ERS1_ARATH
ID ERS1_ARATH Reviewed; 613 AA.
AC Q38846;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ethylene response sensor 1;
DE Short=AtERS1;
DE EC=2.7.11.-;
DE EC=2.7.13.3;
DE AltName: Full=Protein ERS1;
GN Name=ERS1; Synonyms=ERS; OrderedLocusNames=At2g40940; ORFNames=T20B5.14;
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].
RC STRAIN=cv. Columbia;
RX PubMed=7569898; DOI=10.1126/science.7569898;
RA Hua J., Chang C., Sun Q., Meyerowitz E.M.;
RT "Ethylene insensitivity conferred by Arabidopsis ERS gene.";
RL Science 269:1712-1714(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY ETHYLENE.
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 DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
RX PubMed=10938361; DOI=10.1104/pp.123.4.1449;
RA Hall A.E., Findell J.L., Schaller G.E., Sisler E.C., Bleecker A.B.;
RT "Ethylene perception by the ERS1 protein in Arabidopsis.";
RL Plant Physiol. 123:1449-1458(2000).
RN [7]
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 [8]
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 [9]
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).
CC -!- FUNCTION: Ethylene receptor related to bacterial two-component
CC regulators. Acts as a redundant negative regulator of ethylene
CC signaling.
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; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per dimer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer; disulfide-linked. Heteromer with ETR1.
CC {ECO:0000269|PubMed:10938361}.
CC -!- INTERACTION:
CC Q38846; Q05609: CTR1; NbExp=2; IntAct=EBI-1606754, EBI-1606697;
CC Q38846; Q8L7L8: TRP1; NbExp=2; IntAct=EBI-1606754, EBI-476071;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:10938361}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:10938361}.
CC -!- TISSUE SPECIFICITY: Expressed in etiolated seedlings, leaves, stems,
CC roots, flowers, embryos, anthers, carpels and ovules.
CC {ECO:0000269|PubMed:9707532}.
CC -!- INDUCTION: By ethylene. {ECO:0000269|PubMed:18577522,
CC ECO:0000269|PubMed:9707532}.
CC -!- PTM: Autophosphorylated on both His and Ser residues in the presence of
CC manganese. Loss of His autophosphorylation in the presence of both
CC manganese and magnesium. {ECO:0000269|PubMed:15358768}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in ethylene response; due to
CC the redundancy with ETR1. 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; U21952; AAC49090.1; -; Genomic_DNA.
DR EMBL; AC002409; AAB86454.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09904.1; -; Genomic_DNA.
DR EMBL; AY054532; AAK96723.1; -; mRNA.
DR EMBL; BT000159; AAN15478.1; -; mRNA.
DR PIR; T00758; T00758.
DR RefSeq; NP_181626.1; NM_129658.4.
DR PDB; 4MT8; X-ray; 1.90 A; A/B=308-407.
DR PDB; 4MTX; X-ray; 2.15 A; A/B/C/D=308-407.
DR PDBsum; 4MT8; -.
DR PDBsum; 4MTX; -.
DR AlphaFoldDB; Q38846; -.
DR SMR; Q38846; -.
DR BioGRID; 4030; 6.
DR IntAct; Q38846; 5.
DR STRING; 3702.AT2G40940.1; -.
DR PaxDb; Q38846; -.
DR PRIDE; Q38846; -.
DR ProteomicsDB; 220703; -.
DR EnsemblPlants; AT2G40940.1; AT2G40940.1; AT2G40940.
DR GeneID; 818693; -.
DR Gramene; AT2G40940.1; AT2G40940.1; AT2G40940.
DR KEGG; ath:AT2G40940; -.
DR Araport; AT2G40940; -.
DR TAIR; locus:2058500; AT2G40940.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_114_48_1; -.
DR InParanoid; Q38846; -.
DR OMA; RQEAHRY; -.
DR OrthoDB; 199912at2759; -.
DR PhylomeDB; Q38846; -.
DR PRO; PR:Q38846; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38846; baseline and differential.
DR Genevisible; Q38846; 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; IBA:GO_Central.
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; TAS:TAIR.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; 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 Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Copper; Disulfide bond; Endoplasmic reticulum;
KW Ethylene signaling pathway; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..613
FT /note="Ethylene response sensor 1"
FT /id="PRO_0000378142"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 158..307
FT /note="GAF"
FT DOMAIN 350..589
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 65
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT MOD_RES 353
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P49333,
FT ECO:0000255|PROSITE-ProRule:PRU00107"
FT DISULFID 4
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 6
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT HELIX 309..370
FT /evidence="ECO:0007829|PDB:4MT8"
FT HELIX 376..403
FT /evidence="ECO:0007829|PDB:4MT8"
SQ SEQUENCE 613 AA; 68333 MW; E4F5DB384E6727B2 CRC64;
MESCDCFETH VNQDDLLVKY QYISDALIAL AYFSIPLELI YFVQKSAFFP YKWVLMQFGA
FIILCGATHF INLWMFFMHS KAVAIVMTIA KVSCAVVSCA TALMLVHIIP DLLSVKNREL
FLKKKADELD REMGLILTQE ETGRHVRMLT HGIRRTLDRH TILRTTLVEL GKTLCLEECA
LWMPSQSGLY LQLSHTLSHK IQVGSSVPIN LPIINELFNS AQAMHIPHSC PLAKIGPPVG
RYSPPEVVSV RVPLLHLSNF QGSDWSDLSG KGYAIMVLIL PTDGARKWRD HELELVENVA
DQVAVALSHA AILEESMHAR DQLMEQNFAL DKARQEAEMA VHARNDFLAV MNHEMRTPMH
AIISLSSLLL ETELSPEQRV MIETILKSSN LVATLISDVL DLSRLEDGSL LLENEPFSLQ
AIFEEVISLI KPIASVKKLS TNLILSADLP TYAIGDEKRL MQTILNIMGN AVKFTKEGYI
SIIASIMKPE SLQELPSPEF FPVLSDSHFY LCVQVKDTGC GIHTQDIPLL FTKFVQPRTG
TQRNHSGGGL GLALCKRFVG LMGGYMWIES EGLEKGCTAS FIIRLGICNG PSSSSGSMAL
HLAAKSQTRP WNW
