ERS2_ARATH
ID ERS2_ARATH Reviewed; 645 AA.
AC P93825; B0FVU3; B0FVU5; B0FVW8; B0FVX0; B0FVX9;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ethylene response sensor 2;
DE Short=AtERS2;
DE EC=2.7.11.-;
DE AltName: Full=Protein ERS2;
GN Name=ERS2; OrderedLocusNames=At1g04310; ORFNames=F19P19.25;
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-67 AND ILE-94,
RP INDUCTION BY ETHYLENE, AND 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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-337.
RC STRAIN=cv. Ag-0, cv. An-1, cv. Bla-10, cv. Br-0, cv. C24, cv. Chi-1,
RC cv. Co-1, cv. Columbia, cv. Ct-1, cv. Cvi-0, cv. Da(1)-12, cv. Di-G,
RC cv. Edi-0, cv. Ei-2, cv. El-0, cv. Ga-0, cv. Gr-3, cv. Gu-0, cv. Gy-0,
RC cv. Kas-1, cv. Kn-0, cv. Landsberg erecta, cv. Li-3, cv. Ll-0, cv. Mrk-0,
RC cv. Mt-0, cv. Mz-0, cv. Ove-0, cv. Oy-0, cv. PHW-1, cv. PHW-32, cv. PHW-36,
RC cv. Se-0, cv. Sha, cv. Sorbo, cv. Stw-0, cv. Ta-0, cv. Ts-5,
RC cv. Wassilewskija, and cv. Wei-0;
RX PubMed=18273534; DOI=10.1007/s00239-007-9063-3;
RA Moore R.C., Stevens M.H.H.;
RT "Local patterns of nucleotide polymorphism are highly variable in the
RT selfing species Arabidopsis thaliana.";
RL J. Mol. Evol. 66:116-129(2008).
RN [5]
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).
CC -!- FUNCTION: Ethylene receptor related to bacterial two-component
CC regulators. Acts as a redundant negative regulator of ethylene
CC signaling.
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.
CC -!- INTERACTION:
CC P93825; P93825: ERS2; NbExp=2; IntAct=EBI-1787556, EBI-1787556;
CC P93825; P49333: ETR1; NbExp=2; IntAct=EBI-1787556, EBI-1606682;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in etiolated seedlings, leaves, roots and
CC stems. Highly expressed in flowers, stamens, pollen cells, tapetum
CC cells, carpels and ovules. {ECO:0000269|PubMed:9707532}.
CC -!- INDUCTION: By ethylene. {ECO:0000269|PubMed:9707532}.
CC -!- PTM: Autophosphorylated predominantly on Ser residues.
CC {ECO:0000269|PubMed:15358768}.
CC -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
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DR EMBL; AF047976; AAC62209.1; -; Genomic_DNA.
DR EMBL; AC000104; AAB70445.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27684.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM61043.1; -; Genomic_DNA.
DR EMBL; EU351674; ABY67593.1; -; Genomic_DNA.
DR EMBL; EU351675; ABY67594.1; -; Genomic_DNA.
DR EMBL; EU351676; ABY67595.1; -; Genomic_DNA.
DR EMBL; EU351677; ABY67596.1; -; Genomic_DNA.
DR EMBL; EU351678; ABY67597.1; -; Genomic_DNA.
DR EMBL; EU351679; ABY67598.1; -; Genomic_DNA.
DR EMBL; EU351680; ABY67599.1; -; Genomic_DNA.
DR EMBL; EU351681; ABY67600.1; -; Genomic_DNA.
DR EMBL; EU351682; ABY67601.1; -; Genomic_DNA.
DR EMBL; EU351683; ABY67602.1; -; Genomic_DNA.
DR EMBL; EU351684; ABY67603.1; -; Genomic_DNA.
DR EMBL; EU351685; ABY67604.1; -; Genomic_DNA.
DR EMBL; EU351686; ABY67605.1; -; Genomic_DNA.
DR EMBL; EU351687; ABY67606.1; -; Genomic_DNA.
DR EMBL; EU351688; ABY67607.1; -; Genomic_DNA.
DR EMBL; EU351689; ABY67608.1; -; Genomic_DNA.
DR EMBL; EU351690; ABY67609.1; -; Genomic_DNA.
DR EMBL; EU351691; ABY67610.1; -; Genomic_DNA.
DR EMBL; EU351692; ABY67611.1; -; Genomic_DNA.
DR EMBL; EU351693; ABY67612.1; -; Genomic_DNA.
DR EMBL; EU351694; ABY67613.1; -; Genomic_DNA.
DR EMBL; EU351695; ABY67614.1; -; Genomic_DNA.
DR EMBL; EU351696; ABY67615.1; -; Genomic_DNA.
DR EMBL; EU351697; ABY67616.1; -; Genomic_DNA.
DR EMBL; EU351698; ABY67617.1; -; Genomic_DNA.
DR EMBL; EU351699; ABY67618.1; -; Genomic_DNA.
DR EMBL; EU351700; ABY67619.1; -; Genomic_DNA.
DR EMBL; EU351701; ABY67620.1; -; Genomic_DNA.
DR EMBL; EU351702; ABY67621.1; -; Genomic_DNA.
DR EMBL; EU351703; ABY67622.1; -; Genomic_DNA.
DR EMBL; EU351704; ABY67623.1; -; Genomic_DNA.
DR EMBL; EU351705; ABY67624.1; -; Genomic_DNA.
DR EMBL; EU351706; ABY67625.1; -; Genomic_DNA.
DR EMBL; EU351707; ABY67626.1; -; Genomic_DNA.
DR EMBL; EU351708; ABY67627.1; -; Genomic_DNA.
DR EMBL; EU351709; ABY67628.1; -; Genomic_DNA.
DR EMBL; EU351710; ABY67629.1; -; Genomic_DNA.
DR EMBL; EU351711; ABY67630.1; -; Genomic_DNA.
DR EMBL; EU351712; ABY67631.1; -; Genomic_DNA.
DR EMBL; EU351713; ABY67632.1; -; Genomic_DNA.
DR EMBL; EU351714; ABY67633.1; -; Genomic_DNA.
DR EMBL; EU351715; ABY67634.1; -; Genomic_DNA.
DR EMBL; EU351716; ABY67635.1; -; Genomic_DNA.
DR EMBL; EU351717; ABY67636.1; -; Genomic_DNA.
DR PIR; F86174; F86174.
DR RefSeq; NP_001323287.1; NM_001331475.1.
DR RefSeq; NP_171927.1; NM_100312.4.
DR AlphaFoldDB; P93825; -.
DR SMR; P93825; -.
DR BioGRID; 24784; 16.
DR IntAct; P93825; 11.
DR STRING; 3702.AT1G04310.1; -.
DR PaxDb; P93825; -.
DR PRIDE; P93825; -.
DR ProteomicsDB; 220704; -.
DR EnsemblPlants; AT1G04310.1; AT1G04310.1; AT1G04310.
DR EnsemblPlants; AT1G04310.2; AT1G04310.2; AT1G04310.
DR GeneID; 839549; -.
DR Gramene; AT1G04310.1; AT1G04310.1; AT1G04310.
DR Gramene; AT1G04310.2; AT1G04310.2; AT1G04310.
DR KEGG; ath:AT1G04310; -.
DR Araport; AT1G04310; -.
DR TAIR; locus:2018259; AT1G04310.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_114_48_1; -.
DR InParanoid; P93825; -.
DR OMA; ENRTEMK; -.
DR OrthoDB; 337812at2759; -.
DR PhylomeDB; P93825; -.
DR PRO; PR:P93825; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P93825; baseline and differential.
DR Genevisible; P93825; 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: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:0004674; F:protein serine/threonine kinase activity; TAS: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 InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR Pfam; PF01590; GAF; 1.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF47384; SSF47384; 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 Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..645
FT /note="Ethylene response sensor 2"
FT /id="PRO_0000378143"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 190..346
FT /note="GAF"
FT DOMAIN 389..623
FT /note="Histidine kinase"
FT BINDING 97
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 36
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VARIANT 14
FT /note="F -> FF (in strain: cv. Bla-10, cv. Cvi-0, cv. Ga-0
FT and cv. Ts-5)"
FT VARIANT 25
FT /note="A -> E (in strain: cv. El-0, Gy-0 and Kn-0)"
FT VARIANT 38
FT /note="D -> E (in strain: cv. El-0, Gy-0 and Kn-0)"
FT VARIANT 61
FT /note="I -> V (in strain: cv. Gu-0 and cv. Ove-0)"
FT VARIANT 244
FT /note="G -> V (in strain: cv. Se-0)"
FT MUTAGEN 67
FT /note="P->L: In ers2-1; ethylene insensitivity."
FT /evidence="ECO:0000269|PubMed:9707532"
FT MUTAGEN 94
FT /note="I->F: In ers2-2; ethylene insensitivity."
FT /evidence="ECO:0000269|PubMed:9707532"
SQ SEQUENCE 645 AA; 72192 MW; D37ABE3A0939D6ED CRC64;
MLKTLLVQWL VFFFFFLIGS VVTAAEDDGS LSLCNCDDED SLFSYETILN SQKVGDFLIA
IAYFSIPIEL VYFVSRTNVP SPYNWVVCEF IAFIVLCGMT HLLAGFTYGP HWPWVMTAVT
VFKMLTGIVS FLTALSLVTL LPLLLKAKVR EFMLSKKTRE LDREVGIIMK QTETSLHVRM
LTTKIRTSLD RHTILYTTLV ELSKTLGLKN CAVWIPNEIK TEMNLTHELR PRIDDENENE
HFGGYAGFSI PISESDVVRI KRSEEVNMLS PGSVLASVTS RGKSGPTVGI RVPMLRVCNF
KGGTPEAIHM CYAILVCVLP LRQPQAWTYQ ELEIVKVVAD QVAVAISHAV ILEESQLMRE
KLAEQNRALQ VARENALRAN QAKAAFEQMM SDAMRCPVRS ILGLLPLILQ DGKLPENQTV
IVDAMRRTSE LLVQLVNNAG DINNGTIRAA ETHYFSLHSV VKESACVARC LCMANGFGFS
AEVYRALPDY VVGDDRKVFQ AILHMLGVLM NRKIKGNVTF WVFPESGNSD VSERKDIQEA
VWRHCYSKEY MEVRFGFEVT AEGEESSSSS SGSNLEEEEE NPSLNACQNI VKYMQGNIRV
VEDGLGLVKS VSVVFRFQLR RSMMSRGGGY SGETFRTSTP PSTSH
