ID A0A3B6QL29_WHEAT Unreviewed; 728 AA.
AC A0A3B6QL29;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ethylene receptor {ECO:0000256|PIRNR:PIRNR026389};
GN ORFNames=CFC21_093911 {ECO:0000313|EMBL:KAF7091312.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS6D02G308300.1};
RN [1] {ECO:0000313|EMBL:KAF7091312.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7091312.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS6D02G308300.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6D02G308300.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS6D02G308300.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7091312.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7091312.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR026389}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|PIRSR:PIRSR026389-2};
CC Note=Binds 1 copper ion per dimer. {ECO:0000256|PIRSR:PIRSR026389-2};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ethylene receptor family.
CC {ECO:0000256|ARBA:ARBA00009842, ECO:0000256|PIRNR:PIRNR026389}.
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DR EMBL; CM022228; KAF7091312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6QL29; -.
DR SMR; A0A3B6QL29; -.
DR STRING; 4565.A0A3B6QL29; -.
DR PaxDb; 4565-Traes_6DL_50AA014D7-1; -.
DR EnsemblPlants; TraesCS6D02G308300.1; TraesCS6D02G308300.1; TraesCS6D02G308300.
DR Gramene; TraesCAD_scaffold_054183_01G000300.1; TraesCAD_scaffold_054183_01G000300.1; TraesCAD_scaffold_054183_01G000300.
DR Gramene; TraesCLE_scaffold_049344_01G000200.1; TraesCLE_scaffold_049344_01G000200.1; TraesCLE_scaffold_049344_01G000200.
DR Gramene; TraesCS6D02G308300.1; TraesCS6D02G308300.1; TraesCS6D02G308300.
DR Gramene; TraesCS6D03G0720800.1; TraesCS6D03G0720800.1.CDS; TraesCS6D03G0720800.
DR Gramene; TraesKAR6D01G0316150.1; cds.TraesKAR6D01G0316150.1; TraesKAR6D01G0316150.
DR Gramene; TraesPAR_scaffold_055066_01G000200.1; TraesPAR_scaffold_055066_01G000200.1; TraesPAR_scaffold_055066_01G000200.
DR Gramene; TraesROB_scaffold_054090_01G000300.1; TraesROB_scaffold_054090_01G000300.1; TraesROB_scaffold_054090_01G000300.
DR Gramene; TraesWEE_scaffold_047630_01G000300.1; TraesWEE_scaffold_047630_01G000300.1; TraesWEE_scaffold_047630_01G000300.
DR OMA; RSCAVWM; -.
DR Proteomes; UP000019116; Chromosome 6D.
DR Proteomes; UP000815260; Chromosome 6D.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR014525; ETR.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24423:SF628; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24423; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR PIRSF; PIRSF026389; Ethyln_sen_HK; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR026389};
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRNR:PIRNR026389};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR026389-3};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR026389};
KW Ethylene signaling pathway {ECO:0000256|ARBA:ARBA00022745,
KW ECO:0000256|PIRNR:PIRNR026389};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR026389};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR026389};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR026389,
KW ECO:0000256|PIRSR:PIRSR026389-2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR026389};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR026389};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR026389};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR026389}.
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 610..726
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT MOD_RES 661
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT DISULFID 22
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-3"
FT CROSSLNK 711
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-4"
SQ SEQUENCE 728 AA; 78405 MW; E0FEF8E26018CEB3 CRC64;
MARHFAAAGA GAVQRYYCGG ACDGGDDGAV QAMLQCQRVS DFLIAASYLS IPLELLYFAS
CADPAPLKWL LLQLAAFAVL GGATHLLAVF SLAHPHSSGL LLASTAAKLL AALVSFATAV
SLVALIPRLI RAKLREAFLR AKARQLDHDL GLIRRRVEAT SRVVRMLTHR IRSSPLDAHS
ILHTTMLHLA DALELHSCAV WMPGRDAGDD LHLVHQLSLR GKGPVRIVLG SQAPISPDDP
DVLDVMASEA AKVLRPGSEL ATASSGELQP PGAVAAIRIP MLKVSNFDGR KTPVASSYAI
LVMALRSKAS GSGSREWSGH DLEVVQVIAD QVAVALSHAA VLEEWQAMSD RLAEQNRALV
HAKQDAMMAT EGINSIQSAM CDGMRRPMYS IIGLLSMVRQ AEDMRPEQRL VADAIARTST
LSLALMNDVD RETLTVNRMP FDLRSLMREA MSVAGCLASC GGAGFSYQLE NALPEWVVGD
ETRVFHLLLQ MAGDVLGRRR DGAGRLSFSI KSCSADQKDC IPVWPNLSAG CSICVEFQVA
MERSTGCSQP PSSPAGSQIN MCKKIVQMMN GTMWSASDGE SITLILHFQL QQSRACRRTS
SSIPHFNGLR ILLAEGDRMS RAVTQKLLEQ LGCQAISVSS GAHCLALLGS AGSSFQLLLL
DLDMDAFEVA LQIRGLKNRR WLLIVAALAV TVDDSIREMC RHSGINGLIQ KPLTLTALGA
QLHRVLRN
//
