ID K7LB30_SOYBN Unreviewed; 740 AA.
AC K7LB30;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Ethylene receptor {ECO:0000256|PIRNR:PIRNR026389};
GN Name=100795799 {ECO:0000313|EnsemblPlants:KRH36428};
GN ORFNames=GLYMA_09G002600 {ECO:0000313|EMBL:KRH36435.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH36435.1};
RN [1] {ECO:0000313|EMBL:KRH36435.1, ECO:0000313|EnsemblPlants:KRH36428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH36428};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH36435.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH36428}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH36428};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH36435.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH36435.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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|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; CM000842; KRH36428.1; -; Genomic_DNA.
DR EMBL; CM000842; KRH36429.1; -; Genomic_DNA.
DR EMBL; CM000842; KRH36430.1; -; Genomic_DNA.
DR EMBL; CM000842; KRH36431.1; -; Genomic_DNA.
DR EMBL; CM000842; KRH36432.1; -; Genomic_DNA.
DR EMBL; CM000842; KRH36433.1; -; Genomic_DNA.
DR EMBL; CM000842; KRH36434.1; -; Genomic_DNA.
DR EMBL; CM000842; KRH36435.1; -; Genomic_DNA.
DR EMBL; CM000842; KRH36436.1; -; Genomic_DNA.
DR RefSeq; XP_003534452.1; XM_003534404.3.
DR RefSeq; XP_006586744.1; XM_006586681.2.
DR RefSeq; XP_006586745.1; XM_006586682.2.
DR RefSeq; XP_006586746.1; XM_006586683.2.
DR RefSeq; XP_006586747.1; XM_006586684.2.
DR RefSeq; XP_006586748.1; XM_006586685.2.
DR RefSeq; XP_014617302.1; XM_014761816.1.
DR RefSeq; XP_014617303.1; XM_014761817.1.
DR AlphaFoldDB; K7LB30; -.
DR SMR; K7LB30; -.
DR STRING; 3847.K7LB30; -.
DR PaxDb; 3847-GLYMA09G00490-2; -.
DR EnsemblPlants; KRH36428; KRH36428; GLYMA_09G002600.
DR EnsemblPlants; KRH36429; KRH36429; GLYMA_09G002600.
DR EnsemblPlants; KRH36430; KRH36430; GLYMA_09G002600.
DR EnsemblPlants; KRH36431; KRH36431; GLYMA_09G002600.
DR EnsemblPlants; KRH36432; KRH36432; GLYMA_09G002600.
DR EnsemblPlants; KRH36433; KRH36433; GLYMA_09G002600.
DR EnsemblPlants; KRH36434; KRH36434; GLYMA_09G002600.
DR EnsemblPlants; KRH36435; KRH36435; GLYMA_09G002600.
DR EnsemblPlants; KRH36436; KRH36436; GLYMA_09G002600.
DR GeneID; 100795799; -.
DR Gramene; KRH36428; KRH36428; GLYMA_09G002600.
DR Gramene; KRH36429; KRH36429; GLYMA_09G002600.
DR Gramene; KRH36430; KRH36430; GLYMA_09G002600.
DR Gramene; KRH36431; KRH36431; GLYMA_09G002600.
DR Gramene; KRH36432; KRH36432; GLYMA_09G002600.
DR Gramene; KRH36433; KRH36433; GLYMA_09G002600.
DR Gramene; KRH36434; KRH36434; GLYMA_09G002600.
DR Gramene; KRH36435; KRH36435; GLYMA_09G002600.
DR Gramene; KRH36436; KRH36436; GLYMA_09G002600.
DR KEGG; gmx:100795799; -.
DR eggNOG; KOG0519; Eukaryota.
DR InParanoid; K7LB30; -.
DR OMA; TKSHERP; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000008827; Chromosome 9.
DR ExpressionAtlas; K7LB30; 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: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: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 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; 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 PANTHER; PTHR24423:SF615; ETHYLENE RECEPTOR 1; 1.
DR PANTHER; PTHR24423; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
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; 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 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|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR026389};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
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 TRANSMEM 26..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 350..587
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 615..731
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT BINDING 65
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT BINDING 470..473
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-1"
FT BINDING 517
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-1"
FT BINDING 533
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-1"
FT BINDING 548
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-1"
FT BINDING 552
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-1"
FT MOD_RES 663
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT DISULFID 4
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-3"
FT DISULFID 6
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-3"
FT CROSSLNK 716
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR026389-4"
SQ SEQUENCE 740 AA; 82693 MW; 8DC9B5E9983AF657 CRC64;
MESCNCIDPQ VPADDLLMKY QYISDFFIAL AYFSIPLELI YFVKKSAVFP YRWVLVQFGA
FIVLCGATHL INLWTFRIHS RTVAVVMTTA KVLTAVVSCA TALMLVHIIP DLLSVKTREL
FLKNKAAELD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GRTLALEECA
LWMPTRTGLE LQLSYTLRQQ NPVGYTVPIH LPVINQVFSS NRAVKISPNC PVARLRPYAG
KYMPGAVVAV RVPLLHLSNF QIYDWPEVST RSYALMVLML PSDSARQWHV HELELVEVVA
DQVAVALSHA AILEESMRAR DQLMEQNVAL DLARREAETA IRARNDFLAV MNHEMRTPMH
AVIALSSLLQ ETDLTAEQRL MVETILKSSN LLATLINDVL DLSRLEDGSL QLEATTFNLH
SLFREVLNLI KPVASVKKLS LTSHIASDLP MYAIGDEKRL MQTILNVVGN AVKFSKEGCI
SISAFVAKPE SFRDARIPDF LPVLSDNHFY LRVQVKDSGS GINPQDIPKI FTKFAQNQSL
TTRNPAGSGL GLAICRRFVN LMEGHIWVES EGIGKGCTVT FIVKLGIPDR SNEFKLPFVP
KVPGNHGSTN FAGLKVLVTD DNGVSRTVTK GLLMHLGCDV TTASSSEECL RVVSLEHEVV
FMDVCAGLDG YELAIRIHEK FTKHQDRPLI VALTGNTKKV TKENCMRVGM DGLILKPVSV
DKMRGVLSEL LERRVLFETV
//
