ID   ETR2_PELHO              Reviewed;         741 AA.
AC   Q9XH57;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Ethylene receptor 2;
DE            EC=2.7.13.3;
DE   AltName: Full=PhETR2;
GN   Name=ETR2;
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; AF141929; AAD37577.1; -; mRNA.
DR   AlphaFoldDB; Q9XH57; -.
DR   SMR; Q9XH57; -.
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..741
FT                   /note="Ethylene receptor 2"
FT                   /id="PRO_0000081421"
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..589
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   741 AA;  82897 MW;  E4F72634EA84E076 CRC64;
     MESCNCIEPQ WPADELLMKY QYISDFFIAI AYFSIPLELI YFVKKSAVFP YRWVLVQFGA
     FIVLCGATHL INLWTFNMHS KTVEIVMTTA KIMTAVVSCA TALMLVHIIP DLLSVKTREL
     FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLALEECA
     LWMPTRTGLE LQLSYTLRQQ NPVGFTVPIH LPVINQVFSS NHAIKISPNS PIARLRPIAG
     KYMPGEVVGV RVPLLHLSNF QINDWPELST KRYALMVLML PSDSARQWHV HELELVEVVA
     DQVAVALSHA AILEESMRAR DLLMEQNVAL DMARREAETA IRARNDFLAV MNHEMRTPMH
     AIIALSSLLQ ETELTPEQRL MVETVLKSSN LLATLINDVL DLSRLEDGSL QLDIGTFNLH
     ALLREVHNLI KPIASVKKLC ISLNVATDLP EYAVGDEKRL VQIILNVVGN AVKFSKEGNI
     SITAFVAKSE SLRDPRAPDF FPICGENQFY LRVQVKDSGL GINPQDIPRL FTKFAQTQPV
     ATKNSGGSGL GLAICKRFVN LMEGHIWIDS EGPGKGCTAT FVVKLGIPER SSEPKLLLMP
     KVPANHGQTN FSGLKVLLLD DNGVSRAVTR GLLAHLGCDV TTVSSSDELL RVVSQDYKVV
     FMDVCMPEVD GFEIAVRIHE KFMTRHERPL IVALTGNIDQ VTKDNCTRVG MEGVVLKPVS
     IDKMRNVLSN LLEHRVLFEA I