ID ETR1_CUCMN Reviewed; 740 AA.
AC O82436;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 22-FEB-2023, entry version 119.
DE RecName: Full=Ethylene receptor 1;
DE EC=2.7.13.3;
DE AltName: Full=Cm-ETR1;
DE AltName: Full=MEETR1;
GN Name=ETR1;
OS Cucumis melo var. cantalupensis (Netted muskmelon) (Cucumis melo var.
OS reticulatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3658;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fruit;
RX PubMed=10318709; DOI=10.1104/pp.120.1.321;
RA Sato-Nara K., Yuhashi K., Higashi K., Hosoya K., Kubota M., Ezura H.;
RT "Stage- and tissue-specific expression of ethylene receptor homolog genes
RT during fruit development in muskmelon.";
RL Plant Physiol. 120:321-330(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fruit;
RA Furukawa H.;
RT "Gene expression analyses of Cm-ERS1 and Cm-ETR1 genes in ripening melon
RT fruit.";
RL Submitted (DEC-2000) 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: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 -!- TISSUE SPECIFICITY: In seeds and placenta.
CC -!- DEVELOPMENTAL STAGE: Early development of fruit and ripening.
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; AF054806; AAC99645.1; -; mRNA.
DR EMBL; AB052228; BAB18937.1; -; mRNA.
DR PIR; T51619; T51619.
DR AlphaFoldDB; O82436; -.
DR SMR; O82436; -.
DR BRENDA; 2.7.13.3; 1735.
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: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 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; 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_0000081414"
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..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; 82657 MW; 7C7D0C56B91C937A CRC64;
MENCYCIEPQ WPADELLMKY QYISDFFIAL AYFSIPLELI YFVKKSAVFP YRWVLVQFGA
FIVLCGATHL INLWTFTMHS RTVAVVMTTA KVLTAVVSCA TALMLVHIIP DLLSVKTREL
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLALEECA
LWMPTRTGLE LQLSYTLHQQ NPVGYTVPIN LPVISQVFSS NRALKISPNS PVASLRPRAG
RYVAGEVVAV RVPLLHLSNF QINDWPELST KRYALMVLML PSDSARQWRV HELELVEVVA
DQVAVALSHA AILEESMRAR DLLMEQNVAL DLARREAETA IRARNDFLAV MNHEMRTPMH
AIIALSSLLQ ETELTPEQRL MVETILKSSN LLATLINDVL DLSRLEDGSL QLDIGTFNLH
AVFKEVLNLI KPVTLVKKLS LTLHLGPDLP VFAVGDEKRL MQAILNVVGN AVKFSKEGSI
SISAIVAKSE TFREIRVPDF HPVPSDSHFY LRVQVKDTGS GISPQDIPKL FTKFAQTTVG
PRNSGGSGLG LAICKRFVNL MEGHIWLESE GLGKGCTATF IVKLGIADQS NESKLPYTSK
IHENSIHTSF PGLKVLVMDD NGVSRSVTKG LLVHLGCEVT TAGSIEEFLR VVSQEHKVVF
MDICTPGVDG YELAIRIREK FAKCHERPFM VVLTGNSDKV TKESCLRAGM DGLILKPVSI
DKMRSVLSEL IERRVLFETS
//
