ETR2_ORYSI
ID ETR2_ORYSI Reviewed; 763 AA.
AC Q8H1X1; A2XQB6;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ethylene receptor 2 {ECO:0000305};
DE Short=OS-ETR2 {ECO:0000303|PubMed:14754915};
DE EC=2.7.13.3 {ECO:0000305};
DE AltName: Full=OsETRL1 {ECO:0000312|EMBL:AAN15203.2};
DE AltName: Full=Protein ETYLENE RESPONSE 2-LIKE 1 {ECO:0000303|PubMed:15020633};
DE Short=Os-ERL1 {ECO:0000303|PubMed:15020633};
GN Name=ETR2 {ECO:0000312|EMBL:AAN15203.2};
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], TISSUE SPECIFICITY, AND INDUCTION BY ETHYLENE.
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 [MRNA], AND INDUCTION.
RC STRAIN=cv. Pin Gaew 56; TISSUE=Stem;
RX PubMed=15020633; DOI=10.1093/jxb/erh110;
RA Watanabe H., Saigusa M., Hase S., Hayakawa T., Satoh S.;
RT "Cloning of a cDNA encoding an ETR2-like protein (Os-ERL1) from deep water
RT rice (Oryza sativa L.) and increase in its mRNA level by submergence,
RT ethylene, and gibberellin treatments.";
RL J. Exp. Bot. 55:1145-1148(2004).
RN [3]
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 delay
CC the transition from the vegetative stage to the floral stage by up-
CC regulating GI (GIGANTEA) and RCN1 and cause starch accumulation in
CC stems by down-regulating the alpha-amylase AMY3D.
CC {ECO:0000250|UniProtKB:Q7XX84}.
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 -!- TISSUE SPECIFICITY: Expressed in anthers and hulls.
CC {ECO:0000269|PubMed:14754915}.
CC -!- INDUCTION: By ethylene and auxin (PubMed:14754915). Induced by
CC submergence, ethylene and gibberellin (PubMed:15020633).
CC {ECO:0000269|PubMed:14754915, ECO:0000269|PubMed:15020633}.
CC -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAY93026.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY136816; AAN15203.2; -; mRNA.
DR EMBL; AB107219; BAF51961.1; -; mRNA.
DR EMBL; CM000129; EAY93026.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q8H1X1; -.
DR STRING; 39946.Q8H1X1; -.
DR PRIDE; Q8H1X1; -.
DR Proteomes; UP000007015; Chromosome 4.
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: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:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 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; IPR001789; Sig_transdc_resp-reg_receiver.
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; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 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..763
FT /note="Ethylene receptor 2"
FT /id="PRO_0000433866"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 190..339
FT /note="GAF"
FT /evidence="ECO:0000305"
FT DOMAIN 382..615
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 641..760
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 97
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT BINDING 101
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT MOD_RES 692
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DISULFID 31
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT CONFLICT 351
FT /note="I -> M (in Ref. 2; BAF51961 and 1; AAN15203)"
FT CONFLICT 453
FT /note="L -> S (in Ref. 2; BAF51961 and 1; AAN15203)"
SQ SEQUENCE 763 AA; 84840 MW; 2A1B9837BFBA71CC CRC64;
MPPIPSLWIR VFFSWLLLSL PAAAAADFSH CGGCDDGDGG GGIWSTDNIL QCQRVSDFLI
AMAYFSIPLE LLYFATCSDL FPLKWIVLQF GAFIVLCGLT HLITMFTYEP HSFHVVLALT
VAKFLTALVS FATAITLLTL IPQLLRVKVR ENFLRIKARE LDREVGMMKR QEEASWHVRM
LTHEIRKSLD RHTILYTTMV ELSKTLELQN CAVWMPSESG SEMILTHQLR QMETEDSNSL
SIAMDNPDVL EIKATKDAKV LAADSALGIA SRGKLEAGPV AAIRMPMLKA SNFKGGTPEV
METSYAILVL VLPEDGSLGW GEEELEIVEV VADQVAVALS HAAVLEESQL IREKLAAQHR
DLLRAKHETT MATEARNSFQ TAMYDGMRRP MHSILGLVSM MQQENMNPEQ RLVMDAIVKT
SSVASTLMND VMQTSTVNRE YLSLVRRAFN LHLLVKEAIS VVRCLTGCKG IDFEFEVDNS
LPERVVGDEK RVFHIVLHMV GTLIQRCNAG CLSLYVNTYN EKEERHNQDW MLRRANFSGS
YVCVKFEIRI RESRGNLLSS SSSRRLQGPN STSSEMGLSF NMCKKIVQMM NGNIWSVSDS
KGLGETIMLA LQFQLQHVTP VSGASSDLFR SAPIPNFNGL QVILVDSDDT NRAVTHKLLE
KLGCLVLSVT SGIQCINSFA SAESSFQLVV LDLTMRTMDG FDVALAIRKF RGNCWPPLIV
ALAASTDDTV RDRCQQAGIN GLIQKPVTLA ALGDELYRVL QNN
