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P49333 (ETR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ethylene receptor 1

Short name=AtETR1
EC=2.7.13.3
Alternative name(s):
Protein ETHYLENE RESPONSE 1
Protein ETR1
Gene names
Name:ETR1
Ordered Locus Names:At1g66340
ORF Names:T27F4.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length738 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling. Ref.11 Ref.12

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Cofactor

Binds 1 copper ion per dimer. Ref.7

Subunit structure

Homodimer; disulfide-linked. Heteromer with ERS1, ERS2, ETR2 and EIN4. Interacts with AHP1, AHP2 and AHP3. Interacts with RTE1. Ref.4 Ref.8 Ref.14 Ref.15

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.9.

Tissue specificity

Leaves, roots, stems, seedlings, flowers, anthers, carpels and ovules. Ref.6

Domain

The GAF domain is sufficient to mediate heteromerization.

Post-translational modification

Autophosphorylated predominantly on His residues. Activation probably requires a transfer of a phosphate group between a His in the transmitter domain and an Asp of the receiver domain By similarity. Ref.10

Disruption phenotype

No visible phenotype in ethylene response; due to redundancy with ERS1. Ers1 and etr1 double mutants display a constitutive ethylene-response phenotype. Ref.13

Sequence similarities

Belongs to the ethylene receptor family.

Contains 1 GAF domain.

Contains 1 histidine kinase domain.

Contains 1 response regulatory domain.

Ontologies

Keywords
   Biological processEthylene signaling pathway
Two-component regulatory system
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Copper
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to iron ion

Inferred from expression pattern PubMed 20627899. Source: TAIR

cytokinin metabolic process

Inferred from mutant phenotype PubMed 15773852. Source: TAIR

defense response

Traceable author statement PubMed 16255250. Source: TAIR

defense response by callose deposition in cell wall

Inferred from mutant phenotype PubMed 19095898. Source: TAIR

defense response to bacterium

Inferred from mutant phenotype PubMed 19095898. Source: TAIR

detection of ethylene stimulus

Inferred from mutant phenotype Ref.7. Source: TAIR

hydrogen peroxide biosynthetic process

Inferred from mutant phenotype PubMed 16961732. Source: TAIR

negative regulation of ethylene-activated signaling pathway

Traceable author statement Ref.9PubMed 11950991PubMed 12177468PubMed 12481081PubMed 12509505PubMed 12953109Ref.4Ref.1Ref.5PubMed 9695954. Source: TAIR

peptidyl-histidine phosphorylation

Inferred from mutant phenotype PubMed 22467798. Source: GOC

regulation of seedling development

Inferred from mutant phenotype PubMed 22467798. Source: TAIR

regulation of stomatal movement

Inferred from mutant phenotype PubMed 16961732. Source: TAIR

response to abscisic acid

Inferred from mutant phenotype PubMed 15773852. Source: TAIR

response to auxin

Inferred from mutant phenotype PubMed 15773852. Source: TAIR

response to ethylene

Inferred from mutant phenotype PubMed 22467798. Source: TAIR

response to gibberellin

Inferred from mutant phenotype PubMed 15773852. Source: TAIR

response to heat

Inferred from mutant phenotype PubMed 15923322. Source: TAIR

response to insect

Inferred from mutant phenotype PubMed 15923339. Source: TAIR

response to molecule of bacterial origin

Inferred from mutant phenotype PubMed 20592040. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 15044023. Source: TAIR

sugar mediated signaling pathway

Traceable author statement PubMed 12663220. Source: TAIR

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.9PubMed 19825542. Source: TAIR

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ethylene binding

Inferred from direct assay Ref.12. Source: TAIR

ethylene receptor activity

Inferred from mutant phenotype Ref.11. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 18384742Ref.14. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphorelay response regulator activity

Inferred from electronic annotation. Source: InterPro

phosphorelay sensor kinase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein histidine kinase activity

Inferred from mutant phenotype PubMed 22467798. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 738738Ethylene receptor 1
PRO_0000081412

Regions

Transmembrane23 – 4321Helical; Potential
Transmembrane53 – 7321Helical; Potential
Transmembrane92 – 11221Helical; Potential
Domain158 – 307150GAF
Domain350 – 585236Histidine kinase
Domain611 – 729119Response regulatory

Sites

Metal binding651Copper
Metal binding691Copper

Amino acid modifications

Modified residue3531Phosphohistidine; by autocatalysis By similarity
Modified residue65914-aspartylphosphate By similarity
Disulfide bond4Interchain Ref.4
Disulfide bond6Interchain Ref.4

Experimental info

Mutagenesis41C → S: Prevents dimerization but not ethylene binding. Ref.4 Ref.5
Mutagenesis61C → S: Prevents dimerization but not ethylene binding. Ref.4 Ref.5
Mutagenesis311A → V in etr1-3; ethylene insensitivity.
Mutagenesis381E → A: No effect on ethylene binding. Ref.7
Mutagenesis621I → F in etr1-4; ethylene insensitivity.
Mutagenesis651C → Y or S in etr1-1; no copper binding and ethylene insensitivity. Ref.5 Ref.7
Mutagenesis691H → A: No copper binding and ethylene insensitivity. Ref.7
Mutagenesis791H → A: No effect. Ref.7
Mutagenesis871M → A: No effect on ethylene binding. Ref.7
Mutagenesis991C → S: No effect on dimerization or ethylene binding. Ref.4 Ref.5
Mutagenesis1021A → T in etr1-2; ethylene insensitivity.
Mutagenesis1041M → A: No effect on ethylene binding. Ref.7
Mutagenesis1071H → A: No effect on ethylene binding. Ref.7

Secondary structure

..................... 738
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49333 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: D6ED3C4BBA87E96E

FASTA73882,566
        10         20         30         40         50         60 
MEVCNCIEPQ WPADELLMKY QYISDFFIAI AYFSIPLELI YFVKKSAVFP YRWVLVQFGA 

        70         80         90        100        110        120 
FIVLCGATHL INLWTFTTHS RTVALVMTTA KVLTAVVSCA TALMLVHIIP DLLSVKTREL 

       130        140        150        160        170        180 
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLALEECA 

       190        200        210        220        230        240 
LWMPTRTGLE LQLSYTLRHQ HPVEYTVPIQ LPVINQVFGT SRAVKISPNS PVARLRPVSG 

       250        260        270        280        290        300 
KYMLGEVVAV RVPLLHLSNF QINDWPELST KRYALMVLML PSDSARQWHV HELELVEVVA 

       310        320        330        340        350        360 
DQVAVALSHA AILEESMRAR DLLMEQNVAL DLARREAETA IRARNDFLAV MNHEMRTPMH 

       370        380        390        400        410        420 
AIIALSSLLQ ETELTPEQRL MVETILKSSN LLATLMNDVL DLSRLEDGSL QLELGTFNLH 

       430        440        450        460        470        480 
TLFREVLNLI KPIAVVKKLP ITLNLAPDLP EFVVGDEKRL MQIILNIVGN AVKFSKQGSI 

       490        500        510        520        530        540 
SVTALVTKSD TRAADFFVVP TGSHFYLRVK VKDSGAGINP QDIPKIFTKF AQTQSLATRS 

       550        560        570        580        590        600 
SGGSGLGLAI SKRFVNLMEG NIWIESDGLG KGCTAIFDVK LGISERSNES KQSGIPKVPA 

       610        620        630        640        650        660 
IPRHSNFTGL KVLVMDENGV SRMVTKGLLV HLGCEVTTVS SNEECLRVVS HEHKVVFMDV 

       670        680        690        700        710        720 
CMPGVENYQI ALRIHEKFTK QRHQRPLLVA LSGNTDKSTK EKCMSFGLDG VLLKPVSLDN 

       730 
IRDVLSDLLE PRVLYEGM 

« Hide

References

« Hide 'large scale' references
[1]"Arabidopsis ethylene-response gene ETR1: similarity of product to two-component regulators."
Chang C., Kwok S.F., Bleecker A.B., Meyerowitz E.M.
Science 262:539-544(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS ETR1-1; ETR1-2; ETR1-3 AND ETR1-4.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"The ethylene response mediator ETR1 from Arabidopsis forms a disulfide-linked dimer."
Schaller G.E., Ladd A.N., Lanahan M.B., Spanbauer J.M., Bleecker A.B.
J. Biol. Chem. 270:12526-12530(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, MUTAGENESIS OF CYS-4; CYS-6 AND CYS-99.
[5]"Ethylene-binding sites generated in yeast expressing the Arabidopsis ETR1 gene."
Schaller G.E., Bleecker A.B.
Science 270:1809-1811(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-4; CYS-6; CYS-65 AND CYS-99.
[6]"EIN4 and ERS2 are members of the putative ethylene receptor gene family in Arabidopsis."
Hua J., Sakai H., Nourizadeh S., Chen Q.G., Bleecker A.B., Ecker J.R., Meyerowitz E.M.
Plant Cell 10:1321-1332(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"A copper cofactor for the ethylene receptor ETR1 from Arabidopsis."
Rodriguez F.I., Esch J.J., Hall A.E., Binder B.M., Schaller G.E., Bleecker A.B.
Science 283:996-998(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, MUTAGENESIS OF GLU-38; CYS-65; HIS-69; HIS-79; MET-87; MET-104 AND HIS-107.
[8]"Possible His to Asp phosphorelay signaling in an Arabidopsis two-component system."
Urao T., Miyata S., Yamaguchi-Shinozaki K., Shinozaki K.
FEBS Lett. 478:227-232(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AHP1; AHP2 AND AHP3.
[9]"Localization of the ethylene receptor ETR1 to the endoplasmic reticulum of Arabidopsis."
Chen Y.-F., Randlett M.D., Findell J.L., Schaller G.E.
J. Biol. Chem. 277:19861-19866(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Autophosphorylation activity of the Arabidopsis ethylene receptor multigene family."
Moussatche P., Klee H.J.
J. Biol. Chem. 279:48734-48741(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[11]"Requirement of the histidine kinase domain for signal transduction by the ethylene receptor ETR1."
Qu X., Schaller G.E.
Plant Physiol. 136:2961-2970(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Ethylene-binding activity, gene expression levels, and receptor system output for ethylene receptor family members from Arabidopsis and tomato."
O'Malley R.C., Rodriguez F.I., Esch J.J., Binder B.M., O'Donnell P., Klee H.J., Bleecker A.B.
Plant J. 41:651-659(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"A strong constitutive ethylene-response phenotype conferred on Arabidopsis plants containing null mutations in the ethylene receptors ETR1 and ERS1."
Qu X., Hall B.P., Gao Z., Schaller G.E.
BMC Plant Biol. 7:3-3(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[14]"Heteromeric interactions among ethylene receptors mediate signaling in Arabidopsis."
Gao Z., Wen C.-K., Binder B.M., Chen Y.-F., Chang J., Chiang Y.-H., Kerris R.J. III, Chang C., Schaller G.E.
J. Biol. Chem. 283:23801-23810(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERS1; ERS2; ETR2 AND EIN4.
[15]"Molecular association of the Arabidopsis ETR1 ethylene receptor and a regulator of ethylene signaling, RTE1."
Dong C.H., Jang M., Scharein B., Malach A., Rivarola M., Liesch J., Groth G., Hwang I., Chang C.
J. Biol. Chem. 285:40706-40713(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTE1.
[16]"The structure of the signal receiver domain of the Arabidopsis thaliana ethylene receptor ETR1."
Mueller-Dieckmann H.-J., Grantz A.A., Kim S.-H.
Structure 7:1547-1556(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 603-738.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L24119 Genomic DNA. Translation: AAA70047.1.
AC020665 Genomic DNA. Translation: AAG52169.1.
CP002684 Genomic DNA. Translation: AEE34497.1.
PIRA48246.
RefSeqNP_176808.3. NM_105305.4.
UniGeneAt.43238.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCFX-ray2.50A605-738[»]
ProteinModelPortalP49333.
SMRP49333. Positions 342-572, 605-736.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid28172. 12 interactions.
IntActP49333. 11 interactions.
MINTMINT-8068106.

Proteomic databases

PaxDbP49333.
PRIDEP49333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G66340.1; AT1G66340.1; AT1G66340.
GeneID842951.
KEGGath:AT1G66340.

Organism-specific databases

TAIRAT1G66340.

Phylogenomic databases

eggNOGCOG2202.
HOGENOMHOG000240343.
InParanoidP49333.
KOK14509.
OMAQIALRIH.
PhylomeDBP49333.

Enzyme and pathway databases

BioCycARA:AT1G66340-MONOMER.
BRENDA2.7.13.3. 399.

Gene expression databases

ArrayExpressP49333.
GenevestigatorP49333.

Family and domain databases

Gene3D1.10.287.130. 1 hit.
3.30.450.40. 1 hit.
3.30.565.10. 1 hit.
InterProIPR011006. CheY-like_superfamily.
IPR003661. EnvZ-like_dim/P.
IPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003594. HATPase_ATP-bd.
IPR004358. Sig_transdc_His_kin-like_C.
IPR014525. Sig_transdc_His_kin_hyb_Et-sen.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamPF01590. GAF. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF026389. Ethyln_sen_HK. 1 hit.
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00065. GAF. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 1 hit.
SSF55781. SSF55781. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEPS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49333.

Entry information

Entry nameETR1_ARATH
AccessionPrimary (citable) accession number: P49333
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names