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FB161_ARATH
ID   FB161_ARATH             Reviewed;         388 AA.
AC   Q9LJ74;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=F-box protein ETP2 {ECO:0000303|PubMed:19196655};
DE   AltName: Full=EIN2 targeting protein 2 {ECO:0000303|PubMed:19196655};
GN   Name=ETP2 {ECO:0000303|PubMed:19196655};
GN   OrderedLocusNames=At3g18910 {ECO:0000312|Araport:AT3G18910};
GN   ORFNames=K13E13.1 {ECO:0000312|EMBL:BAB01688.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA   Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA   Shinozaki K., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, INTERACTION WITH EIN2, DISRUPTION PHENOTYPE, AND INDUCTION BY
RP   ETHYLENE.
RX   PubMed=19196655; DOI=10.1101/gad.1765709;
RA   Qiao H., Chang K.N., Yazaki J., Ecker J.R.;
RT   "Interplay between ethylene, ETP1/ETP2 F-box proteins, and degradation of
RT   EIN2 triggers ethylene responses in Arabidopsis.";
RL   Genes Dev. 23:512-521(2009).
CC   -!- FUNCTION: Negative regulator of EIN2 protein stability.
CC       {ECO:0000269|PubMed:19196655}.
CC   -!- SUBUNIT: Interacts with EIN2 (via C-terminus).
CC       {ECO:0000269|PubMed:19196655}.
CC   -!- INTERACTION:
CC       Q9LJ74; Q9S814: EIN2; NbExp=2; IntAct=EBI-2437385, EBI-2437287;
CC   -!- INDUCTION: Ethylene treatment has no effect on RNA, but down-regulates
CC       the protein levels. {ECO:0000269|PubMed:19196655}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, probably due to the
CC       redundancy with ETP1. {ECO:0000269|PubMed:19196655}.
CC   -!- MISCELLANEOUS: Double knock-down mutants of ETP1 and ETP2 show an
CC       accumulation of EIN2 protein and a constitutive ethylene response.
CC       {ECO:0000269|PubMed:19196655}.
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DR   EMBL; AP000735; BAB01688.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76168.1; -; Genomic_DNA.
DR   EMBL; BT012550; AAS99694.1; -; mRNA.
DR   EMBL; AK175224; BAD42987.1; -; mRNA.
DR   RefSeq; NP_188521.1; NM_112777.4.
DR   AlphaFoldDB; Q9LJ74; -.
DR   BioGRID; 6757; 1.
DR   IntAct; Q9LJ74; 1.
DR   STRING; 3702.AT3G18910.1; -.
DR   PaxDb; Q9LJ74; -.
DR   PRIDE; Q9LJ74; -.
DR   ProteomicsDB; 230879; -.
DR   DNASU; 821424; -.
DR   EnsemblPlants; AT3G18910.1; AT3G18910.1; AT3G18910.
DR   GeneID; 821424; -.
DR   Gramene; AT3G18910.1; AT3G18910.1; AT3G18910.
DR   KEGG; ath:AT3G18910; -.
DR   Araport; AT3G18910; -.
DR   TAIR; locus:2085834; AT3G18910.
DR   HOGENOM; CLU_034692_0_0_1; -.
DR   InParanoid; Q9LJ74; -.
DR   OMA; CCERWID; -.
DR   OrthoDB; 634455at2759; -.
DR   PhylomeDB; Q9LJ74; -.
DR   PRO; PR:Q9LJ74; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LJ74; baseline and differential.
DR   Genevisible; Q9LJ74; AT.
DR   InterPro; IPR006527; F-box-assoc_dom_typ1.
DR   InterPro; IPR017451; F-box-assoc_interact_dom.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF07734; FBA_1; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF50965; SSF50965; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   TIGRFAMs; TIGR01640; F_box_assoc_1; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..388
FT                   /note="F-box protein ETP2"
FT                   /id="PRO_0000283431"
FT   DOMAIN          2..48
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
SQ   SEQUENCE   388 AA;  44619 MW;  059A4B219DE2AF0C CRC64;
     MKTIQEQLPN DLVEEILCRV PATSLRRLRS TCKAWNRLFK GDRILASKHF EKSAKQFRSL
     SLRNDYRIFP ISFNLHGNSP SLELKSELID PHSKNSAAPF EISRVIHCEG LLLCSSQLDE
     SRVVVWNPLT GETRWIRTGD FRQKGRSFDV GYYYQKDKRS WIKSYKLLCY YRGTKYFEIY
     DFDSDSWRIL DDIIAPRGSI GYSELSVSLK GNTYWFAKGV TEERPRTISL LKFDFYTEKS
     VPVLLPYQSR RLFQASSLSV VREDKLSVLL QLDQSSKTEI WVTNVIDETT KGAVSWTKVL
     ALDLSPHLQI GNDGSFFLGE DKKVVMFCEK LIDENKVKDM VYIVGEDNVV TEVGFGVDEM
     DGCRAVILNY VPSLVQIERA GGNRKRGH
 
 
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