ETR1_PRUPE
ID ETR1_PRUPE Reviewed; 738 AA.
AC Q9M7M1;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ethylene receptor;
DE EC=2.7.13.3;
GN Name=ETR1;
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Loring;
RA Bassett C.B., Artlip T.S., Nickerson M.L.;
RT "ETR (ethylene receptor) homologue from peach (Prunus persica).";
RL Submitted (JAN-1999) 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 -!- 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; AF124527; AAF28893.1; -; mRNA.
DR AlphaFoldDB; Q9M7M1; -.
DR SMR; Q9M7M1; -.
DR STRING; 3760.EMJ26422; -.
DR PRIDE; Q9M7M1; -.
DR eggNOG; KOG0519; Eukaryota.
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..738
FT /note="Ethylene receptor"
FT /id="PRO_0000081422"
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..589
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 612..729
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 660
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 738 AA; 82714 MW; 6D0E25B3BC7CB71D CRC64;
MEACNCIEPQ WPADELLMKY QYISDFFIAL AYFSIPLELI YFVKKSAVFP YRWVLVQFGA
FIVLCGATHL INLWTFSMHS RTVAIVMTTA KVLTAVVSCA TALMLVHIIP DLLSVKTREL
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLALEECA
LWMPTRTGLE LQLSYTLRQQ NPVGYTVPIH LPVINQVFSS NRALKISPNS PVARMRPLAG
KHMPGEVVAV RVPLLHLSNF QINDWPELST KRYALMVLML PSDSARQWHV HELELVEVVA
DQVAVALSHA AILEESMRAR DLLMEQNIAL DLARREAETA IRARNDFLAV MNHEMRTPMH
AIIALSSLLQ ETELTPEQRL MVETILKSSH LLATLINDVL DLSRLEDGSL QLEIATFNLH
SVFREVHNLI KPVASVKKLS VSLNLAADLP VQAVGDEKRL MQIVLNVVGN AVKFSKEGSI
SITAFVAKSE SLRDFRAPEF FPAQSDNHFY LRVQVKDSGS GINPQDIPKL FTKFAQTQSL
ATRNSGGSGL GLAICKRFVN LMEGHIWIES EGPGKGCTAI FIVKLGFAER SNESKLPFLT
KVQANHVQTN FPGLKVLVMD DNGSVTKGLL VHLGCDVTTV SSIDEFLHVI SQEHKVVFMD
VCMPGIDGYE LAVRIHEKFT KRHERPVLVA LTGNIDKMTK ENCMRVGMDG VILKPVSVDK
MRSVLSELLE HRVLFEAM
