ETR1_PASED
ID ETR1_PASED Reviewed; 738 AA.
AC Q9ZWL6;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ethylene receptor;
DE EC=2.7.13.3;
DE AltName: Full=PE-ETR1;
GN Name=ETR1;
OS Passiflora edulis (Passion fruit).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Passifloraceae; Passiflora.
OX NCBI_TaxID=78168;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9891418; DOI=10.1093/oxfordjournals.pcp.a029322;
RA Mita S., Kawamura S., Yamawaki K., Nakamura K., Hyodo H.;
RT "Differential expression of genes involved in the biosynthesis and
RT perception of ethylene during ripening of passion fruit (Passiflora edulis
RT Sims).";
RL Plant Cell Physiol. 39:1209-1217(1998).
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: Higher expression in arils than in seeds.
CC -!- DEVELOPMENTAL STAGE: Constitutive expression during 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; AB015496; BAA37136.1; -; mRNA.
DR AlphaFoldDB; Q9ZWL6; -.
DR SMR; Q9ZWL6; -.
DR BRENDA; 2.7.13.3; 4556.
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_0000081419"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
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..730
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 738 AA; 82684 MW; 0B2423DD83554080 CRC64;
MESCNCIEPQ WPAEELLMKY QYISDFFIAL AYFSIPLELI YFVKKSAVFP YRWVLVQFGA
FIVLCGATHL INLWTFTMHS RTVATVMTIA KVLTAVVSCA TALMLVHIIP DLLSVKTREL
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILRTTLVEL GRTLALEECA
LWMPTRTGLE LQLSYTLRQQ NPVGYTVPIQ LPVINQVFST NRAVKISPNC PVARLRPLAG
KYVPGEVVAV RVPLLHLNNF QINDWPELST RRYALMVLML PSDSARQWRV HELELVEVVA
DQVAVALSHA AILEESMRAR DLLMEQNVAL DLARREAETA IRARNDFLAV MNHEMRTPMH
AVIALSSLLQ ETELTPEQRL MVETILKSSN LLATLINDVL DLSKLEDGSL QLDSGTFNLH
AVFREVLNLI KPIASVKKLL LLLNLAPDLP EYAVGDEKRL IQIILNIVGN AMKFSKEGSI
SITAIVAKLE SLRDARVPDF FPTPSENHFY LRVQVKDSGV GINPQDIPKL FIKFAQTQTT
GARNSSGSGL GLAICRRFVN LMDGHIWLES EGLGKGCTAI FIVKLGIPER LNESKPPFMS
KVAVDHGQTT FPGLKVLLMD DNGVSRMVTK GLLLHLGCDV TTVGSSEECI RVASQDHRVV
FMDVGMPEGF EAAVRLHEKF TKRHERPLVV ALTASTDRMT KENCMRVGMD GAILKPVSVD
KMRSVLSDLL EHKVLFEC
