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ERS1_ORYSJ
ID   ERS1_ORYSJ              Reviewed;         636 AA.
AC   Q53RH0; A0A0N7KHW3;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Probable ethylene response sensor 1 {ECO:0000305};
DE            Short=OsERS1 {ECO:0000303|PubMed:16891544};
DE            EC=2.7.13.3 {ECO:0000305};
DE   AltName: Full=Ethylene response factor 1 {ECO:0000303|PubMed:16891544};
GN   Name=ERS1;
GN   OrderedLocusNames=Os03g0701700 {ECO:0000312|EMBL:BAF12918.1},
GN   LOC_Os03g49500 {ECO:0000312|EMBL:ABF98410.1};
GN   ORFNames=OsJ_12251 {ECO:0000312|EMBL:EAZ28278.1};
OS   Oryza sativa subsp. japonica (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=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
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).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   TISSUE SPECIFICITY, AND INDUCTION.
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   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16891544; DOI=10.1104/pp.106.086371;
RA   Pareek A., Singh A., Kumar M., Kushwaha H.R., Lynn A.M.,
RA   Singla-Pareek S.L.;
RT   "Whole-genome analysis of Oryza sativa reveals similar architecture of two-
RT   component signaling machinery with Arabidopsis.";
RL   Plant Physiol. 142:380-397(2006).
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, leaves and hulls. {ECO:0000269|PubMed:14754915}.
CC   -!- INDUCTION: Repressed by treatment with silver.
CC       {ECO:0000269|PubMed:14754915}.
CC   -!- DISRUPTION PHENOTYPE: Dwarf, chlorina and half sterility phenotypes.
CC       {ECO:0000269|PubMed:16891544}.
CC   -!- SIMILARITY: Belongs to the ethylene receptor family. {ECO:0000305}.
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DR   EMBL; AC091670; AAX95525.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF98410.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF98411.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF12918.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS85937.1; -; Genomic_DNA.
DR   EMBL; CM000140; EAZ28278.1; -; Genomic_DNA.
DR   EMBL; AK065161; BAG89392.1; -; mRNA.
DR   EMBL; AK067813; BAG90616.1; -; mRNA.
DR   RefSeq; XP_015631949.1; XM_015776463.1.
DR   AlphaFoldDB; Q53RH0; -.
DR   SMR; Q53RH0; -.
DR   STRING; 4530.OS03T0701700-02; -.
DR   PaxDb; Q53RH0; -.
DR   PRIDE; Q53RH0; -.
DR   EnsemblPlants; Os03t0701700-01; Os03t0701700-01; Os03g0701700.
DR   EnsemblPlants; Os03t0701700-02; Os03t0701700-02; Os03g0701700.
DR   GeneID; 4333832; -.
DR   Gramene; Os03t0701700-01; Os03t0701700-01; Os03g0701700.
DR   Gramene; Os03t0701700-02; Os03t0701700-02; Os03g0701700.
DR   KEGG; osa:4333832; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_000445_114_48_1; -.
DR   InParanoid; Q53RH0; -.
DR   OMA; CRCLLYR; -.
DR   OrthoDB; 199912at2759; -.
DR   PlantReactome; R-OSA-5225756; Ethylene mediated signaling.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; Q53RH0; OS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0038199; F:ethylene receptor activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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_0000433861"
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:0000305"
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"
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
 
 
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