ID A0A2P5DJJ8_TREOI Unreviewed; 765 AA.
AC A0A2P5DJJ8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ethylene receptor {ECO:0000256|PIRNR:PIRNR026389};
GN Name=TorETR2 {ECO:0000313|EMBL:PON73467.1};
GN ORFNames=TorRG33x02_249500 {ECO:0000313|EMBL:PON73467.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON73467.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PON73467.1}.
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DR EMBL; JXTC01000266; PON73467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5DJJ8; -.
DR STRING; 63057.A0A2P5DJJ8; -.
DR InParanoid; A0A2P5DJJ8; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000237000; Unassembled WGS sequence.
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: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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000237000};
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..765
FT /note="Ethylene receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015173184"
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 374..608
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 640..758
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 337..364
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 88
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT MOD_RES 691
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 743
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-4"
SQ SEQUENCE 765 AA; 86315 MW; D4977E1555F3D56C CRC64;
MLRAFLLILL ISCLIFSVSA IDNEYPHCSC DDEGFWSLST ILECQKVSDF LIAVAYFSIP
IELLYFVSFS SLPFKWVLFQ FIAFIVLCGL THLLNGWTYY GPHSFQLMLS LTIAKFLTAL
VSCATAITLL TLIPLLLKVK VRELFLKQNV LELDQEVGMM KRQKEASWHV RMLTREIRKS
LDKHTILYTT LVELSKTLEL YNCAVWMPNE NRREMNLTHE LKPRSSKGYP RSIPINDPDV
LEIRESKGVR ILRPESALGD ASRGESGESG AVAAIRMPML RVSNFKGGTP EMVDTCYAIL
VLVLPGANSR AWSYPEMEIV EVVADQVAVA LSHADVLEES QMMREKLAEQ NRALQQAKKN
AMMASHARNT FQKVMSHGMR RPMHSILGLL SIVTEENMSF EQRIIIDTML KTSSVLSTLI
NDVMEISTND NGRFPLQMRP FELHSMIREA ACLVKCLCMY KGVGFETDVQ SSLPNQVIGD
ERRAFQVILH MVGYLLSIYK GGGTVMFRVF SESGSEGRAD KLPGMWRPSM ADEFVSIKFE
FQISKGGSWS EGSTSDIDYA SRRQNSNEIK EGLSFSICKR LVQMMQGNIW ISPNPVGFAQ
SMTLLLRFQV RPYFGRGIFG PGNSIDQQQP RSNPQFRGLR VILADDDDVN RTVTKKLLEK
LGCQVLAVSS GFECLTAVTS AENSCRVVLL DIHMPEMDGF EVAMRIRKFR SHNWPLIIAV
TASAEEHVWE RCLQMGMNGL IRKPVLLQCL ADELQRVLQR AGEGL
//
