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ERS2_ORYSI
ID   ERS2_ORYSI              Reviewed;         635 AA.
AC   B8AY75; Q8W129;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable ethylene response sensor 2 {ECO:0000305};
DE            Short=OS-ERS2 {ECO:0000303|PubMed:14754915};
DE            EC=2.7.13.3 {ECO:0000305};
DE   AltName: Full=Ethylene response factor 2 {ECO:0000303|PubMed:14754915};
GN   Name=ERS2 {ECO:0000312|EMBL:AAL66363.1};
GN   ORFNames=OsI_18521 {ECO:0000312|EMBL:EEC78552.1};
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], AND TISSUE SPECIFICITY.
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 negative regulator of ethylene signaling. May play
CC       a role in the regulation of flowering by up-regulating GI (GIGANTEA)
CC       and RCN1 and regulate starch accumulation by down-regulating the alpha-
CC       amylase AMY3D. {ECO:0000250|UniProtKB:Q0DKM0}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49333}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P49333}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in anthers and hulls.
CC       {ECO:0000269|PubMed:14754915}.
CC   -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
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DR   EMBL; AF460181; AAL66363.1; -; mRNA.
DR   EMBL; CM000130; EEC78552.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8AY75; -.
DR   SMR; B8AY75; -.
DR   STRING; 39946.B8AY75; -.
DR   EnsemblPlants; BGIOSGA018780-TA; BGIOSGA018780-PA; BGIOSGA018780.
DR   Gramene; BGIOSGA018780-TA; BGIOSGA018780-PA; BGIOSGA018780.
DR   HOGENOM; CLU_000445_114_48_1; -.
DR   OMA; HLADWCL; -.
DR   Proteomes; UP000007015; Chromosome 5.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
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   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Copper; Disulfide bond; Endoplasmic reticulum;
KW   Ethylene signaling pathway; Kinase; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..635
FT                   /note="Probable ethylene response sensor 2"
FT                   /id="PRO_0000433864"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          159..308
FT                   /note="GAF"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          351..589
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   BINDING         66
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P49333"
FT   BINDING         70
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P49333"
FT   MOD_RES         354
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DISULFID        5
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P49333"
FT   DISULFID        7
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P49333"
FT   CONFLICT        345
FT                   /note="R -> C (in Ref. 1; AAL66363)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="V -> M (in Ref. 1; AAL66363)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        491
FT                   /note="D -> H (in Ref. 1; AAL66363)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        510
FT                   /note="F -> L (in Ref. 1; AAL66363)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   635 AA;  70458 MW;  E6F5DBD007582413 CRC64;
     MDGSCDCIEP LWQADDLLVK YQYISDFFIA LAYFSIPLEL IYFVKKSAFF PYRWVLIQFG
     AFIVLCGATH LINLWTFAIY TKTIAVVLTV AKAATAVVSC ITALMLVHII PDLLNVKLRE
     RFLKDKADEL DREMGIIRTQ EETGRHVHML THEIRSTLDR HTILRTTLVE LGRTLALAEC
     ALWMPTRSGS ALQLSHTIYN SAAIGSVVPI NLPIVSKVFN SNRVVKIPHT SPLASITADK
     SRYVPPEVVA IRVPLLHLTN FQINDWPELS AKSFAVMVLM LPPDSAREWR PHERELVEVV
     ADQVAVALSH AAILEESMRA RDLLMEQNIA LDAARREAEM AICARNDFLA VMNHEMRTPM
     RAIVSLSSLL LETNLSAEQR LMVETILKSS DLLATLTNDV LDVSKLENGS LELEIAPFNL
     HSTFTDVVNL IKPVAACKRL SVVVTLAPEL PLHAIGDQKR LMQIILNVAG NSIKFTKEGH
     VSITASMARP DALRGPHEPD YHPVVSDGFF YLAVQVKDTG CGISPQDMPH TFRKFAHPEN
     AGKWNSGSGL GLALSRRFVS LMEGNIWLES EGVGKGCTAM FFVKLGMPEK PNANLRRMAP
     HPLQPNQGAG GPDALSISIM DSNPRVPRVR YQSSV
 
 
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