ETR1_SOLLC
ID ETR1_SOLLC Reviewed; 754 AA.
AC Q41342; O49186;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ethylene receptor 1;
DE Short=LeETR1;
DE EC=2.7.13.3;
GN Name=ETR1;
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=Abscission zone, and Fruit;
RX PubMed=8704141; DOI=10.1007/bf00019564;
RA Zhou D., Kalaitzis P., Mattoo A.K., Tucker M.L.;
RT "The mRNA for an ETR1 homologue in tomato is constitutively expressed in
RT vegetative and reproductive tissues.";
RL Plant Mol. Biol. 30:1331-1338(1996).
RN [2]
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).
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 -!- INTERACTION:
CC Q41342; B6GVA2: int106; NbExp=2; IntAct=EBI-2407792, EBI-2407896;
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: Expressed at all stages.
CC -!- INDUCTION: Constitutively expressed and accumulation not affected by
CC ethylene, silver ions or auxin.
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; U41103; AAA85479.1; -; mRNA.
DR EMBL; AF043084; AAC02213.1; -; mRNA.
DR PIR; S71783; S71783.
DR PIR; T52288; T52288.
DR RefSeq; NP_001234149.1; NM_001247220.2.
DR AlphaFoldDB; Q41342; -.
DR SMR; Q41342; -.
DR BioGRID; 2310725; 1.
DR IntAct; Q41342; 2.
DR STRING; 4081.Solyc12g011330.2.1; -.
DR PaxDb; Q41342; -.
DR GeneID; 606298; -.
DR KEGG; sly:606298; -.
DR eggNOG; KOG0519; Eukaryota.
DR InParanoid; Q41342; -.
DR OrthoDB; 199912at2759; -.
DR BRENDA; 2.7.13.3; 3101.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q41342; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
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 GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
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 1: Evidence at protein 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..754
FT /note="Ethylene receptor 1"
FT /id="PRO_0000081416"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 173..321
FT /note="GAF"
FT DOMAIN 364..601
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 629..746
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 80
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT MOD_RES 367
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 677
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DISULFID 18
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 20
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 105
FT /note="P -> A (in Ref. 2; AAC02213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 84202 MW; D7443B6517781D0A CRC64;
MGSLLRMNRL LSSIVESCNC IIDPQLPADD LLMKYQYISD FFIALAYFSI PVELIYFVKK
SAVFPYRWVL VQFGAFIVLC GATHLINLWT FNMHTRNVAI VMTTPKALTA LVSCITALML
VHIIPDLLSV KTRELFLKKK AAQLDREMGI IRTQEETGRH VRMLTHEIRS TLDRHTILKT
TLVELGRTLA LEECALWMPT RTGLELQLSY TLRHQNPVGL TVPIQLPVIN QVFGTNHVVK
ISPNSPVARL RPAGKYMPGE VVAVRVPLLH LSNFQINDWP ELSTKRYALM VLMLPSDSAR
QWHVHELELV EVVADQVAVA LSHAAILEES MRARDLLMEQ NVALDLARRE AEMAVRARND
FLAVMNHEMR TPMHAIIALS SLLQETDLTP EQRLMVETIL KSSNLLATLI NDVLDLSRLE
DGSLQLDIGT FNLHALFREV HSLIKPIASV KKLFVTLSLS SDLPEYVIGD EKRLMQILLN
VVGNAVKFSK EGNVSISAFV AKSDSLRDPR APEFFAVPSE NHFYLRVQIK DTGIGITPQD
IPNLFSKFTQ SQALATTNSG GTGLGLAICK RFVNLMEGHI WIESEGLGKG STAIFIIKLG
IPGRANESKL PFVTKLPANH TQMSFQGLKV LVMDENGVSR MVTKGLLTHL GCDVTTVGSR
DECLRVVTHE HKVVIMDVSM QGIDCYEVAV VIHERFGKRH GRPLIVALTG NTDRVTKENC
MRVGMDGVIL KPVSVYKMRS VLSELLEHGV VLES