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Database: UniProt
Entry: Q6T5K3
LinkDB: Q6T5K3
Original site: Q6T5K3 
ID   ETR4_ORYSI              Reviewed;         777 AA.
AC   Q6T5K3;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Ethylene receptor 4 {ECO:0000305};
DE            Short=OS-ETR4 {ECO:0000303|PubMed:14754915};
DE            EC=2.7.13.3 {ECO:0000305};
GN   Name=ETR4 {ECO:0000312|EMBL:AAR08914.1};
GN   ORFNames=OsI_25565 {ECO:0000312|EMBL:EAZ03426.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. IR36;
RX   PubMed=14754915; DOI=10.1093/jxb/erh055;
RA   Yau C.P., Wang L., Yu M., Zee S.Y., Yip W.K.;
RT   "Differential expression of three genes encoding an ethylene receptor in
RT   rice during development, and in response to indole-3-acetic acid and silver
RT   ions.";
RL   J. Exp. Bot. 55:547-556(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Ethylene receptor related to bacterial two-component
CC       regulators. Acts as a redundant negative regulator of ethylene
CC       signaling. {ECO:0000250|UniProtKB:P49333}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P49333};
CC       Note=Binds 1 copper ion per dimer. {ECO:0000250|UniProtKB:P49333};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P49333}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
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DR   EMBL; AY434734; AAR08914.1; -; mRNA.
DR   EMBL; CM000132; EAZ03426.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6T5K3; -.
DR   STRING; 39946.Q6T5K3; -.
DR   EnsemblPlants; BGIOSGA024506-TA; BGIOSGA024506-PA; BGIOSGA024506.
DR   Gramene; BGIOSGA024506-TA; BGIOSGA024506-PA; BGIOSGA024506.
DR   HOGENOM; CLU_000445_114_48_1; -.
DR   OMA; ACAVWMP; -.
DR   Proteomes; UP000007015; Chromosome 7.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16938; HATPase_ETR2_ERS2-EIN4-like; 1.
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; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR24423:SF618; ETHYLENE RECEPTOR 4; 1.
DR   PANTHER; PTHR24423; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00072; Response_reg; 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   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Copper; Endoplasmic reticulum; Ethylene signaling pathway;
KW   Kinase; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Receptor; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..777
FT                   /note="Ethylene receptor 4"
FT                   /id="PRO_0000433870"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          184..344
FT                   /note="GAF"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          387..521
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          645..774
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   BINDING         88
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P49333"
FT   BINDING         92
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P49333"
FT   MOD_RES         390
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         696
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   777 AA;  83327 MW;  399D1684558AC117 CRC64;
     MAMVTARQFL ASAAELGSGR RRCGGGGACD MREDGGVEAL MQCQRVSNLL IAASFLSIPL
     ELFYFATCAD LSEVKCAVLH FCAFIVLCGA THLLAAFTHA HPHSAPLLRA LTAAKVLAAV
     ASSAAAVSLL TFIPKLLRIK VRESLLRDKA SRLHRDLGLV RRREEATSRA VRELTGRIRA
     SPPDAHAILR TTALQLADAL GLHACAVWMP AAGRPHDLVL VHHLTSRPDD AADLLLEVGD
     ACTVAADDPD VVDVMASKVA KVLEPDSALA MASSVGAAPA GAVAAIRIPI LRVSIYDGGG
     TPEVTEASYA ILVLLLPPHD AAGGWSSHDL EIVQVVADQA AVALSHAAVL EESRSMRDRF
     AEQHRALMQA KHRAAMATRA FSSIQSAMCH AMRRPVHSIV GLVSMLQHPE ADTMRPEQRL
     AVDAIARTSN LLSALMDEVI VNRQHLSVQR KPFSLHALIK EAISVAGCLS HCGGAGFLHQ
     LECALPEWVV GDERRVFHLL LDMVGTLLNR CNTESGACRL SFSIRICNVG EERYSLDWIP
     MRPTFSGCNV CVKFKVGIGR SRSCAIERSL PCELPRRSAA TTSSQMGHIF SGYFNKIVQM
     MNGNMWSASD SEGVGESVTL ILQFKLQQGH VEASPPYIPH LNGLRVLLAD DDAMNRGVTK
     KILERLGCQV MSAPSGAHCL SLLASAEASF QLVVLDLDDR AVPSAAMDGF EVALRIRELR
     YSCWLLIVIA VAAGVVATDD GGAVQELCQR AGINGLVQKP VTLPALGAQL CRVLQDN
//
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