ID V7BQ95_PHAVU Unreviewed; 759 AA.
AC V7BQ95;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Ethylene receptor {ECO:0000256|PIRNR:PIRNR026389};
GN ORFNames=PHAVU_006G106400g {ECO:0000313|EMBL:ESW19220.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW19220.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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|ARBA:ARBA00003286, ECO:0000256|PIRNR:PIRNR026389}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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 -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
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; CM002293; ESW19220.1; -; Genomic_DNA.
DR RefSeq; XP_007147226.1; XM_007147164.1.
DR AlphaFoldDB; V7BQ95; -.
DR STRING; 3885.V7BQ95; -.
DR EnsemblPlants; ESW19220; ESW19220; PHAVU_006G106400g.
DR GeneID; 18628417; -.
DR Gramene; ESW19220; ESW19220; PHAVU_006G106400g.
DR KEGG; pvu:PHAVU_006G106400g; -.
DR eggNOG; KOG0519; Eukaryota.
DR OMA; FNCCDED; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000000226; Chromosome 6.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0038199; F:ethylene receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IEA:UniProt.
DR CDD; cd16938; HATPase_ETR2_ERS2-EIN4-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19933; REC_ETR-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR014525; ETR.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24423:SF629; PROTEIN EIN4; 1.
DR PANTHER; PTHR24423; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF026389; Ethyln_sen_HK; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR026389};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRNR:PIRNR026389};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW 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|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR026389};
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:UP000000226};
KW Signal {ECO:0000256|SAM:SignalP};
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|PIRNR:PIRNR026389}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..759
FT /note="Ethylene receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004754774"
FT TRANSMEM 51..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 376..613
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 634..752
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 342..369
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 89
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT BINDING 93
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT MOD_RES 685
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT DISULFID 29
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-3"
FT DISULFID 31
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-3"
FT CROSSLNK 737
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-4"
SQ SEQUENCE 759 AA; 85134 MW; C7C1CD13D5B01DC0 CRC64;
MERGLLLFIF LLLVMVLSVF AIEVEYSHCN CDEEGLWSIH NVLVSQKVSD FFIAIAYFSI
PLELLYFVSR SNVPFKLVFL QFIAFIVLCG LTHLLNAYTY YGPHSFQLFL SLTVAKFLTA
LVSCATAISF PTLIPLLLKI KVRELFLRQN VLELGQEVGI MKKQKEASWH VRMLTCEIRK
SLDKHTILYT TLVELSKTLD LHNCAVWMPD DDRGEMLLTH ELKPNSASSF HNSIPISDPD
VLDIKKSKGV WILRPDSALG AASRGGGSGD SGAVAAIRMP ILHVSNFKGG TPELVETSYA
ILVLVLPNSN SRAWTSHEIE IVEVVADQVA VALSHASVLE ESQLMSQKLA EQNRALQHAQ
KNAMMARKAR SSFEKVMSHG MRRPMHSILG LLSMFQEDNI RPEQKIIIDS IFKVSNALSR
LINDVMEIST NDNGNFRLEM KPFNLHSMMR EVSCTTKCLC IYKGFGLEVD VDKTLPDLVA
GDEARSFQVI LHMIGYLLNI CDKGTLIFKV YLERSSGDKD DRSFGIWRSS MQNDYVHIKF
NFRINDISSQ SDESFSTANY SGRRHHNNEP KAGLSFSMCK TLVQMMQGNI WMSTNSLGVT
EGMTLLLRFP KGSSHGRSIL APKDFSNSQF RGLKVVLADD DDVNRTVTKK LLEKLGCQVT
AVSSGFECLG AISASGNSFK IILLDLHMPE MDGFEVARRI RKFQSRNWPL IVALTASAEE
HVKERCLQVG MNGLIQKPIL LHEIADELRT VLQRAGEKL
//
