ERS1_ORYSI
ID ERS1_ORYSI Reviewed; 636 AA.
AC A2XL32; O24176; Q7EWE2;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable ethylene response sensor 1 {ECO:0000305};
DE Short=OS-ERS1 {ECO:0000303|PubMed:14754915};
DE EC=2.7.13.3 {ECO:0000305};
DE AltName: Full=Ethylene response factor 1 {ECO:0000303|PubMed:14754915};
GN Name=ERS1; Synonyms=OSERS {ECO:0000312|EMBL:AAB72193.1};
GN ORFNames=OsI_13175 {ECO:0000312|EMBL:EAY91542.1};
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.
RA Yau C.P., Yip W.K.;
RT "Nucleotide sequence of a full-length cDNA encoding an ethylene receptor
RT from rice.";
RL (er) Plant Gene Register PGR97-134(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [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 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 -!- 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: Highly expressed in anthers and at lower levels in
CC roots, mature leaves and hulls. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
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DR EMBL; AF013979; AAB72193.1; -; mRNA.
DR EMBL; AY043031; AAK77941.1; -; Genomic_DNA.
DR EMBL; CM000128; EAY91542.1; -; Genomic_DNA.
DR PIR; T03439; T03439.
DR AlphaFoldDB; A2XL32; -.
DR SMR; A2XL32; -.
DR STRING; 39946.A2XL32; -.
DR iPTMnet; A2XL32; -.
DR PRIDE; A2XL32; -.
DR EnsemblPlants; BGIOSGA009973-TA; BGIOSGA009973-PA; BGIOSGA009973.
DR Gramene; BGIOSGA009973-TA; BGIOSGA009973-PA; BGIOSGA009973.
DR HOGENOM; CLU_000445_114_48_1; -.
DR OMA; CRCLLYR; -.
DR Proteomes; UP000007015; Chromosome 3.
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..636
FT /note="Probable ethylene response sensor 1"
FT /id="PRO_0000433862"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 158..307
FT /note="GAF"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT DOMAIN 350..587
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 615..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT MOD_RES 353
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DISULFID 4
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT DISULFID 6
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P49333"
FT CONFLICT 535
FT /note="A -> P (in Ref. 1; AAB72193 and 2; AAK77941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 70683 MW; A66DA65A7A48B9E8 CRC64;
MDGCDCIEPL WPTDELLIKY QYISDFFIAL AYFSIPLELI YFVKKSSFFP YRWVLIQFGA
FIVLCGATHL INLWTFTTHT KTVAMVMTVA KVSTAVVSCA TALMLVHIIP DLLSVKTREL
FLKNKAEQLD REMGLIRTQE ETGRHVRMLT HEIRSTLDRH TILKTTLVEL GGTLGLEECA
LWMPSRSGSS LQLSHTLRHQ ITVGSTVSIN LPVVNQVFSS NRAIIIPHTS PLARIRPLAG
RYVPPEVAAV RVPLLHLSNF QINDWPELSA KSYAIMVLML PSDSARKWHV HELELVEVVA
DQVAVALSHA AILEESMRAR DLLMEQNVAL DLARREAEMA IRARNDFLAV MNHEMRTPMN
AIIALSSLLL ETELTPEQRL MVETVLKSSN LLATLINDVL DLSKLEDGSL ELEIKAFNLH
AVFKEVMSFI KPIAAIKRLS VSVMLAPDLP LCAIGDEKRL MQTILNISGN AVKFTKEGHI
TLVASVVKAD SLREFRTPDF HPTASDDNFY LKVQIKDTGC GISPQDLPQV FTKFAQSQPG
GNRGYSGSGL GLAICKRFVT LMGGHIWLDS EGTGRGCTVT FVIQLGICDN TNAYQQKLIP
LVWPSSGDAD FVGPVPNAPN EEKGQASLKS RYQRSI
