ETR1_TOBAC
ID ETR1_TOBAC Reviewed; 738 AA.
AC O48929;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ethylene receptor;
DE EC=2.7.13.3;
DE AltName: Full=NT-ETR1;
GN Name=ETR1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun NN; TISSUE=Leaf;
RA Knoester M., Hennig J., van Loon L.C., Bol J.F., Linthorst H.J.M.;
RT "Isolation and characterization of a tobacco cDNA encoding an ETR1
RT homolog.";
RL (er) Plant Gene Register PGR97-188(1997).
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 -!- INDUCTION: Constitutive expression. Not induced by senescence,
CC wounding, application of ethephon or infection with virus.
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; AF022727; AAB97160.1; -; mRNA.
DR PIR; T01897; T01897.
DR AlphaFoldDB; O48929; -.
DR SMR; O48929; -.
DR STRING; 4097.O48929; -.
DR BRENDA; 2.7.13.3; 3645.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0038199; F:ethylene receptor activity; IBA:GO_Central.
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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..738
FT /note="Ethylene receptor"
FT /id="PRO_0000081423"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 157..305
FT /note="GAF"
FT DOMAIN 348..585
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 613..730
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT MOD_RES 351
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 661
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DISULFID 3
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 5
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 738 AA; 82294 MW; D6C5F7B16F16A7DE CRC64;
MDCNCFDPQW PADELLMKYQ YISDFFIAVA YFSIPIELVY FVQKSAVFPY RWVLVQFGAF
IVLCGATHLI NLWTSTAHTR TLAIVMTTAK VLTAVVSCAT ALMLVHIIPD LLSVKTRELF
LKNKAAELDR EMGLIRTQEE TGRYVRMLTH EIRSTLDRHT ILKTTLVELG RTLALEECAL
WMPTPPGLEL QLSYTLRHQN PIGFTVPIQL PVINQVFGTN RAVKISPNSP VARLRPAGKY
MPGEVVAVRV PLLHLSNFQI NDWPELSTKR YALMVLMLPS GSARQWHVHE LELVEVVADQ
VAVALSHAAI LEESMRARDL LMEQNVALDL ARREAEMAVR ARNDFLAVMN HEMRTPMHAI
IALSSLLQET ELTPEQRLMV ETILKSSNLL ATLINDVLDL SRLEDGSLQL DVGTFNLHVL
FRKVLNLIKP IASVKNCLSR LTCLQICPEF AIGDEKRLMQ ILLNVVGNAV KFSKEGSVSI
SAVAAKSESL SDPRAPEFFP VQSENHFYLR VQVKDTGSGI NPQDIPKLFC KFAQNQALAT
KSSGGTGLGL AISKRFVNLM EGHIWIESEG LGKGSTAIFI VKLGIPGRSN EPKLPFMPRL
PANHMQMTFQ GLKVLIMDDN GFSRMVTKGL LVHLGCDVTT VSSGDECLRV LTQEHKVVFM
DVSIPGIDCY EVAVQIHEKF GKHHNRPLIV ALTGNTDRVT KENCMRVGMD GVILKPVSVD
KMRSVLSELL EHGVILQS
