EIN4_ARATH
ID EIN4_ARATH Reviewed; 766 AA.
AC Q9ZTP3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein EIN4 {ECO:0000303|PubMed:9707532};
DE Short=AtEIN4 {ECO:0000303|PubMed:9707532};
DE EC=2.7.11.-;
DE AltName: Full=Protein ETHYLENE INSENSITIVE 4 {ECO:0000303|PubMed:9707532};
GN Name=EIN4 {ECO:0000303|PubMed:9707532};
GN OrderedLocusNames=At3g04580 {ECO:0000312|Araport:AT3G04580};
GN ORFNames=F7O18.5 {ECO:0000312|EMBL:AAF04908.1};
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 ILE-84 AND THR-117, LACK
RP OF 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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 [5]
RP INTERACTION WITH ETR1.
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 [6]
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 [7]
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 [8]
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.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos, etiolated seedlings, leaves,
CC roots, inflorescences, stamens, pollen cells and tapetum cells.
CC Moderate expression in carpels. {ECO:0000269|PubMed:9707532}.
CC -!- INDUCTION: Not induced by ethylene.
CC -!- PTM: Autophosphorylated predominantly on Ser residues.
CC {ECO:0000269|PubMed:15358768}.
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}.
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DR EMBL; AF048982; AAD02485.1; -; Genomic_DNA.
DR EMBL; AC011437; AAF04908.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74099.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74100.1; -; Genomic_DNA.
DR RefSeq; NP_187108.1; NM_111329.4.
DR RefSeq; NP_974218.1; NM_202489.2.
DR AlphaFoldDB; Q9ZTP3; -.
DR SMR; Q9ZTP3; -.
DR BioGRID; 4949; 8.
DR IntAct; Q9ZTP3; 1.
DR STRING; 3702.AT3G04580.1; -.
DR iPTMnet; Q9ZTP3; -.
DR PaxDb; Q9ZTP3; -.
DR PRIDE; Q9ZTP3; -.
DR ProteomicsDB; 224521; -.
DR EnsemblPlants; AT3G04580.1; AT3G04580.1; AT3G04580.
DR EnsemblPlants; AT3G04580.2; AT3G04580.2; AT3G04580.
DR GeneID; 819614; -.
DR Gramene; AT3G04580.1; AT3G04580.1; AT3G04580.
DR Gramene; AT3G04580.2; AT3G04580.2; AT3G04580.
DR KEGG; ath:AT3G04580; -.
DR Araport; AT3G04580; -.
DR TAIR; locus:2084968; AT3G04580.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_114_48_1; -.
DR InParanoid; Q9ZTP3; -.
DR OMA; LNAWTYY; -.
DR OrthoDB; 253193at2759; -.
DR PhylomeDB; Q9ZTP3; -.
DR PRO; PR:Q9ZTP3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ZTP3; baseline and differential.
DR Genevisible; Q9ZTP3; 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: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 SUPFAM; SSF55874; SSF55874; 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..766
FT /note="Protein EIN4"
FT /id="PRO_0000378144"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 181..331
FT /note="GAF"
FT DOMAIN 374..612
FT /note="Histidine kinase"
FT DOMAIN 643..761
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT MOD_RES 377
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT MOD_RES 694
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DISULFID 27
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 29
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CROSSLNK 746
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q0WPQ2"
FT MUTAGEN 84
FT /note="I->F: In ein4-1 and ein4-2; ethylene insensitivity."
FT /evidence="ECO:0000269|PubMed:9707532"
FT MUTAGEN 117
FT /note="T->M: In ein4-3; ethylene insensitivity."
FT /evidence="ECO:0000269|PubMed:9707532"
SQ SEQUENCE 766 AA; 86250 MW; 5DEA2DC3BFD38552 CRC64;
MLRSLGLGLL LFALLALVSG DNDYVSCNCD DEGFLSVHTI LECQRVSDLL IAIAYFSIPL
ELLYFISFSN VPFKWVLVQF IAFIVLCGMT HLLNAWTYYG PHSFQLMLWL TIFKFLTALV
SCATAITLLT LIPLLLKWKV RELYLKQNVL ELNEEVGLMK RQKEMSVQVR MLTREIRKSL
DKHMILRTTL VELSKILDLQ NSAVWMPNEN RTEMHLTHEL RANPMRSFRV IPINDPDVVQ
VRETKVVTIL RKNSVLAVES SGCGGSEEFG PVAAIRMPML HGLNFKGGTP EFVDTPYAIM
VLVLPSANSR VWTDKEIEIA EVVADQVAVA ISHASVLEES QLMREKLGIQ NRALLRAKQN
AMMASQARNT CQKVMSHGMR RPMHTILGLL SMFQSESMSL DQKIIVDALM KTSTVLSALI
NDVIDISPKD NGKSALEVKR FQLHSLIREA ACVAKCLSVY KGYGFEMDVQ TRLPNLVVGD
EKRTFQLVMY MLGYILDMTD GGKTVTFRVI CEGTGTSQDK SKRETGMWKS HMSDDSLGVK
FEVEINEIQN PPLDGSAMAM RHIPNRRYHS NGIKEGLSLG MCRKLAQMMQ GNIWISPKSH
GQTQSMQLVL RFQTRPSIRR SILAGNAPEL QHPNSNSILR GLRITLADDD DVNRTVTKRL
LEKLGCEVTA VSSGFECLNA LSNVEMSYRV VILDLQMPEM DGFEVAMKIR KFCGHHWPLI
IALTASTEDH VRERCLQMGM NGMIQKPVLL HVMASELRRA LQTASE
