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EBF1_ARATH
ID   EBF1_ARATH              Reviewed;         628 AA.
AC   Q9SKK0; B9DHK7; Q0WM37;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=EIN3-binding F-box protein 1;
DE   AltName: Full=F-box/LRR-repeat protein 6;
GN   Name=EBF1; Synonyms=FBL6; OrderedLocusNames=At2g25490; ORFNames=F13B15.15;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH CUL1; SKP1A/ASK1;
RP   SKP1B/ASK2; EIN3 AND EIL1.
RX   PubMed=14675533; DOI=10.1016/s0092-8674(03)00968-1;
RA   Potuschak T., Lechner E., Parmentier Y., Yanagisawa S., Grava S., Koncz C.,
RA   Genschik P.;
RT   "EIN3-dependent regulation of plant ethylene hormone signaling by two
RT   Arabidopsis F box proteins: EBF1 and EBF2.";
RL   Cell 115:679-689(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-628.
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-384.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11077244; DOI=10.1016/s1360-1385(00)01769-6;
RA   Xiao W., Jang J.-C.;
RT   "F-box proteins in Arabidopsis.";
RL   Trends Plant Sci. 5:454-457(2000).
RN   [8]
RP   INTERACTION WITH SKP1A/ASK1; SKP1B/ASK2; ASK11; ASK13 AND ASK18.
RX   PubMed=12169662; DOI=10.1073/pnas.162339999;
RA   Gagne J.M., Downes B.P., Shiu S.-H., Durski A.M., Vierstra R.D.;
RT   "The F-box subunit of the SCF E3 complex is encoded by a diverse
RT   superfamily of genes in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:11519-11524(2002).
RN   [9]
RP   INTERACTION WITH SKP1A/ASK1; SKP1B/ASK2; ASK11 AND ASK12.
RX   PubMed=14749489; DOI=10.1093/pcp/pch009;
RA   Takahashi N., Kuroda H., Kuromori T., Hirayama T., Seki M., Shinozaki K.,
RA   Shimada H., Matsui M.;
RT   "Expression and interaction analysis of Arabidopsis Skp1-related genes.";
RL   Plant Cell Physiol. 45:83-91(2004).
CC   -!- FUNCTION: Component of SCF(EBF1) E3 ubiquitin ligase complexes, which
CC       may mediate the ubiquitination and subsequent proteasomal degradation
CC       of target proteins (probably including EIN3 and EIL1). Regulator of the
CC       ethylene signaling cascade by modulating the stability of EIN3 and EIL1
CC       proteins. Confers insensitivity to ethylene.
CC       {ECO:0000269|PubMed:14675533}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       Interacts with CUL1, SKP1A/ASK1, SKP1B/ASK2, ASK11, ASK12, ASK13,
CC       ASK18, EIN3, and EIL1. {ECO:0000269|PubMed:12169662,
CC       ECO:0000269|PubMed:14675533, ECO:0000269|PubMed:14749489}.
CC   -!- INTERACTION:
CC       Q9SKK0; O49484: ASK11; NbExp=3; IntAct=EBI-401198, EBI-401185;
CC       Q9SKK0; A0A178VSX5: At2g46900; NbExp=3; IntAct=EBI-401198, EBI-25518256;
CC       Q9SKK0; A0A1I9LTW1: At3g54390; NbExp=3; IntAct=EBI-401198, EBI-15191983;
CC       Q9SKK0; Q94AH6: CUL1; NbExp=4; IntAct=EBI-401198, EBI-532411;
CC       Q9SKK0; O24606: EIN3; NbExp=4; IntAct=EBI-401198, EBI-593576;
CC       Q9SKK0; Q8RXD6: HUB1; NbExp=3; IntAct=EBI-401198, EBI-2012188;
CC       Q9SKK0; P46639: KNAT1; NbExp=3; IntAct=EBI-401198, EBI-530486;
CC       Q9SKK0; O23160: MYB73; NbExp=3; IntAct=EBI-401198, EBI-25506855;
CC       Q9SKK0; Q9CAN4: PP2A11; NbExp=4; IntAct=EBI-401198, EBI-604272;
CC       Q9SKK0; A8MRK9: RPC14; NbExp=3; IntAct=EBI-401198, EBI-25518040;
CC       Q9SKK0; Q39255: SKP1A; NbExp=7; IntAct=EBI-401198, EBI-532357;
CC       Q9SKK0; Q9FHW7: SKP1B; NbExp=5; IntAct=EBI-401198, EBI-604076;
CC       Q9SKK0; Q9FUA4: SPT; NbExp=3; IntAct=EBI-401198, EBI-1536703;
CC       Q9SKK0; P43291: SRK2A; NbExp=2; IntAct=EBI-401198, EBI-401164;
CC       Q9SKK0; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-401198, EBI-15192297;
CC       Q9SKK0; Q84MB2: TIFY8; NbExp=5; IntAct=EBI-401198, EBI-4426557;
CC       Q9SKK0; O22768: UNE12; NbExp=3; IntAct=EBI-401198, EBI-3133156;
CC       Q9SKK0; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-401198, EBI-15193683;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14675533}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14675533}.
CC   -!- INDUCTION: EIN3-dependent induction by ethylene.
CC       {ECO:0000269|PubMed:14675533}.
CC   -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC       {ECO:0000250}.
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DR   EMBL; AJ609238; CAE75864.1; -; Genomic_RNA.
DR   EMBL; AC006300; AAD20708.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07708.1; -; Genomic_DNA.
DR   EMBL; AY072205; AAL60026.1; -; mRNA.
DR   EMBL; AY091333; AAM14272.1; -; mRNA.
DR   EMBL; AK317560; BAH20224.1; -; mRNA.
DR   EMBL; AK229995; BAF01819.1; -; mRNA.
DR   PIR; A84649; A84649.
DR   RefSeq; NP_565597.1; NM_128106.4.
DR   AlphaFoldDB; Q9SKK0; -.
DR   SMR; Q9SKK0; -.
DR   BioGRID; 2439; 26.
DR   DIP; DIP-31329N; -.
DR   IntAct; Q9SKK0; 27.
DR   STRING; 3702.AT2G25490.1; -.
DR   PaxDb; Q9SKK0; -.
DR   PRIDE; Q9SKK0; -.
DR   ProteomicsDB; 224711; -.
DR   EnsemblPlants; AT2G25490.1; AT2G25490.1; AT2G25490.
DR   GeneID; 817087; -.
DR   Gramene; AT2G25490.1; AT2G25490.1; AT2G25490.
DR   KEGG; ath:AT2G25490; -.
DR   Araport; AT2G25490; -.
DR   TAIR; locus:2040105; AT2G25490.
DR   eggNOG; KOG1947; Eukaryota.
DR   HOGENOM; CLU_016072_2_0_1; -.
DR   InParanoid; Q9SKK0; -.
DR   OMA; CGLKGIT; -.
DR   OrthoDB; 1282076at2759; -.
DR   PhylomeDB; Q9SKK0; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9SKK0; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SKK0; baseline and differential.
DR   Genevisible; Q9SKK0; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; TAS:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:TAIR.
DR   Gene3D; 3.80.10.10; -; 4.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF13516; LRR_6; 3.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00367; LRR_CC; 13.
DR   SUPFAM; SSF81383; SSF81383; 1.
PE   1: Evidence at protein level;
KW   Ethylene signaling pathway; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..628
FT                   /note="EIN3-binding F-box protein 1"
FT                   /id="PRO_0000272245"
FT   DOMAIN          61..109
FT                   /note="F-box"
SQ   SEQUENCE   628 AA;  66589 MW;  805CD1A3D441F392 CRC64;
     MSQIFSFAGE NDFYRRGAIY PNPKDASLLL SLGSFADVYF PPSKRSRVVA PTIFSAFEKK
     PVSIDVLPDE CLFEIFRRLS GPQERSACAF VSKQWLTLVS SIRQKEIDVP SKITEDGDDC
     EGCLSRSLDG KKATDVRLAA IAVGTAGRGG LGKLSIRGSN SAKVSDLGLR SIGRSCPSLG
     SLSLWNVSTI TDNGLLEIAE GCAQLEKLEL NRCSTITDKG LVAIAKSCPN LTELTLEACS
     RIGDEGLLAI ARSCSKLKSV SIKNCPLVRD QGIASLLSNT TCSLAKLKLQ MLNVTDVSLA
     VVGHYGLSIT DLVLAGLSHV SEKGFWVMGN GVGLQKLNSL TITACQGVTD MGLESVGKGC
     PNMKKAIISK SPLLSDNGLV SFAKASLSLE SLQLEECHRV TQFGFFGSLL NCGEKLKAFS
     LVNCLSIRDL TTGLPASSHC SALRSLSIRN CPGFGDANLA AIGKLCPQLE DIDLCGLKGI
     TESGFLHLIQ SSLVKINFSG CSNLTDRVIS AITARNGWTL EVLNIDGCSN ITDASLVSIA
     ANCQILSDLD ISKCAISDSG IQALASSDKL KLQILSVAGC SMVTDKSLPA IVGLGSTLLG
     LNLQQCRSIS NSTVDFLVER LYKCDILS
 
 
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