ID ETR1_BRAOL Reviewed; 735 AA.
AC O49230;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 22-FEB-2023, entry version 125.
DE RecName: Full=Ethylene receptor 1;
DE EC=2.7.13.3;
GN Name=ETR1;
OS Brassica oleracea (Wild cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3712;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen H.-H., Charng Y.-Y., Yang S.F., Shaw J.-F.;
RT "Molecular cloning and sequencing of a broccoli cDNA encoding an ETR-type
RT ethylene receptor.";
RL (er) Plant Gene Register PGR98-088(1998).
CC -!- FUNCTION: May act early in the ethylene signal transduction pathway,
CC possibly as an ethylene receptor, or as a regulator of the pathway.
CC {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- PTM: Activation probably requires a transfer of a phosphate group
CC between a His in the transmitter domain and an Asp of the receiver
CC domain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
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DR EMBL; AF047476; AAC39497.1; -; mRNA.
DR AlphaFoldDB; O49230; -.
DR SMR; O49230; -.
DR BRENDA; 2.7.13.3; 947.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051740; F:ethylene binding; IEA:EnsemblPlants.
DR GO; GO:0038199; F:ethylene receptor activity; IEA:EnsemblPlants.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblPlants.
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:0051301; P:cell division; IEA:EnsemblPlants.
DR GO; GO:0009690; P:cytokinin metabolic process; IEA:EnsemblPlants.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IEA:EnsemblPlants.
DR GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0009727; P:detection of ethylene stimulus; IEA:EnsemblPlants.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IEA:UniProt.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IEA:EnsemblPlants.
DR GO; GO:1900140; P:regulation of seedling development; IEA:EnsemblPlants.
DR GO; GO:0010119; P:regulation of stomatal movement; IEA:EnsemblPlants.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009733; P:response to auxin; IEA:EnsemblPlants.
DR GO; GO:0009739; P:response to gibberellin; IEA:EnsemblPlants.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR GO; GO:0009625; P:response to insect; IEA:EnsemblPlants.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR GO; GO:0010162; P:seed dormancy process; IEA:EnsemblPlants.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19933; REC_ETR-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR014525; ETR.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24423:SF615; ETHYLENE RECEPTOR 1; 1.
DR PANTHER; PTHR24423; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF026389; Ethyln_sen_HK; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Copper; Disulfide bond; Endoplasmic reticulum;
KW Ethylene signaling pathway; Isopeptide bond; Kinase; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system;
KW Ubl conjugation.
FT CHAIN 1..735
FT /note="Ethylene receptor 1"
FT /id="PRO_0000081413"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 158..307
FT /note="GAF"
FT DOMAIN 350..586
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 609..726
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
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 MOD_RES 657
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DISULFID 4
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 6
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CROSSLNK 711
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q0WPQ2"
SQ SEQUENCE 735 AA; 82240 MW; 520B77291CF2BCC6 CRC64;
MEVCNCIEPQ WPADELLMKY QYISDFFIAV AYFSIPLELI YFVKKSAVFP YRWVLVQFGA
FIVLCGATHL INLWTFTTHS RTVALVMTTA KVLTAVVSCA TALMLVHIIP DLLSVKTREL
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLALEECA
LWMPTRTGLE LQLSYTLRQQ HPVEYTVPIQ LPVINQVFGT SRAVKISPNS PVARLRPVSG
KYLLGEVVAV RVPLLHLSNF QINDWPELST KRYALMVLML PSDSARQWHV HELELVEVVA
DQVAVALSHA AILEESMRAR DLLMEQNVAL DIARREAETA IRARNDFLAV MNHEMRTPMH
AIIALSSLLQ ETELTPEQRL MVETVLKSSS LLATLMNDVL DLSRLEDGSL QLELGTFNLH
TLFREVLNLI KPIAVVKKLP ITLNLAPDLP EFVVGDEKRL MQIILNIVGN AVKFSKQGSI
SVTALVTKSD NRAPPDFFVV PTGSHFYLRV KVKDLGAGIN PQDIPKLFTK FAQTQSLATR
SSGGSGLGLA ISKRFVNLME GNIWIESEGV GKGCTAIFDV KLAISNESKQ SGIPKVPANP
QHVNFAGLKV LVMDENGVSR MVTKGLLVHL GCEVTTVSSN EECLRVVSHE HRVVFMDVCT
PGVENYQIAL RIHEKFTKRH QRPLLVALTG NTDKSTKEKC MSFGLDGVLL KPVSLDNMRN
VLSDRLEHRV LYEAM
//
