ID   MOE3_CAEEL              Reviewed;         367 AA.
AC   Q9XV46;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=CCCH-type zinc finger protein moe-3 {ECO:0000305};
DE   AltName: Full=Maturation oocyte expansion protein 3 {ECO:0000303|PubMed:12296824};
GN   Name=moe-3 {ECO:0000303|PubMed:12296824, ECO:0000312|WormBase:F32A11.6};
GN   ORFNames=F32A11.6 {ECO:0000312|WormBase:F32A11.6};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=12296824; DOI=10.1046/j.1365-2443.2002.00570.x;
RA   Shimada M., Kawahara H., Doi H.;
RT   "Novel family of CCCH-type zinc-finger proteins, MOE-1, -2 and -3,
RT   participates in C. elegans oocyte maturation.";
RL   Genes Cells 7:933-947(2002).
CC   -!- FUNCTION: Zinc-finger protein that may play a role in oocyte maturation
CC       and fertility. {ECO:0000269|PubMed:12296824}.
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in the hermaphrodite gonad.
CC       Weakly distributed throughout gonadal oocytes from the mitotic stage to
CC       the developing diakinesis stage, with expression restricted to the
CC       distal region of the gonad. {ECO:0000269|PubMed:12296824}.
CC   -!- DISRUPTION PHENOTYPE: In adult hermaphrodites, double RNAi-mediated
CC       knockdown with oma-1 results in a 20% reduction in number of eggs laid.
CC       Triple RNAi-mediated knockdown with oma-1 and oma-2 results in a 85%
CC       reduction in number of eggs laid. {ECO:0000269|PubMed:12296824}.
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DR   EMBL; BX284602; CAB04229.1; -; Genomic_DNA.
DR   PIR; T21620; T21620.
DR   RefSeq; NP_496795.1; NM_064394.1.
DR   AlphaFoldDB; Q9XV46; -.
DR   DIP; DIP-25142N; -.
DR   IntAct; Q9XV46; 22.
DR   STRING; 6239.F32A11.6; -.
DR   EPD; Q9XV46; -.
DR   PaxDb; Q9XV46; -.
DR   PeptideAtlas; Q9XV46; -.
DR   EnsemblMetazoa; F32A11.6.1; F32A11.6.1; WBGene00003388.
DR   GeneID; 174960; -.
DR   KEGG; cel:CELE_F32A11.6; -.
DR   UCSC; F32A11.6; c. elegans.
DR   CTD; 174960; -.
DR   WormBase; F32A11.6; CE18657; WBGene00003388; moe-3.
DR   eggNOG; KOG1677; Eukaryota.
DR   GeneTree; ENSGT00970000196212; -.
DR   HOGENOM; CLU_062303_0_0_1; -.
DR   InParanoid; Q9XV46; -.
DR   OMA; KIEPRQN; -.
DR   OrthoDB; 1216752at2759; -.
DR   PhylomeDB; Q9XV46; -.
DR   PRO; PR:Q9XV46; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00003388; Expressed in larva and 3 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   InterPro; IPR045877; ZFP36-like.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR12547; PTHR12547; 1.
DR   Pfam; PF00642; zf-CCCH; 2.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   SUPFAM; SSF90229; SSF90229; 2.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..367
FT                   /note="CCCH-type zinc finger protein moe-3"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438918"
FT   ZN_FING         130..158
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         172..200
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          63..92
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        15..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  41032 MW;  77EB2D6EBDE8D7B6 CRC64;
     MSKVKGDLEK SDKRPPSSMS TGSADSGVFS SGVHASSPSH SQGSSSQSGP PSPTTQLNSL
     LFETANLIAV NEQLRKEIAE NKQIQTNQMR ALRYSSNPVD QPFVANSISP HHGFPQRPPR
     GERRMQKPES YKTVICQAWL ESKTCTFAEN CRFAHGEEEL RPAKLESRQN NKYKTKLCDK
     YTTTGLCPYG KRCLFIHPDN QPNAYIRADK LYEVSQRHAL ADLRDHVESQ IMTGNTRNSY
     NQQPPPMGGL EMQSSPMKSS SDSSHMRSPM AQMNCETTRP HPSWPLESSS FFLPPEMSSI
     NNNNLMSPFE TPFPNGSTGI QPHFVTAKRR AAFPPVPSNF QQDDDNMSSI PGFDHLAEDM
     AKHLELW