ETR1_CUCSA
ID ETR1_CUCSA Reviewed; 740 AA.
AC Q9SSY6;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ethylene receptor 1;
DE EC=2.7.13.3;
DE AltName: Full=CS-ETR1;
GN Name=ETR1;
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10929944; DOI=10.1093/pcp/41.5.608;
RA Yamasaki S., Fujii N., Takahashi H.;
RT "The ethylene-regulated expression of CS-ETR2 and CS-ERS genes in cucumber
RT plants and their possible involvement with sex expression in flowers.";
RL Plant Cell Physiol. 41:608-616(2000).
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; AB026498; BAA85817.1; -; mRNA.
DR RefSeq; NP_001267562.1; NM_001280633.1.
DR AlphaFoldDB; Q9SSY6; -.
DR SMR; Q9SSY6; -.
DR STRING; 3659.XP_004152845.1; -.
DR GeneID; 101213479; -.
DR KEGG; csv:101213479; -.
DR eggNOG; KOG0519; Eukaryota.
DR BRENDA; 2.7.13.3; 1733.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051740; F:ethylene binding; IEA:InterPro.
DR GO; GO:0038199; F:ethylene receptor activity; IEA:InterPro.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IEA:UniProt.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 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 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; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 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; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Receptor; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..740
FT /note="Ethylene receptor 1"
FT /id="PRO_0000081415"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
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..588
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 614..731
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:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 662
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"
SQ SEQUENCE 740 AA; 82640 MW; 6ADEDF0865391F8D CRC64;
METCYCIEPQ WPADELLMKY QYISDFFIAL AYFSIPLELI YFVKKSAVFP YRWVLVQFGA
FIVLCGATHL INLWTFTMHS RTVAVVMTTA KVLTAVVSCA TALMLVHIIP DLLSVKTREL
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLALEECA
LWMPTRTGLE LQLSYTLHQQ NPVGYTVPIN LPVISQVFSS NRAVKISPNS PVASLRPRAG
RYVAGEVVAV RVPLLHLSNF QINDWPELST KRYALMVLML PSDSARQWRV HELELVEVVA
DQVAVALSHA AILEESMRAR DPLMEQNVAL DLARREAETA NHARNDFLAV MNHEMRTPMH
AIIALSSLLQ ETELTPEQRL MVETILKSSN LLATLINDVL DLSRLEDGSL QLDIGTFNLH
AVFKEVLNLI KPVTLVKKLS LTLHLGLDLP VFAVGDEKRL MQAILNVVGN AVKFSKEGSI
SISAIVAKAE TFREIRVPDF HPVPSDSHFY LRVQVKDTGS GISPQDIPKL FTKFAQTTVG
PRNSCGSGLG LAICKRFVNL MEGHIWLESE GLGKGCTATF IVKLGIAEQS NESKLPFTSK
IHENSIHTSF PGLKVLVMDD NGVSRSVTKG LLVHLGCEVT TAGSIEEFLR VVSQEHKVVF
MDICTPGVDG YELAIRIREK FAKCHERPFM VVLTGNSDKV TKESCLRAGM DGLILKPVSI
DKMRSVLSEL IERRVLFETS
