ID E7D236_CICAR Unreviewed; 760 AA.
AC E7D236;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Ethylene receptor {ECO:0000256|PIRNR:PIRNR026389};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|EMBL:ADU03221.1};
RN [1] {ECO:0000313|EMBL:ADU03221.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22238063; DOI=10.1007/s00299-011-1221-9;
RA Madrid E., Rajesh P.N., Rubio J., Gil J., Millan T., Chen W.;
RT "Characterization and genetic analysis of an EIN4-like sequence (CaETR-1)
RT located in QTL(AR1) implicated in ascochyta blight resistance in
RT chickpea.";
RL Plant Cell Rep. 31:1033-1042(2012).
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|ARBA:ARBA00003286, ECO:0000256|PIRNR:PIRNR026389}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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 -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
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; HQ009511; ADU03221.1; -; Genomic_DNA.
DR AlphaFoldDB; E7D236; -.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0038199; F:ethylene receptor activity; IEA:UniProtKB-UniRule.
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:SF636; ETHYLENE RECEPTOR; 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|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR026389};
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..760
FT /note="Ethylene receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003218311"
FT TRANSMEM 51..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 377..614
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 635..753
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 340..370
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 89
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT BINDING 93
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT BINDING 558
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-1"
FT MOD_RES 686
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 DISULFID 30
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-3"
FT CROSSLNK 738
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-4"
SQ SEQUENCE 760 AA; 84916 MW; CA9AE44938234D77 CRC64;
MKILLLLLLL FFNLTLYATA TEAEYDHCNC DDEEALFSIH TILVGQKVSD FFIAVAYFSI
PIELLYFVSR SNVPFKLLFL QFIAFIVLCG MTHLLNAYSY HGPPSFHLLL SITVAKFLTA
LVSCATALTL PPLIPLLLKI KVRELFLRQN VMELGQEVGI MKKQKEASWH VRMLTREIRK
SLDKHTILYT TLVELSKAFD LHNCAVWMPN EDRREMYLTH ELKSDSGKSF HNSIPVIDPD
VLEIRKTKGV KILRPESKLG AGSSGGGSGK ELGAVAAIRM PMLHVSNFKG GTPELVDTCH
AILVLVLPSS NSRVWTKQEM EIVEVVADQV AVALSHASVL EESHLMRQKL EEQNRALQQS
QKNAMMASQA RKSFQTVMSH GLRRPMHSVV GMLSLFQDGI TRPEQKIIGD TMLKVGNVLS
SLVNDVMDIS DNKKGGLQLE MKPFLLHSML REAASIAKCL CVYEGFGFEI DVQKSLPEKV
LGVEARTFQV IMHIIGYLLN TCDRGKLAFR VLLASDGGDK DDKKLGVWRS SSQVEYVNIK
FDFQITGSSE SDESISTKQH SSRRLYHNSE SKEGLSFNMC RKLVQIMQGN IWISPNSDGL
VQGMSLLLKF QTGPSLERYI FAPKDSSNSQ FRGLKILLAD DDGLNRIVTK KLLEKLGCQV
TAVTSGFECL SAISSSANSF KIIMLDIHMP EMDGFEVATR IRKFNGPNWP LIIAVIANAE
DQVKDRCVLA GMNGVIRKPI LLHQIADELR TVLQRAGEKL
//
