P49333 (ETR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	738 AA.
Sequence status	Complete.
Protein existence	Evidence 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 effect on ethylene response due to the redundancy with ERS1. Double mutants in ERS1 and ETR1 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 process	Ethylene signaling pathway Two-component regulatory system
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Copper Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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 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 ethylene mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW hydrogen peroxide biosynthetic process Inferred from mutant phenotype PubMed 16961732. Source: TAIR intracellular signal transduction Inferred from electronic annotation. Source: GOC negative regulation of ethylene mediated signaling pathway Traceable author statement Ref.9PubMed 11950991PubMed 12177468PubMed 12481081PubMed 12509505PubMed 12953109Ref.4Ref.1Ref.5PubMed 9695954. Source: TAIR regulation of seedling development Inferred from mutant phenotype PubMed 22467798. Source: TAIR regulation of stomatal movement Inferred from mutant phenotype PubMed 16961732. Source: TAIR regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro response to abscisic acid stimulus Inferred from mutant phenotype PubMed 15773852. Source: TAIR response to auxin stimulus Inferred from mutant phenotype PubMed 15773852. Source: TAIR response to gibberellin stimulus 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 signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC sugar mediated signaling pathway Traceable author statement PubMed 12663220. Source: TAIR
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.9PubMed 19825542. Source: TAIR endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ethylene binding Inferred from direct assay Ref.12. Source: TAIR 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 histidine kinase activity Inferred from mutant phenotype PubMed 22467798. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1606682,EBI-1606682
AHP1	Q9ZNV9	3	EBI-1606682,EBI-1100673
CTR1	Q05609	6	EBI-1606682,EBI-1606697
EIN2	Q9S814	2	EBI-1606682,EBI-2437287
ERS2	P93825	2	EBI-1606682,EBI-1787556
ETR2	Q0WPQ2	2	EBI-1606682,EBI-1787533
RTE1	F4ITL6	5	EBI-1606682,EBI-2437263

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 738

738

Ethylene receptor 1

PRO_0000081412

Regions

Transmembrane

23 – 43

21

Helical; Potential

Transmembrane

53 – 73

21

Helical; Potential

Transmembrane

92 – 112

21

Helical; Potential

Domain

158 – 307

150

GAF

Domain

350 – 585

236

Histidine kinase

Domain

611 – 729

119

Response regulatory

Sites

Metal binding

65

1

Copper

Metal binding

69

1

Copper

Amino acid modifications

Modified residue

353

1

Phosphohistidine; by autocatalysis By similarity

Modified residue

659

1

4-aspartylphosphate By similarity

Disulfide bond

4

Interchain Ref.4

Disulfide bond

6

Interchain Ref.4

Experimental info

Mutagenesis

4

1

C → S: Prevents dimerization but not ethylene binding. Ref.4 Ref.5

Mutagenesis

6

1

C → S: Prevents dimerization but not ethylene binding. Ref.4 Ref.5

Mutagenesis

31

1

A → V in etr1-3; ethylene insensitivity.

Mutagenesis

38

1

E → A: No effect on ethylene binding. Ref.7

Mutagenesis

62

1

I → F in etr1-4; ethylene insensitivity.

Mutagenesis

65

1

C → Y or S in etr1-1; no copper binding and ethylene insensitivity. Ref.5 Ref.7

Mutagenesis

69

1

H → A: No copper binding and ethylene insensitivity. Ref.7

Mutagenesis

79

1

H → A: No effect. Ref.7

Mutagenesis

87

1

M → A: No effect on ethylene binding. Ref.7

Mutagenesis

99

1

C → S: No effect on dimerization or ethylene binding. Ref.4 Ref.5

Mutagenesis

102

1

A → T in etr1-2; ethylene insensitivity.

Mutagenesis

104

1

M → A: No effect on ethylene binding. Ref.7

Mutagenesis

107

1

H → A: No effect on ethylene binding. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

738

Helix Strand Turn

Details...

Beta strand

611 – 615

5

Helix

619 – 631

13

Beta strand

635 – 641

7

Helix

642 – 648

7

Beta strand

654 – 659

6

Turn

664 – 668

5

Helix

669 – 678

10

Beta strand

687 – 693

7

Helix

697 – 705

9

Beta strand

710 – 715

6

Helix

718 – 729

12

Sequences

	Sequence		Length	Mass (Da)
	P49333 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: D6ED3C4BBA87E96E	FASTA	738	82,566
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00538410.

PIR

A48246.

RefSeq

NP_176808.3. NM_105305.4.

UniGene

At.43238.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DCF	X-ray	2.50	A	605-738	[»]

ProteinModelPortal

P49333.

SMR

P49333. Positions 342-572, 605-736.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49333. 11 interactions.

Proteomic databases

PaxDb

P49333.

PRIDE

P49333.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT1G66340.1; AT1G66340.1; AT1G66340.

GeneID

842951.

KEGG

ath:AT1G66340.

Organism-specific databases

TAIR

At1g66340.

Phylogenomic databases

eggNOG

COG2202.

HOGENOM

HOG000240343.

InParanoid

P49333.

KO

K14509.

OMA

NIWIESD.

PhylomeDB

P49333.

ProtClustDB

CLSN2680572.

Enzyme and pathway databases

BRENDA

2.7.13.3. 399.

Gene expression databases

ArrayExpress

P49333.

Genevestigator

P49333.

GermOnline

AT1G66340. Arabidopsis thaliana.

Family and domain databases

Gene3D

1.10.287.130. 1 hit.
3.30.565.10. 1 hit.

InterPro

IPR011006. CheY-like_superfamily.
IPR003018. GAF.
IPR003594. HATPase_ATP-bd.
IPR004358. Sig_transdc_His_kin-like_C.
IPR014525. Sig_transdc_His_kin_hyb_Et-sen.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]

Pfam

PF01590. GAF. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]

PIRSF

PIRSF026389. Ethyln_sen_HK. 1 hit.

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00065. GAF. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF52172. CheY_like. 1 hit.
SSF47384. His_kin_homodim. 1 hit.

PROSITE

PS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P49333.

Entry information

Entry name

ETR1_ARATH

Accession

Primary (citable) accession number: P49333

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program