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FIE_ARATH
ID   FIE_ARATH               Reviewed;         369 AA.
AC   Q9LT47; Q9XF44;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   25-MAY-2022, entry version 163.
DE   RecName: Full=Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM;
DE   AltName: Full=Protein FERTILIZATION-INDEPENDENT SEED 3;
GN   Name=FIE; Synonyms=FIS3; OrderedLocusNames=At3g20740; ORFNames=MOE17.5;
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], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP   OF 365-ASP--LYS-369.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RX   PubMed=10072400; DOI=10.2307/3870869;
RA   Ohad N., Yadegari R., Margossian L., Hannon M., Michaeli D., Harada J.J.,
RA   Goldberg R.B., Fischer R.L.;
RT   "Mutations in FIE, a WD polycomb group gene, allow endosperm development
RT   without fertilization.";
RL   Plant Cell 11:407-416(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
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   [6]
RP   INTERACTION WITH MEA, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11114524; DOI=10.1016/s0960-9822(00)00839-3;
RA   Spillane C., MacDougall C., Stock C., Koehler C., Vielle-Calzada J.-P.,
RA   Nunes S.M., Grossniklaus U., Goodrich J.;
RT   "Interaction of the Arabidopsis polycomb group proteins FIE and MEA
RT   mediates their common phenotypes.";
RL   Curr. Biol. 10:1535-1538(2000).
RN   [7]
RP   INTERACTION WITH MEA, AND TISSUE SPECIFICITY.
RX   PubMed=10962025; DOI=10.1073/pnas.170292997;
RA   Luo M., Bilodeau P., Dennis E.S., Peacock W.J., Chaudhury A.;
RT   "Expression and parent-of-origin effects for FIS2, MEA, and FIE in the
RT   endosperm and embryo of developing Arabidopsis seeds.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10637-10642(2000).
RN   [8]
RP   INTERACTION WITH MEA, AND TISSUE SPECIFICITY.
RX   PubMed=11148284; DOI=10.2307/3871235;
RA   Yadegari R., Kinoshita T., Lotan O., Cohen G., Katz A., Choi Y., Katz A.,
RA   Nakashima K., Harada J.J., Goldberg R.B., Fischer R.L., Ohad N.;
RT   "Mutations in the FIE and MEA genes that encode interacting polycomb
RT   proteins cause parent-of-origin effects on seed development by distinct
RT   mechanisms.";
RL   Plant Cell 12:2367-2382(2000).
RN   [9]
RP   FUNCTION.
RX   PubMed=11250158; DOI=10.1016/s0960-9822(01)00072-0;
RA   Soerensen M.B., Chaudhury A.M., Robert H., Bancharel E., Berger F.;
RT   "Polycomb group genes control pattern formation in plant seed.";
RL   Curr. Biol. 11:277-281(2001).
RN   [10]
RP   FUNCTION.
RX   PubMed=12815071; DOI=10.1101/gad.257403;
RA   Koehler C., Hennig L., Spillane C., Pien S., Gruissem W., Grossniklaus U.;
RT   "The Polycomb-group protein MEDEA regulates seed development by controlling
RT   expression of the MADS-box gene PHERES1.";
RL   Genes Dev. 17:1540-1553(2003).
RN   [11]
RP   FUNCTION.
RX   PubMed=15151989; DOI=10.1242/dev.01168;
RA   Guitton A.-E., Page D.R., Chambrier P., Lionnet C., Faure J.-E.,
RA   Grossniklaus U., Berger F.;
RT   "Identification of new members of fertilisation independent seed Polycomb
RT   group pathway involved in the control of seed development in Arabidopsis
RT   thaliana.";
RL   Development 131:2971-2981(2004).
RN   [12]
RP   INTERACTION WITH CLF.
RX   PubMed=14871310; DOI=10.1111/j.1365-313x.2003.01996.x;
RA   Katz A., Oliva M., Mosquna A., Hakim O., Ohad N.;
RT   "FIE and CURLY LEAF polycomb proteins interact in the regulation of
RT   homeobox gene expression during sporophyte development.";
RL   Plant J. 37:707-719(2004).
RN   [13]
RP   SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18854416; DOI=10.1073/pnas.0808687105;
RA   De Lucia F., Crevillen P., Jones A.M.E., Greb T., Dean C.;
RT   "A PHD-polycomb repressive complex 2 triggers the epigenetic silencing of
RT   FLC during vernalization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:16831-16836(2008).
RN   [14]
RP   INTERACTION WITH ALP1.
RX   PubMed=26642436; DOI=10.1371/journal.pgen.1005660;
RA   Liang S.C., Hartwig B., Perera P., Mora-Garcia S., de Leau E., Thornton H.,
RA   de Lima Alves F., de Alves F.L., Rappsilber J., Rapsilber J., Yang S.,
RA   James G.V., Schneeberger K., Finnegan E.J., Turck F., Goodrich J.;
RT   "Kicking against the PRCs - A domesticated transposase antagonises
RT   silencing mediated by polycomb group proteins and is an accessory component
RT   of polycomb repressive complex 2.";
RL   PLoS Genet. 11:E1005660-E1005660(2015).
CC   -!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by forming
CC       multiprotein complexes, which are required to maintain the
CC       transcriptionally repressive state of homeotic genes throughout
CC       development. PcG proteins are not required to initiate repression, but
CC       to maintain it during later stages of development. They probably act
CC       via the methylation of histones, rendering chromatin heritably changed
CC       in its expressibility. Required to prevent the proliferation of the
CC       central cell by repressing unknown target genes before fertilization.
CC       Probably also involved in floral repression mechanism established
CC       during early plant development. Regulates the anteroposterior
CC       organization of the endosperm. Interacts with the promoter and
CC       represses the transcription of genes such as PHE1, that are paternally
CC       active and maternally silenced. {ECO:0000269|PubMed:10072400,
CC       ECO:0000269|PubMed:11250158, ECO:0000269|PubMed:12815071,
CC       ECO:0000269|PubMed:15151989}.
CC   -!- SUBUNIT: Interacts directly with MEA. These two proteins are probably
CC       indirectly associated with FIS2. In plants, PcG complexes are probably
CC       composed of a member of the EZ family (CLF or MEA), FIE, and a member
CC       of the VEFS family (FIS2, VRN2 or EMF2). Component of the plant
CC       homeodomain / polycomb repressive complex 2 (PHD-PRC2) large complex
CC       during prolonged cold, composed of core PRC2 components (VRN2, EZA1,
CC       FIE and MSI1), and three related PHD finger proteins (VIL1, VIL2 and
CC       VIN3) that mediates histone H3 trimethylation on 'Lys-27' (H3K27me3).
CC       Binds to ALP1 (PubMed:26642436). {ECO:0000269|PubMed:10962025,
CC       ECO:0000269|PubMed:11114524, ECO:0000269|PubMed:11148284,
CC       ECO:0000269|PubMed:14871310, ECO:0000269|PubMed:18854416,
CC       ECO:0000269|PubMed:26642436}.
CC   -!- INTERACTION:
CC       Q9LT47; P93831: CLF; NbExp=4; IntAct=EBI-307146, EBI-307155;
CC       Q9LT47; O65312: MEA; NbExp=12; IntAct=EBI-307146, EBI-632832;
CC       Q9LT47; O22467: MSI1; NbExp=6; IntAct=EBI-307146, EBI-632891;
CC       Q9LT47; Q9LKZ3: RBR1; NbExp=2; IntAct=EBI-307146, EBI-398590;
CC       Q9LT47; Q8W5B1: VRN2; NbExp=3; IntAct=EBI-307146, EBI-2128880;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11114524}.
CC       Note=Excluded from the nucleolus.
CC   -!- TISSUE SPECIFICITY: Expressed in cauline leaves, root and stems. In the
CC       male reproductive organ, it is expressed in the developing anther; and
CC       is abundant in microspore mother cells, in microsporocytes and in the
CC       tapetum, but is absent from vascular bundles, the connective tissue and
CC       the filament. It is also absent from pollen grains at subsequent
CC       developmental stages. In the developing female reproductive organs, it
CC       is highly expressed in all cells of the young ovules primordium before
CC       archesporial differentiation. Then, it is highly expressed in the ovule
CC       sporophytic tissue and the megaspore mother cell before meiosis, but is
CC       absent from placenta or the developing carpel. Then, it decreases.
CC       {ECO:0000269|PubMed:10072400, ECO:0000269|PubMed:10962025,
CC       ECO:0000269|PubMed:11114524, ECO:0000269|PubMed:11148284}.
CC   -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically. Expressed in
CC       both egg and central cell before fertilization, and in the embryo and
CC       endosperm after fertilization.
CC   -!- SIMILARITY: Belongs to the WD repeat ESC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB02481.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF129516; AAD23584.1; -; mRNA.
DR   EMBL; AB025629; BAB02481.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE76418.1; -; Genomic_DNA.
DR   EMBL; AK117114; BAC41793.1; -; mRNA.
DR   EMBL; BT005326; AAO63390.1; -; mRNA.
DR   RefSeq; NP_188710.1; NM_112965.1.
DR   AlphaFoldDB; Q9LT47; -.
DR   SMR; Q9LT47; -.
DR   BioGRID; 6954; 11.
DR   DIP; DIP-31378N; -.
DR   IntAct; Q9LT47; 11.
DR   STRING; 3702.AT3G20740.1; -.
DR   iPTMnet; Q9LT47; -.
DR   PaxDb; Q9LT47; -.
DR   PRIDE; Q9LT47; -.
DR   ProteomicsDB; 230511; -.
DR   EnsemblPlants; AT3G20740.1; AT3G20740.1; AT3G20740.
DR   GeneID; 821622; -.
DR   Gramene; AT3G20740.1; AT3G20740.1; AT3G20740.
DR   KEGG; ath:AT3G20740; -.
DR   Araport; AT3G20740; -.
DR   TAIR; locus:2091876; AT3G20740.
DR   eggNOG; KOG1034; Eukaryota.
DR   HOGENOM; CLU_032683_2_0_1; -.
DR   InParanoid; Q9LT47; -.
DR   OMA; WSYDSVT; -.
DR   OrthoDB; 1191277at2759; -.
DR   PhylomeDB; Q9LT47; -.
DR   PRO; PR:Q9LT47; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LT47; baseline and differential.
DR   Genevisible; Q9LT47; AT.
DR   GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR   GO; GO:0035098; C:ESC/E(Z) complex; IBA:GO_Central.
DR   GO; GO:0043078; C:polar nucleus; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0016571; P:histone methylation; IMP:TAIR.
DR   GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:2000014; P:regulation of endosperm development; IMP:TAIR.
DR   GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:TAIR.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0010048; P:vernalization response; IMP:TAIR.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 2.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Developmental protein; Nucleus; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation; WD repeat.
FT   CHAIN           1..369
FT                   /note="Polycomb group protein FERTILIZATION-INDEPENDENT
FT                   ENDOSPERM"
FT                   /id="PRO_0000050977"
FT   REPEAT          31..73
FT                   /note="WD 1"
FT   REPEAT          81..123
FT                   /note="WD 2"
FT   REPEAT          126..166
FT                   /note="WD 3"
FT   REPEAT          172..212
FT                   /note="WD 4"
FT   REPEAT          238..275
FT                   /note="WD 5"
FT   REPEAT          287..328
FT                   /note="WD 6"
FT   REPEAT          335..368
FT                   /note="WD 7"
FT   MUTAGEN         365..369
FT                   /note="Missing: In fie-6; induces endosperm proliferation
FT                   without fertilization. Abolishes interaction with MEA."
FT                   /evidence="ECO:0000269|PubMed:10072400"
SQ   SEQUENCE   369 AA;  41257 MW;  EDF0989C02B4FD4A CRC64;
     MSKITLGNES IVGSLTPSNK KSYKVTNRIQ EGKKPLYAVV FNFLDARFFD VFVTAGGNRI
     TLYNCLGDGA ISALQSYADE DKEESFYTVS WACGVNGNPY VAAGGVKGII RVIDVNSETI
     HKSLVGHGDS VNEIRTQPLK PQLVITASKD ESVRLWNVET GICILIFAGA GGHRYEVLSV
     DFHPSDIYRF ASCGMDTTIK IWSMKEFWTY VEKSFTWTDD PSKFPTKFVQ FPVFTASIHT
     NYVDCNRWFG DFILSKSVDN EILLWEPQLK ENSPGEGASD VLLRYPVPMC DIWFIKFSCD
     LHLSSVAIGN QEGKVYVWDL KSCPPVLITK LSHNQSKSVI RQTAMSVDGS TILACCEDGT
     IWRWDVITK
 
 
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