FZR3_ARATH
ID FZR3_ARATH Reviewed; 481 AA.
AC Q8LPL5; Q9FFY8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein FIZZY-RELATED 3;
DE AltName: Full=Cell cycle switch protein CCS52B;
GN Name=FZR3; Synonyms=CCS52B, CDH1-3; OrderedLocusNames=At5g13840;
GN ORFNames=MAC12.21;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
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 [4]
RP REVIEW.
RX PubMed=12597875; DOI=10.1016/s1360-1385(02)00028-6;
RA Capron A., Okresz L., Genschik P.;
RT "First glance at the plant APC/C, a highly conserved ubiquitin-protein
RT ligase.";
RL Trends Plant Sci. 8:83-89(2003).
RN [5]
RP FUNCTION, DEVELOPMENTAL STAGE, ASSOCIATION WITH THE APC/C COMPLEX, AND
RP INTERACTION WITH CYCA1-1; CYCA3-4; CYCB1-1 AND CYCB1-2.
RX PubMed=15970679;
RA Fueloep K., Tarayre S., Kelemen Z., Horvath G., Kevei Z., Nikovics K.,
RA Bako L., Brown S., Kondorosi A., Kondorosi E.;
RT "Arabidopsis anaphase-promoting complexes: multiple activators and wide
RT range of substrates might keep APC perpetually busy.";
RL Cell Cycle 4:1084-1092(2005).
RN [6]
RP REVIEW, AND GENE FAMILY.
RX PubMed=21087491; DOI=10.1186/1471-2229-10-254;
RA Lima M.D.F., Eloy N.B., Pegoraro C., Sagit R., Rojas C., Bretz T.,
RA Vargas L., Elofsson A., de Oliveira A.C., Hemerly A.S., Ferreira P.C.G.;
RT "Genomic evolution and complexity of the Anaphase-promoting Complex (APC)
RT in land plants.";
RL BMC Plant Biol. 10:254-254(2010).
RN [7]
RP INTERACTION WITH GIG1 AND PYM.
RX PubMed=22167058; DOI=10.1105/tpc.111.092049;
RA Iwata E., Ikeda S., Matsunaga S., Kurata M., Yoshioka Y., Criqui M.-C.,
RA Genschik P., Ito M.;
RT "GIGAS CELL1, a novel negative regulator of the anaphase-promoting
RT complex/cyclosome, is required for proper mitotic progression and cell fate
RT determination in Arabidopsis.";
RL Plant Cell 23:4382-4393(2011).
RN [8]
RP INTERACTION WITH CDC20-1 AND CDC20-2.
RX PubMed=21687678; DOI=10.1371/journal.pone.0020618;
RA Kevei Z., Baloban M., Da Ines O., Tiricz H., Kroll A., Regulski K.,
RA Mergaert P., Kondorosi E.;
RT "Conserved CDC20 cell cycle functions are carried out by two of the five
RT isoforms in Arabidopsis thaliana.";
RL PLoS ONE 6:E20618-E20618(2011).
RN [9]
RP INTERACTION WITH GIG1.
RX PubMed=22844260; DOI=10.1371/journal.pgen.1002865;
RA Cromer L., Heyman J., Touati S., Harashima H., Araou E., Girard C.,
RA Horlow C., Wassmann K., Schnittger A., De Veylder L., Mercier R.;
RT "OSD1 promotes meiotic progression via APC/C inhibition and forms a
RT regulatory network with TDM and CYCA1;2/TAM.";
RL PLoS Genet. 8:E1002865-E1002865(2012).
CC -!- FUNCTION: Activator protein that regulates the ubiquitin ligase
CC activity and substrate specificity of the anaphase promoting
CC complex/cyclosome (APC/C). {ECO:0000269|PubMed:15970679}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Associates with the APC/C complex. Interacts with CDC20-1,
CC CDC20-2, CYCA1-1, CYCA3-4, CYCB1-1 AND CYCB1-2. Binds to GIG1 and PYM.
CC {ECO:0000269|PubMed:15970679, ECO:0000269|PubMed:21687678,
CC ECO:0000269|PubMed:22167058, ECO:0000269|PubMed:22844260}.
CC -!- INTERACTION:
CC Q8LPL5; Q8LGU6: CDC27B; NbExp=2; IntAct=EBI-1749341, EBI-1668733;
CC -!- DEVELOPMENTAL STAGE: Expressed during G2/M and M phases.
CC {ECO:0000269|PubMed:15970679}.
CC -!- MISCELLANEOUS: FZR2 controls the induction of early rounds of
CC endoreduplication while the remaining rounds may be mediated by FZR1
CC and FZR3.
CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11112.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Arabidopsis APC/C subunits;
CC URL="http://personal.rhul.ac.uk/ujba/110/apc/APC.htm";
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DR EMBL; AB005230; BAB11112.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91948.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91949.1; -; Genomic_DNA.
DR EMBL; AY099581; AAM20433.1; -; mRNA.
DR EMBL; BT002165; AAN72176.1; -; mRNA.
DR RefSeq; NP_001190305.1; NM_001203376.1.
DR RefSeq; NP_196888.2; NM_121387.4.
DR AlphaFoldDB; Q8LPL5; -.
DR SMR; Q8LPL5; -.
DR BioGRID; 16508; 32.
DR ELM; Q8LPL5; -.
DR IntAct; Q8LPL5; 24.
DR STRING; 3702.AT5G13840.1; -.
DR PaxDb; Q8LPL5; -.
DR PRIDE; Q8LPL5; -.
DR ProteomicsDB; 248555; -.
DR EnsemblPlants; AT5G13840.1; AT5G13840.1; AT5G13840.
DR EnsemblPlants; AT5G13840.2; AT5G13840.2; AT5G13840.
DR GeneID; 831230; -.
DR Gramene; AT5G13840.1; AT5G13840.1; AT5G13840.
DR Gramene; AT5G13840.2; AT5G13840.2; AT5G13840.
DR KEGG; ath:AT5G13840; -.
DR Araport; AT5G13840; -.
DR TAIR; locus:2159078; AT5G13840.
DR eggNOG; KOG0305; Eukaryota.
DR HOGENOM; CLU_014831_4_2_1; -.
DR InParanoid; Q8LPL5; -.
DR OMA; MDQDYES; -.
DR OrthoDB; 1220675at2759; -.
DR PhylomeDB; Q8LPL5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LPL5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LPL5; baseline and differential.
DR Genevisible; Q8LPL5; AT.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IBA:GO_Central.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IBA:GO_Central.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR033010; Cdc20/Fizzy.
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 PANTHER; PTHR19918; PTHR19918; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..481
FT /note="Protein FIZZY-RELATED 3"
FT /id="PRO_0000364437"
FT REPEAT 172..209
FT /note="WD 1"
FT REPEAT 213..252
FT /note="WD 2"
FT REPEAT 255..292
FT /note="WD 3"
FT REPEAT 296..335
FT /note="WD 4"
FT REPEAT 338..380
FT /note="WD 5"
FT REPEAT 382..423
FT /note="WD 6"
FT REPEAT 426..465
FT /note="WD 7"
FT REGION 100..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 52378 MW; 0FB036D826589914 CRC64;
MASPQSTKTG LNLPAGMNQT SLRLETFSSS FRGISSLSSP SKSTCSDRFI PCRSSSRLHA
FDLQDKEPTT PVKEGGNEAY SRLLKSELFG SDFASPLLSP AGGQGSASSP MSPCTNMLRF
KTDRSNSSPS SPFSPSILGN DNGHSSDSSP PPKPPRKVPK TPHKVLDAPS LQDDFYLNVV
DWSSQNVLAV GLGTCVYLWT ASNSKVTKLC DLGPNDSVCS VQWTREGSYI SIGTSHGQVQ
VWDGTQCKRV RTMGGHQTRT GVLAWNSRIL SSGSRDRNIL QHDIRVQSDF VSKLVGHKSE
VCGLKWSHDD RELASGGNDN QLLVWNNHSQ QPILKLTEHT AAVKAITWSP HQSSLLASGG
GTADRCIRFW NTTNGNQLNS IDTGSQVCNL AWSKNVNEIV STHGYSQNQI MLWKYPSMSK
VATLTGHSMR VLYLATSPDG QTIVTGAGDE TLRFWNVFPS VKMQTPVKDT GLWSLGRTQI
R
