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 07-APR-2021, entry version 110. 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 CC upregulating 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY136816; AAN15203.2; -; mRNA. DR EMBL; AB107219; BAF51961.1; -; mRNA. DR EMBL; CM000129; EAY93026.1; ALT_SEQ; Genomic_DNA. DR SMR; 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 METAL 97 FT /note="Copper" FT /evidence="ECO:0000250|UniProtKB:P49333" FT METAL 101 FT /note="Copper" 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 //