ETR2_SOLLC
ID ETR2_SOLLC Reviewed; 736 AA.
AC O49187; Q41343;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ethylene receptor 2;
DE Short=LeETR2;
DE EC=2.7.13.3;
GN Name=ETR2;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Rutgers; TISSUE=Root;
RX PubMed=9721682; DOI=10.1046/j.1365-313x.1998.00202.x;
RA Lashbrook C.C., Tieman D.M., Klee H.J.;
RT "Differential regulation of the tomato ETR gene family throughout plant
RT development.";
RL Plant J. 15:243-252(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-736.
RC STRAIN=cv. UC82B;
RA Zhou D., Mattoo A.K., Tucker M.L.;
RT "Molecular cloning of a tomato cDNA encoding an ethylene receptor.";
RL (er) Plant Gene Register PGR96-015(1996).
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: Leaves, flowers and fruits.
CC -!- DEVELOPMENTAL STAGE: Induced in imbibing seeds prior to germination and
CC down-regulated in elongating seedlings and senescing leaf petioles.
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; AF043085; AAC02214.1; -; mRNA.
DR EMBL; U47279; AAB39386.1; -; mRNA.
DR PIR; T06271; T06271.
DR RefSeq; NP_001234153.2; NM_001247224.2.
DR AlphaFoldDB; O49187; -.
DR SMR; O49187; -.
DR STRING; 4081.Solyc07g056580.2.1; -.
DR PaxDb; O49187; -.
DR GeneID; 606299; -.
DR KEGG; sly:606299; -.
DR eggNOG; KOG0519; Eukaryota.
DR InParanoid; O49187; -.
DR OrthoDB; 199912at2759; -.
DR BRENDA; 2.7.13.3; 3101.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; O49187; baseline and differential.
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..736
FT /note="Ethylene receptor 2"
FT /id="PRO_0000081417"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
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"
FT CONFLICT 474
FT /note="K -> E (in Ref. 2; AAB39386)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 736 AA; 81701 MW; A804C61EBC190320 CRC64;
MDCNCFDPLL PADELLMKYQ YISDFFIAVA YFSIPIELVY FVQKSAVFPY RWVLVQFGAF
IVLCGATHLI NLWTSTPHTR TVAMVMTTAK FSTAAVSCAT AVMLVHIIPD LLSVKTRELF
LKNKAAELDR EMGLIRTQEE TGRYVRMLTH EIRSTLDRHT ILKTTLVELG RALQLEECAL
WMPTRTGVEL QLSYTLHHQN PVGFTVPIQL PVINQVFSAN CAVKISPNSA VARLRPTRKY
IPGEVVAVRV PLLHLSNFQT NDWPELSPKS YALMVLMLPS NSARQWHVHE LELVDVVADQ
VAVALSHAAI LEESMRARDL LIEQNVALDL ARREAETAVR ARNDFLGVMN HEMRTPMHAV
VALSSLLQES ELIPEQRLMV ETILKSSNLL ATLINDVLDL SRLEDGSLQL DVGTFNLHAL
FREVLNLIKP VAAVKKLFVT LSLSSDFPEV AIGDEKRLMQ ILLNVVGNAV KFSKEGSVSV
SAVNAKSESL IDPRAPEFFP VQSENHFYLR VQVKDTGSGI NPQDFPKLFC KFAQNQEPAT
KNSAGTGLGL AICKRFVNLM EGHIWIESEG VGKGSTAIFI VKLGIPGRLN ESKLPFTAGL
PANHMQMTFQ GLKVLVMDDN GFSRMVTKSL LVHLGCDVTT IGSGDECLRI LTREHKVLIM
DASITGMNCY DVAVSVHEKF GKRLERPLIV ALTGNTDQVT KENCLRVGMD GVILKPVSID
KMRSVLSGLL EHGTVL
