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EIL3_ARATH
ID   EIL3_ARATH              Reviewed;         567 AA.
AC   O23116;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=ETHYLENE INSENSITIVE 3-like 3 protein;
GN   Name=EIL3; OrderedLocusNames=At1g73730; ORFNames=F25P22.15;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=9215635; DOI=10.1016/s0092-8674(00)80300-1;
RA   Chao Q., Rothenberg M., Solano R., Roman G., Terzaghi W., Ecker J.R.;
RT   "Activation of the ethylene gas response pathway in Arabidopsis by the
RT   nuclear protein ETHYLENE-INSENSITIVE3 and related proteins.";
RL   Cell 89:1133-1144(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   CHARACTERIZATION, AND FUNCTION.
RX   PubMed=9851977; DOI=10.1101/gad.12.23.3703;
RA   Solano R., Stepanova A.N., Chao Q., Ecker J.R.;
RT   "Nuclear events in ethylene signaling: a transcriptional cascade mediated
RT   by ETHYLENE-INSENSITIVE3 and ETHYLENE-RESPONSE-FACTOR1.";
RL   Genes Dev. 12:3703-3714(1998).
RN   [6]
RP   STRUCTURE BY NMR OF 162-288.
RX   PubMed=15811366; DOI=10.1016/j.jmb.2005.02.065;
RA   Yamasaki K., Kigawa T., Inoue M., Yamasaki T., Yabuki T., Aoki M., Seki E.,
RA   Matsuda T., Tomo Y., Terada T., Shirouzu M., Tanaka A., Seki M.,
RA   Shinozaki K., Yokoyama S.;
RT   "Solution structure of the major DNA-binding domain of Arabidopsis thaliana
RT   ethylene-insensitive3-like3.";
RL   J. Mol. Biol. 348:253-264(2005).
RN   [7]
RP   INTERACTION WITH MYB72.
RC   STRAIN=cv. Columbia;
RX   PubMed=18218967; DOI=10.1104/pp.107.113829;
RA   Van der Ent S., Verhagen B.W.M., Van Doorn R., Bakker D., Verlaan M.G.,
RA   Pel M.J.C., Joosten R.G., Proveniers M.C.G., Van Loon L.C., Ton J.,
RA   Pieterse C.M.J.;
RT   "MYB72 is required in early signaling steps of rhizobacteria-induced
RT   systemic resistance in Arabidopsis.";
RL   Plant Physiol. 146:1293-1304(2008).
CC   -!- FUNCTION: Probable transcription factor that may be involved in the
CC       ethylene response pathway. {ECO:0000269|PubMed:9215635,
CC       ECO:0000269|PubMed:9851977}.
CC   -!- SUBUNIT: Interacts with MYB72. {ECO:0000269|PubMed:18218967}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EIN3 family. {ECO:0000305}.
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DR   EMBL; AF004215; AAC49748.1; -; mRNA.
DR   EMBL; AC012679; AAG52067.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35502.1; -; Genomic_DNA.
DR   EMBL; AY070044; AAL49801.1; -; mRNA.
DR   EMBL; AY133839; AAM91773.1; -; mRNA.
DR   PIR; E96764; E96764.
DR   RefSeq; NP_177514.1; NM_106032.5.
DR   PDB; 1WIJ; NMR; -; A=162-288.
DR   PDBsum; 1WIJ; -.
DR   AlphaFoldDB; O23116; -.
DR   SMR; O23116; -.
DR   BioGRID; 28927; 4.
DR   IntAct; O23116; 3.
DR   STRING; 3702.AT1G73730.1; -.
DR   iPTMnet; O23116; -.
DR   PaxDb; O23116; -.
DR   PRIDE; O23116; -.
DR   ProteomicsDB; 222674; -.
DR   EnsemblPlants; AT1G73730.1; AT1G73730.1; AT1G73730.
DR   GeneID; 843708; -.
DR   Gramene; AT1G73730.1; AT1G73730.1; AT1G73730.
DR   KEGG; ath:AT1G73730; -.
DR   Araport; AT1G73730; -.
DR   TAIR; locus:2027754; AT1G73730.
DR   eggNOG; ENOG502QQCD; Eukaryota.
DR   HOGENOM; CLU_027306_1_1_1; -.
DR   InParanoid; O23116; -.
DR   OrthoDB; 674199at2759; -.
DR   PhylomeDB; O23116; -.
DR   EvolutionaryTrace; O23116; -.
DR   PRO; PR:O23116; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O23116; baseline and differential.
DR   Genevisible; O23116; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0009970; P:cellular response to sulfate starvation; IMP:TAIR.
DR   GO; GO:0009873; P:ethylene-activated signaling pathway; TAS:TAIR.
DR   GO; GO:0042762; P:regulation of sulfur metabolic process; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR   Gene3D; 1.10.3180.10; -; 2.
DR   InterPro; IPR006957; EIN3.
DR   InterPro; IPR023278; Ethylene_insens-like_DNA-bd.
DR   PANTHER; PTHR33305; PTHR33305; 1.
DR   Pfam; PF04873; EIN3; 1.
DR   SUPFAM; SSF116768; SSF116768; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; DNA-binding; Ethylene signaling pathway;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..567
FT                   /note="ETHYLENE INSENSITIVE 3-like 3 protein"
FT                   /id="PRO_0000113501"
FT   DNA_BIND        162..288
FT   REGION          55..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..44
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        286..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           171..181
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   STRAND          182..187
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   HELIX           199..202
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   HELIX           209..214
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   HELIX           227..229
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   HELIX           232..245
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   HELIX           250..255
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   TURN            256..259
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   STRAND          260..263
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   TURN            264..266
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   HELIX           270..279
FT                   /evidence="ECO:0007829|PDB:1WIJ"
FT   TURN            280..284
FT                   /evidence="ECO:0007829|PDB:1WIJ"
SQ   SEQUENCE   567 AA;  64042 MW;  308AFEE4B3109594 CRC64;
     MGDLAMSVAD IRMENEPDDL ASDNVAEIDV SDEEIDADDL ERRMWKDRVR LKRIKERQKA
     GSQGAQTKET PKKISDQAQR KKMSRAQDGI LKYMLKLMEV CKVRGFVYGI IPEKGKPVSG
     SSDNIRAWWK EKVKFDKNGP AAIAKYEEEC LAFGKSDGNR NSQFVLQDLQ DATLGSLLSS
     LMQHCDPPQR KYPLEKGTPP PWWPTGNEEW WVKLGLPKSQ SPPYRKPHDL KKMWKVGVLT
     AVINHMLPDI AKIKRHVRQS KCLQDKMTAK ESAIWLAVLN QEESLIQQPS SDNGNSNVTE
     THRRGNNADR RKPVVNSDSD YDVDGTEEAS GSVSSKDSRR NQIQKEQPTA ISHSVRDQDK
     AEKHRRRKRP RIRSGTVNRQ EEEQPEAQQR NILPDMNHVD APLLEYNING THQEDDVVDP
     NIALGPEDNG LELVVPEFNN NYTYLPLVNE QTMMPVDERP MLYGPNPNQE LQFGSGYNFY
     NPSAVFVHNQ EDDILHTQIE MNTQAPPHNS GFEEAPGGVL QPLGLLGNED GVTGSELPQY
     QSGILSPLTD LDFDYGGFGD DFSWFGA
 
 
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