FZY1_CAEEL
ID FZY1_CAEEL Reviewed; 507 AA.
AC Q09373; Q09661;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=WD repeat-containing protein fzy-1;
DE AltName: Full=CDC20 protein family homolog 1 {ECO:0000305};
DE AltName: Full=Fizzy protein 1;
GN Name=fzy-1 {ECO:0000303|PubMed:12498686};
GN ORFNames=ZK177.6 {ECO:0000312|WormBase:ZK177.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-433.
RX PubMed=12498686; DOI=10.1016/s0960-9822(02)01392-1;
RA Kitagawa R., Law E., Tang L., Rose A.M.;
RT "The Cdc20 homolog, FZY-1, and its interacting protein, IFY-1, are required
RT for proper chromosome segregation in Caenorhabditis elegans.";
RL Curr. Biol. 12:2118-2123(2002).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11832245; DOI=10.1016/s1534-5807(02)00114-4;
RA Rappleye C.A., Tagawa A., Lyczak R., Bowerman B., Aroian R.V.;
RT "The anaphase-promoting complex and separin are required for embryonic
RT anterior-posterior axis formation.";
RL Dev. Cell 2:195-206(2002).
CC -!- FUNCTION: Plays a role in metaphase-anaphase transition during meiosis
CC I (PubMed:12498686). Required for embryonic anterior-posterior axis
CC formation (PubMed:11832245). {ECO:0000269|PubMed:11832245,
CC ECO:0000269|PubMed:12498686}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:12498686}.
CC Cytoplasm {ECO:0000269|PubMed:12498686}. Note=At prometaphase,
CC localizes around condensed chromosomes. At metaphase, localizes along
CC chromosomes, dissociates from the sister chromatid after separation and
CC localizes to the cytoplasm at anaphase and interphase.
CC {ECO:0000269|PubMed:12498686}.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes at the prometaphase and
CC metaphase of meiosis I (at protein level). Expressed in early embryo at
CC the prometaphase and metaphase of mitosis (at protein level).
CC {ECO:0000269|PubMed:12498686}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic
CC lethality (PubMed:12498686). Embryos are arrested at the metaphase-
CC anaphase transition of meiosis I and lack formation of polar bodies
CC (PubMed:12498686). In addition, causes a loss of asymmetric cell
CC division and par-2 mislocalization in the one-cell embryo followed by
CC an arrest at the one-cell stage (PubMed:11832245).
CC {ECO:0000269|PubMed:11832245, ECO:0000269|PubMed:12498686}.
CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
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DR EMBL; FO080583; CCD64859.1; -; Genomic_DNA.
DR PIR; T27761; T27761.
DR RefSeq; NP_495051.1; NM_062650.4.
DR AlphaFoldDB; Q09373; -.
DR SMR; Q09373; -.
DR BioGRID; 57344; 3.
DR IntAct; Q09373; 2.
DR STRING; 6239.ZK177.6; -.
DR iPTMnet; Q09373; -.
DR EPD; Q09373; -.
DR PaxDb; Q09373; -.
DR PeptideAtlas; Q09373; -.
DR EnsemblMetazoa; ZK177.6.1; ZK177.6.1; WBGene00001511.
DR EnsemblMetazoa; ZK177.6.2; ZK177.6.2; WBGene00001511.
DR GeneID; 266859; -.
DR KEGG; cel:CELE_ZK177.6; -.
DR UCSC; ZK177.6; c. elegans.
DR CTD; 266859; -.
DR WormBase; ZK177.6; CE26338; WBGene00001511; fzy-1.
DR eggNOG; KOG0305; Eukaryota.
DR GeneTree; ENSGT00950000183104; -.
DR HOGENOM; CLU_041348_0_0_1; -.
DR InParanoid; Q09373; -.
DR OMA; DMDMAYF; -.
DR OrthoDB; 420441at2759; -.
DR PhylomeDB; Q09373; -.
DR Reactome; R-CEL-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
DR Reactome; R-CEL-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q09373; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001511; Expressed in embryo and 4 other tissues.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
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:0008356; P:asymmetric cell division; IMP:UniProtKB.
DR GO; GO:1990949; P:metaphase/anaphase transition of meiosis I; IMP:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:UniProtKB.
DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
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; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19918; PTHR19918; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cytoplasm; Meiosis; Mitosis;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..507
FT /note="WD repeat-containing protein fzy-1"
FT /id="PRO_0000051003"
FT REPEAT 219..258
FT /note="WD 1"
FT REPEAT 313..352
FT /note="WD 2"
FT REPEAT 364..406
FT /note="WD 3"
FT REPEAT 411..450
FT /note="WD 4"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 433
FT /note="D->N: In h1983; reduction in the number of eggs
FT laid."
FT /evidence="ECO:0000269|PubMed:12498686"
SQ SEQUENCE 507 AA; 56384 MW; C68E9F2899109610 CRC64;
MNNKGRTPGS AGRTVRSSAQ QNGLTMRKRD MTPTRNTNLL PNATFVGDRF LGVRLDQDEL
DHANHLMTSK LYSNKENLNN SMSEPNSPEK KSVEGEALKQ MMRHKSTGAL TDADDGDRIL
CYKKNLAPPP AIGYINQAKV LYSTNSVINP ASSVKKSTRH VKETATKVLD GPGLTKDLYS
RHLDWGCHNW VAVALGHELY LWNTETCVIK NLFEDNAPTN EGLITSVRWS QEGRYISLGY
ASGAVKIYDP NRPKTTEYVR ELRTLRVGGA SRCASIAWRK QGVMTCGYKS GDIVNHDVRI
SQHVVSSWGG DNGHCRDVTA LEWSADENMC VSGSSDRTAK IWDGRHVRGS TVIQDPEPMF
TIDEHTGQVR TAQFCSFRDG ILATGGGIND GTVKLWDVKR QFQKVRELNV CETGGVGGIV
FNRPYSEMLT ASDDGFLRIY RFNANYKLSH EIQASNEPIM DLVGSPFDEV LIGDMEETLK
VFQLFNVDKS TNILDRTAPK NVGLNVR