene receptors ETR1 and ERS1.";
RL BMC Plant Biol. 7:3-3(2007).
RN [14]
RP INTERACTION WITH ERS1; ERS2; ETR2 AND EIN4.
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 [15]
RP INTERACTION WITH EIN2, AND SUBCELLULAR LOCATION.
RX PubMed=19769567; DOI=10.1042/bj20091102;
RA Bisson M.M., Bleckmann A., Allekotte S., Groth G.;
RT "EIN2, the central regulator of ethylene signalling, is localized at the ER
RT membrane where it interacts with the ethylene receptor ETR1.";
RL Biochem. J. 424:1-6(2009).
RN [16]
RP INTERACTION WITH RTE1.
RX PubMed=20952388; DOI=10.1074/jbc.m110.146605;
RA Dong C.H., Jang M., Scharein B., Malach A., Rivarola M., Liesch J.,
RA Groth G., Hwang I., Chang C.;
RT "Molecular association of the Arabidopsis ETR1 ethylene receptor and a
RT regulator of ethylene signaling, RTE1.";
RL J. Biol. Chem. 285:40706-40713(2010).
RN [17]
RP FUNCTION, PHOSPHORYLATION AT HIS-353, AND MUTAGENESIS OF HIS-353.
RX PubMed=20591837; DOI=10.1093/mp/ssq036;
RA Bisson M.M., Groth G.;
RT "New insight in ethylene signaling: autokinase activity of ETR1 modulates
RT the interaction of receptors and EIN2.";
RL Mol. Plant 3:882-889(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 603-738.
RX PubMed=10647185; DOI=10.1016/s0969-2126(00)88345-8;
RA Mueller-Dieckmann H.-J., Grantz A.A., Kim S.-H.;
RT "The structure of the signal receiver domain of the Arabidopsis thaliana
RT ethylene receptor ETR1.";
RL Structure 7:1547-1556(1999).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 407-589 IN COMPLEX WITH ADP.
RX PubMed=25451923; DOI=10.1074/jbc.m114.587667;
RA Mayerhofer H., Panneerselvam S., Kaljunen H., Tuukkanen A., Mertens H.D.,
RA Mueller-Dieckmann J.;
RT "Structural model of the cytosolic domain of the plant ethylene receptor 1
RT (ETR1).";
RL J. Biol. Chem. 290:2644-2658(2015).
CC -!- FUNCTION: Ethylene receptor related to bacterial two-component
CC regulators. Acts as a redundant negative regulator of ethylene
CC signaling (PubMed:15466228, PubMed:15703053). In the presence of
CC ethylene, the auto-kinase activity of ETR1 is inhibited and the non-
CC phosphorylated kinase domain binds tightly to the corresponding domain
CC of EIN2 (PubMed:20591837). {ECO:0000269|PubMed:15466228,
CC ECO:0000269|PubMed:15703053, ECO:0000269|PubMed:20591837}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:9974395};
CC Note=Binds 1 copper ion per dimer. {ECO:0000269|PubMed:9974395};
CC -!- SUBUNIT: Homodimer; disulfide-linked. Heteromer with ERS1, ERS2, ETR2
CC and EIN4. Interacts with AHP1, AHP2 and AHP3. Interacts with RTE1
CC (PubMed:10930573, PubMed:18577522, PubMed:20952388, PubMed:7759498).
CC Interacts with EIN2 (PubMed:19769567). {ECO:0000269|PubMed:10930573,
CC ECO:0000269|PubMed:18577522, ECO:0000269|PubMed:19769567,
CC ECO:0000269|PubMed:20952388, ECO:0000269|PubMed:7759498}.
CC -!- INTERACTION:
CC P49333; Q9ZNV9: AHP1; NbExp=3; IntAct=EBI-1606682, EBI-1100673;
CC P49333; Q05609: CTR1; NbExp=6; IntAct=EBI-1606682, EBI-1606697;
CC P49333; Q9S814: EIN2; NbExp=2; IntAct=EBI-1606682, EBI-2437287;
CC P49333; P93825: ERS2; NbExp=2; IntAct=EBI-1606682, EBI-1787556;
CC P49333; P49333: ETR1; NbExp=2; IntAct=EBI-1606682, EBI-1606682;
CC P49333; Q0WPQ2: ETR2; NbExp=2; IntAct=EBI-1606682, EBI-1787533;
CC P49333; F4ITL6: RTE1; NbExp=5; IntAct=EBI-1606682, EBI-2437263;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11916973, ECO:0000269|PubMed:19769567}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Leaves, roots, stems, seedlings, flowers, anthers,
CC carpels and ovules. {ECO:0000269|PubMed:9707532}.
CC -!- DOMAIN: The GAF domain is sufficient to mediate heteromerization.
CC -!- PTM: Autophosphorylated. Phosphorylation at His-353 modulates the
CC interaction with EIN2. {ECO:0000269|PubMed:20591837}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in ethylene response; due to
CC redundancy with ERS1. Ers1 and etr1 double mutants display a
CC constitutive ethylene-response phenotype.
CC {ECO:0000269|PubMed:17224067}.
CC -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
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DR EMBL; L24119; AAA70047.1; -; Genomic_DNA.
DR EMBL; AC020665; AAG52169.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34497.1; -; Genomic_DNA.
DR PIR; A48246; A48246.
DR RefSeq; NP_176808.3; NM_105305.4.
DR PDB; 1DCF; X-ray; 2.50 A; A=605-738.
DR PDB; 4PL9; X-ray; 1.90 A; A=407-589.
DR PDBsum; 1DCF; -.
DR PDBsum; 4PL9; -.
DR AlphaFoldDB; P49333; -.
DR BMRB; P49333; -.
DR SASBDB; P49333; -.
DR SMR; P49333; -.
DR BioGRID; 28172; 47.
DR IntAct; P49333; 39.
DR STRING; 3702.AT1G66340.1; -.
DR iPTMnet; P49333; -.
DR PaxDb; P49333; -.
DR PRIDE; P49333; -.
DR ProteomicsDB; 222329; -.
DR EnsemblPlants; AT1G66340.1; AT1G66340.1; AT1G66340.
DR GeneID; 842951; -.
DR Gramene; AT1G66340.1; AT1G66340.1; AT1G66340.
DR KEGG; ath:AT1G66340; -.
DR Araport; AT1G66340; -.
DR TAIR; locus:2201552; AT1G66340.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_114_48_1; -.
DR InParanoid; P49333; -.
DR OMA; NEYRFKR; -.
DR OrthoDB; 199912at2759; -.
DR PhylomeDB; P49333; -.
DR BRENDA; 2.7.13.3; 399.
DR EvolutionaryTrace; P49333; -.
DR PRO; PR:P49333; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P49333; baseline and differential.
DR Genevisible; P49333; 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; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0004673; F:protein histidine kinase activity; IMP:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0009690; P:cytokinin metabolic process; IMP:TAIR.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009727; P:detection of ethylene stimulus; IMP:TAIR.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:TAIR.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; TAS:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:1900140; P:regulation of seedling development; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0009625; P:response to insect; IMP:TAIR.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0010162; P:seed dormancy process; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated 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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF026389; Ethyln_sen_HK; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 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 3D-structure; 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; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system; Ubl conjugation.
FT CHAIN 1..738
FT /note="Ethylene receptor 1"
FT /id="PRO_0000081412"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 158..307
FT /note="GAF"
FT DOMAIN 350..585
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 611..729
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 65
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 470..473
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007744|PDB:4PL9"
FT BINDING 513
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007744|PDB:4PL9"
FT BINDING 529
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007744|PDB:4PL9"
FT BINDING 544
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007744|PDB:4PL9"
FT BINDING 548
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007744|PDB:4PL9"
FT MOD_RES 353
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20591837"
FT MOD_RES 659
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DISULFID 4
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:7759498"
FT DISULFID 6
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:7759498"
FT CROSSLNK 714
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q0WPQ2"
FT MUTAGEN 4
FT /note="C->S: Prevents dimerization but not ethylene
FT binding."
FT /evidence="ECO:0000269|PubMed:7759498,
FT ECO:0000269|PubMed:8525372"
FT MUTAGEN 6
FT /note="C->S: Prevents dimerization but not ethylene
FT binding."
FT /evidence="ECO:0000269|PubMed:7759498,
FT ECO:0000269|PubMed:8525372"
FT MUTAGEN 31
FT /note="A->V: In etr1-3; ethylene insensitivity."
FT MUTAGEN 38
FT /note="E->A: No effect on ethylene binding."
FT /evidence="ECO:0000269|PubMed:9974395"
FT MUTAGEN 62
FT /note="I->F: In etr1-4; ethylene insensitivity."
FT MUTAGEN 65
FT /note="C->Y,S: In etr1-1; no copper binding and ethylene
FT insensitivity."
FT /evidence="ECO:0000269|PubMed:8525372,
FT ECO:0000269|PubMed:9974395"
FT MUTAGEN 69
FT /note="H->A: No copper binding and ethylene insensitivity."
FT /evidence="ECO:0000269|PubMed:9974395"
FT MUTAGEN 79
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9974395"
FT MUTAGEN 87
FT /note="M->A: No effect on ethylene binding."
FT /evidence="ECO:0000269|PubMed:9974395"
FT MUTAGEN 99
FT /note="C->S: No effect on dimerization or ethylene
FT binding."
FT /evidence="ECO:0000269|PubMed:7759498,
FT ECO:0000269|PubMed:8525372"
FT MUTAGEN 102
FT /note="A->T: In etr1-2; ethylene insensitivity."
FT MUTAGEN 104
FT /note="M->A: No effect on ethylene binding."
FT /evidence="ECO:0000269|PubMed:9974395"
FT MUTAGEN 107
FT /note="H->A: No effect on ethylene binding."
FT /evidence="ECO:0000269|PubMed:9974395"
FT MUTAGEN 353
FT /note="H->A: Loss of phosphorylation and increased affinity
FT toward EIN2."
FT /evidence="ECO:0000269|PubMed:20591837"
FT MUTAGEN 353
FT /note="H->E: Reduced affinity toward EIN2."
FT /evidence="ECO:0000269|PubMed:20591837"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:4PL9"
FT HELIX 419..437
FT /evidence="ECO:0007829|PDB:4PL9"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:4PL9"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:4PL9"
FT HELIX 457..474
FT /evidence="ECO:0007829|PDB:4PL9"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:4PL9"
FT STRAND 480..487
FT /evidence="ECO:0007829|PDB:4PL9"
FT STRAND 504..512
FT /evidence="ECO:0007829|PDB:4PL9"
FT HELIX 520..525
FT /evidence="ECO:0007829|PDB:4PL9"
FT HELIX 547..557
FT /evidence="ECO:0007829|PDB:4PL9"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:4PL9"
FT STRAND 574..583
FT /evidence="ECO:0007829|PDB:4PL9"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:1DCF"
FT HELIX 619..631
FT /evidence="ECO:0007829|PDB:1DCF"
FT STRAND 635..641
FT /evidence="ECO:0007829|PDB:1DCF"
FT HELIX 642..648
FT /evidence="ECO:0007829|PDB:1DCF"
FT STRAND 654..659
FT /evidence="ECO:0007829|PDB:1DCF"
FT TURN 664..668
FT /evidence="ECO:0007829|PDB:1DCF"
FT HELIX 669..678
FT /evidence="ECO:0007829|PDB:1DCF"
FT STRAND 687..693
FT /evidence="ECO:0007829|PDB:1DCF"
FT HELIX 697..705
FT /evidence="ECO:0007829|PDB:1DCF"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:1DCF"
FT HELIX 718..729
FT /evidence="ECO:0007829|PDB:1DCF"
SQ SEQUENCE 738 AA; 82566 MW; D6ED3C4BBA87E96E CRC64;
MEVCNCIEPQ WPADELLMKY QYISDFFIAI AYFSIPLELI YFVKKSAVFP YRWVLVQFGA
FIVLCGATHL INLWTFTTHS RTVALVMTTA KVLTAVVSCA TALMLVHIIP DLLSVKTREL
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLALEECA
LWMPTRTGLE LQLSYTLRHQ HPVEYTVPIQ LPVINQVFGT SRAVKISPNS PVARLRPVSG
KYMLGEVVAV RVPLLHLSNF QINDWPELST KRYALMVLML PSDSARQWHV HELELVEVVA
DQVAVALSHA AILEESMRAR DLLMEQNVAL DLARREAETA IRARNDFLAV MNHEMRTPMH
AIIALSSLLQ ETELTPEQRL MVETILKSSN LLATLMNDVL DLSRLEDGSL QLELGTFNLH
TLFREVLNLI KPIAVVKKLP ITLNLAPDLP EFVVGDEKRL MQIILNIVGN AVKFSKQGSI
SVTALVTKSD TRAADFFVVP TGSHFYLRVK VKDSGAGINP QDIPKIFTKF AQTQSLATRS
SGGSGLGLAI SKRFVNLMEG NIWIESDGLG KGCTAIFDVK LGISERSNES KQSGIPKVPA
IPRHSNFTGL KVLVMDENGV SRMVTKGLLV HLGCEVTTVS SNEECLRVVS HEHKVVFMDV
CMPGVENYQI ALRIHEKFTK QRHQRPLLVA LSGNTDKSTK EKCMSFGLDG VLLKPVSLDN
IRDVLSDLLE PRVLYEGM
