ID A0A059B7A8_EUCGR Unreviewed; 762 AA.
AC A0A059B7A8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Ethylene receptor {ECO:0000256|PIRNR:PIRNR026389};
GN ORFNames=EUGRSUZ_H04259 {ECO:0000313|EMBL:KCW61540.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW61540.1};
RN [1] {ECO:0000313|EMBL:KCW61540.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW61540.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR026389}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|PIRSR:PIRSR026389-2};
CC Note=Binds 1 copper ion per dimer. {ECO:0000256|PIRSR:PIRSR026389-2};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ethylene receptor family.
CC {ECO:0000256|ARBA:ARBA00009842, ECO:0000256|PIRNR:PIRNR026389}.
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DR EMBL; KK198760; KCW61539.1; -; Genomic_DNA.
DR EMBL; KK198760; KCW61540.1; -; Genomic_DNA.
DR RefSeq; XP_010024975.1; XM_010026673.2.
DR RefSeq; XP_018717244.1; XM_018861699.1.
DR STRING; 71139.A0A059B7A8; -.
DR EnsemblPlants; KCW61539; KCW61539; EUGRSUZ_H04259.
DR EnsemblPlants; KCW61540; KCW61540; EUGRSUZ_H04259.
DR GeneID; 104415384; -.
DR Gramene; KCW61539; KCW61539; EUGRSUZ_H04259.
DR Gramene; KCW61540; KCW61540; EUGRSUZ_H04259.
DR KEGG; egr:104415384; -.
DR eggNOG; KOG0519; Eukaryota.
DR OMA; FNCCDED; -.
DR OrthoDB; 1770905at2759; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051740; F:ethylene binding; IBA:GO_Central.
DR GO; GO:0038199; F:ethylene receptor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IEA:UniProt.
DR CDD; cd16938; HATPase_ETR2_ERS2-EIN4-like; 1.
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; 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; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24423:SF629; PROTEIN EIN4; 1.
DR PANTHER; PTHR24423; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00512; HisKA; 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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR026389};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRNR:PIRNR026389};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR026389-3};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR026389};
KW Ethylene signaling pathway {ECO:0000256|ARBA:ARBA00022745,
KW ECO:0000256|PIRNR:PIRNR026389};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR026389};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR026389};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR026389,
KW ECO:0000256|PIRSR:PIRSR026389-2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR026389};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR026389};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR026389};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|PIRNR:PIRNR026389}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..762
FT /note="Ethylene receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015026486"
FT TRANSMEM 48..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 372..607
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 637..755
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 335..365
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 86
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT BINDING 90
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT MOD_RES 688
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT DISULFID 28
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-3"
FT CROSSLNK 740
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-4"
SQ SEQUENCE 762 AA; 85582 MW; B37C649E103394AC CRC64;
MLRAVALGLF LSSLTVRAYA DDNGYSCCDD EGFWTVERIL ECQRVSDFLI AVAYFSIPLE
LLYFVSLSNV PFKWVLALFI AFIVLCGLTH LLNGWTYYGP HSFQLMLSLT VAKFFTALVS
CLTAIALLTL IPLLLKVKVR ETFLRRNVLE LDQEVEMMKR QKEASWHVRM LTREIRKSLD
KHTILYTTLV ELSKTLDLHN CAVLMPNNDR TEMIMTHELK GSSRKSYGRS ITISDPDVIE
IKESKGVKIL RPDSALAVVS SGGLDELGAV AAIRMPMLQA SNFKGGTPQS IDTHYAILVL
VLPQANPRDW SYQELEIVEV VADQVAVALS HAAVLEESQL MREKLAEQNR ALQQARRKAM
MASQARHSFQ KVMSHGMRRP MHSIVGLLSI LREETVNPEQ KLTVDAMATT SNVLSTLIND
VMEMSAKDDG KFPFEMRRFH LHAMIKEASY LAKCLCVYRG CGFEISVKSS PPDQVMGDER
RTFQVILHMF GYLLDIYDGG GNVTFRVSCE SDTEVKHDKT WGPQAISPAN EFVTVKFEIE
IASGSAPSGG LIPVMHSAGW SRGSSNNNKD TLSFNVCKKL VQMMQGNIWI ASNSRGLTQR
MTLVLRFLKQ DSRGRAMLPS GNHMEQQNLD SLFRGLRVLL ADDDVVNRTV TKKLLEKLGC
QVTSVSTGLE CLTALSHTDN SLRVVFLDLH MPDMDGFEVA MRIRKYRSRH WPLIIALTAS
AEEHVWERCL QMGMNGVLWK PVVLQGVADE LRRVLQRAGE AV
//
