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Database: UniProt
Entry: K3Z066_SETIT
LinkDB: K3Z066_SETIT
Original site: K3Z066_SETIT 
ID   K3Z066_SETIT            Unreviewed;       771 AA.
AC   K3Z066;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Ethylene receptor {ECO:0000256|PIRNR:PIRNR026389};
GN   Name=101758978 {ECO:0000313|EnsemblPlants:KQL32162};
GN   ORFNames=SETIT_1G370200v2 {ECO:0000313|EMBL:RCV08977.1};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV08977.1};
RN   [1] {ECO:0000313|EMBL:RCV08977.1, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL32162,
RC   ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC   {ECO:0000313|EMBL:RCV08977.1};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EMBL:RCV08977.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Yugu1 {ECO:0000313|EMBL:RCV08977.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQL32162}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL32162};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR   EMBL; AGNK02000605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM003528; RCV08977.1; -; Genomic_DNA.
DR   RefSeq; XP_004954424.1; XM_004954367.3.
DR   RefSeq; XP_004954427.1; XM_004954370.3.
DR   RefSeq; XP_012698320.1; XM_012842866.2.
DR   RefSeq; XP_012698323.1; XM_012842869.2.
DR   RefSeq; XP_012698326.1; XM_012842872.1.
DR   AlphaFoldDB; K3Z066; -.
DR   STRING; 4555.K3Z066; -.
DR   EnsemblPlants; KQL32162; KQL32162; SETIT_019927mg.
DR   GeneID; 101758978; -.
DR   Gramene; KQL32162; KQL32162; SETIT_019927mg.
DR   KEGG; sita:101758978; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_000445_114_48_1; -.
DR   InParanoid; K3Z066; -.
DR   OMA; MEMSADS; -.
DR   OrthoDB; 1770905at2759; -.
DR   Proteomes; UP000004995; Chromosome I.
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: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   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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR24423:SF624; ETHYLENE RECEPTOR 3; 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; 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   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   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR026389};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004995};
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|ARBA:ARBA00023012,
KW   ECO:0000256|PIRNR:PIRNR026389}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..771
FT                   /note="Ethylene receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010127331"
FT   TRANSMEM        72..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          652..768
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          352..379
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         112
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT   BINDING         116
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026389-2"
FT   CROSSLNK        753
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026389-4"
SQ   SEQUENCE   771 AA;  85443 MW;  4EBB06C36D65ED71 CRC64;
     MLWPRFRCPS RRHFPPISMR RLLLLVLAAA PAAATAGEMG YTHCACDGGG GGGGGGFWSL
     DNIFKWQKVS DLLIAAAYFS IPLELLYFVA GLRHLLPFRW VLVQFGAFIV LCGLTHLLAA
     FTYEPHPFMV VLLLTAAKFL TALVSFLTAI TLLTLIPQLL RVKVRESLLW IKAHELDREV
     VLMKRQEEAS WHVRMLTQEI RRSLDRHTVL YTTLIELSRV LALNNCAVWM PSEDKSGMCL
     THELRRGSDG EAIVSADDAD VLKVKGSDGV KLLPPESVLG SASGGGKEGT GTVAAIRMPM
     LKVADFKGGT PEVIQTSYAV LVLVPPSDRN WAPHELEIVE VVADQVAVAL SHASLLEESQ
     AMRDRLAEQN RELLQARRDT LMANEARDAF QRVMSQGMRK PIHSILGLVS VVQEEGLTSE
     QKLVIDTMAR TATVVSTLIN DVMEMSAVNQ ERFPLETRPF HLHSMIRDAA CVARCLCDFR
     GFGFTVHVEN TLPDLVIGDE RRIFHVLLHM VGNLIGRINA GNVTFRVRAD DEAMEDQRWD
     PWRPSYSGGH SSVKFVIGVK RQESADSSSS LAQFLRKPST EGFDLRLSFS MCRKLVQMMQ
     GNIWAILDGQ GLPESMTLVL RFQLQPSLSG SSLRGSFDLQ YPSPSSQIAG LKVLLIDDDD
     INLVVARKLL EKLGCTVSSL PSGSGFMNSV GPTSTLFQLV VVNLEITAVN PLDVASRIRQ
     YRSTQWPLVM TMTSEHNVWE KCAQSGINGV LKKPLVLQEI KDELTRILQN T
//
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