ETR1_PELHO
ID ETR1_PELHO Reviewed; 740 AA.
AC Q9XH58;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ethylene receptor 1;
DE EC=2.7.13.3;
DE AltName: Full=PhETR1;
GN Name=ETR1;
OS Pelargonium hortorum (Common geranium) (Pelargonium inquinans x Pelargonium
OS zonale).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Geraniales; Geraniaceae; Pelargonium.
OX NCBI_TaxID=4031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10890532; DOI=10.1023/a:1006409827860;
RA Dervinis C., Clark D.G., Barrett J.E., Nell T.A.;
RT "Effect of pollination and exogenous ethylene on accumulation of ETR1
RT homologue transcripts during flower petal abscission in geranium
RT (Pelargonium x hortorum L.H. Bailey).";
RL Plant Mol. Biol. 42:847-856(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 -!- DEVELOPMENTAL STAGE: Constant expression throughout floral development.
CC -!- INDUCTION: Not induced by ethylene.
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; AF141928; AAD37576.1; -; mRNA.
DR AlphaFoldDB; Q9XH58; -.
DR SMR; Q9XH58; -.
DR BRENDA; 2.7.13.3; 4583.
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_0000081420"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 158..307
FT /note="GAF"
FT DOMAIN 350..587
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 615..732
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 663
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; 82957 MW; 3F191A3EB51F1335 CRC64;
MEACNCFEPQ WPADDLLMKY QYISDFFIAV AYFSIPLELI YFVKKSAVFP YKWVLVQFGA
FIVLCGATHL INLWTFNLHT RTVEIVMTTA KLMTAAVSCV TALMLVHIIP DLLSVKTREL
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLGLEECA
LWMPTRTGLE LQLSHTLRQQ NPVGYTVPIH LPVLNQVFSS NRAIKISPNS PIARLRPLAG
KYVPGEVVAV RVPLLHLSNF QINDWPELST KRYAMMVLML PSDSARQWHV HELELVEVVA
DQVAVALSHA AILEESMRAR DLLMEQNVAL DMARREAETA IRARNDFLAV MNHEMRTPMH
AIIALSSLLQ ETDLTSEQRL MVETILKSSN LLATLINDVL DLSRLEDGSL QLDIATFNLH
AVFRQVFNLI KPIASVKKLF ITLNVSPDLP EYVIGDEKRL VQIMLNVVGN AVKFSKEGII
SVTAFVAKSE SVRDPRAPDF FPVSSDNQFY MRVQVKDSGS GINPQDMPKL FTKFAQSQPV
ATKNSGGSGL GLAISKRFVN LMDGHIWIDS EGPSKGCTVT FVVKLGIPEG SNEPKLPLMP
KVSANNSQTD FPGLKVLLMD ENGISRMVTK GLLMHLGCDV TSVSSSEECL RMVSQDHKVV
FMDVRVPGLD GHELAVRIHE KFMKRHERPL IVALTSNADK VTKENCLRVG MEGVILKPVS
VDKMRNVLSK LLEHRILFEA
