MOE2_CAEEL
ID MOE2_CAEEL Reviewed; 393 AA.
AC Q23359;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=CCCH-type zinc finger protein oma-2 {ECO:0000305};
DE AltName: Full=Maturation oocyte expansion protein 2 {ECO:0000303|PubMed:12296824};
DE AltName: Full=Oocyte maturation defective protein 2 {ECO:0000303|PubMed:11702779};
GN Name=oma-2 {ECO:0000303|PubMed:11702779, ECO:0000312|WormBase:ZC513.6};
GN Synonyms=moe-2 {ECO:0000303|PubMed:12296824, ECO:0000312|WormBase:ZC513.6};
GN ORFNames=ZC513.6 {ECO:0000312|WormBase:ZC513.6};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-162.
RX PubMed=11702779; DOI=10.1016/s1534-5807(01)00026-0;
RA Detwiler M.R., Reuben M., Li X., Rogers E., Lin R.;
RT "Two zinc finger proteins, OMA-1 and OMA-2, are redundantly required for
RT oocyte maturation in C. elegans.";
RL Dev. Cell 1:187-199(2001).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP 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).
RN [4] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12781695; DOI=10.1016/s0012-1606(03)00119-2;
RA Lin R.;
RT "A gain-of-function mutation in oma-1, a C. elegans gene required for
RT oocyte maturation, results in delayed degradation of maternal proteins and
RT embryonic lethality.";
RL Dev. Biol. 258:226-239(2003).
RN [5] {ECO:0000305}
RP FUNCTION, PHOSPHORYLATION AT THR-327, AND MUTAGENESIS OF THR-327.
RX PubMed=16289132; DOI=10.1016/j.ydbio.2005.09.053;
RA Nishi Y., Lin R.;
RT "DYRK2 and GSK-3 phosphorylate and promote the timely degradation of OMA-1,
RT a key regulator of the oocyte-to-embryo transition in C. elegans.";
RL Dev. Biol. 288:139-149(2005).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16611242; DOI=10.1111/j.1365-2443.2006.00945.x;
RA Shimada M., Yokosawa H., Kawahara H.;
RT "OMA-1 is a P granules-associated protein that is required for germline
RT specification in Caenorhabditis elegans embryos.";
RL Genes Cells 11:383-396(2006).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18854162; DOI=10.1016/j.cell.2008.07.040;
RA Guven-Ozkan T., Nishi Y., Robertson S.M., Lin R.;
RT "Global transcriptional repression in C. elegans germline precursors by
RT regulated sequestration of TAF-4.";
RL Cell 135:149-160(2008).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18417623; DOI=10.1242/dev.013656;
RA Jadhav S., Rana M., Subramaniam K.;
RT "Multiple maternal proteins coordinate to restrict the translation of C.
RT elegans nanos-2 to primordial germ cells.";
RL Development 135:1803-1812(2008).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19786575; DOI=10.1083/jcb.200903003;
RA Li W., DeBella L.R., Guven-Ozkan T., Lin R., Rose L.S.;
RT "An eIF4E-binding protein regulates katanin protein levels in C. elegans
RT embryos.";
RL J. Cell Biol. 187:33-42(2009).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20826530; DOI=10.1242/dev.055327;
RA Guven-Ozkan T., Robertson S.M., Nishi Y., Lin R.;
RT "zif-1 translational repression defines a second, mutually exclusive OMA
RT function in germline transcriptional repression.";
RL Development 137:3373-3382(2010).
RN [11] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25261697; DOI=10.1534/genetics.114.168823;
RA Spike C.A., Coetzee D., Nishi Y., Guven-Ozkan T., Oldenbroek M.,
RA Yamamoto I., Lin R., Greenstein D.;
RT "Translational control of the oogenic program by components of OMA
RT ribonucleoprotein particles in Caenorhabditis elegans.";
RL Genetics 198:1513-1533(2014).
CC -!- FUNCTION: Zinc-finger RNA-binding protein that binds to 5'-UA[AU]-3'
CC motifs in the 3'-UTR of maternal mRNAs to suppress translation in
CC oocytes and embryos (PubMed:18417623). Acts redundantly with oma-1 to
CC control the temporal expression and distribution of maternal proteins
CC and thereby promote meiotic progression, oocyte maturation,
CC fertilization and embryonic development (PubMed:11702779,
CC PubMed:12296824, PubMed:12781695, PubMed:16289132, PubMed:16611242,
CC PubMed:18854162, PubMed:18417623, PubMed:19786575, PubMed:20826530,
CC PubMed:25261697). Also, together with oma-1, is involved in P-granule
CC distribution during embryonic development (PubMed:16611242).
CC {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:12296824,
CC ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:16611242,
CC ECO:0000269|PubMed:18417623, ECO:0000269|PubMed:18854162,
CC ECO:0000269|PubMed:19786575, ECO:0000305|PubMed:18417623}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11702779,
CC ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:16611242}. Cytoplasmic
CC granule {ECO:0000269|PubMed:12296824}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:12296824}. Note=Expressed in cytoplasmic P-granules
CC following fertilization and in developing oocytes. Expression ceases in
CC P-granules in 2-cell stage embryos. Expressed in the centrosome after
CC the 2-cell stage of embryogenesis, during the early cleavage stage, and
CC also at later blastula stages. {ECO:0000269|PubMed:12296824}.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in the hermaphrodite gonad
CC (PubMed:11702779, PubMed:12296824). Expression only in cellulized
CC oocytes (PubMed:11702779). Widely distributed throughout gonadal
CC oocytes from the mitotic stage to the developing diakinesis stage
CC (PubMed:12296824). {ECO:0000269|PubMed:11702779,
CC ECO:0000269|PubMed:12296824}.
CC -!- DEVELOPMENTAL STAGE: Expressed in newly fertilized embryos, but is
CC rapidly degraded after initiation of the first mitotic division
CC (PubMed:12296824, PubMed:12781695, PubMed:16611242). Weak, if any,
CC expression during larval stages (PubMed:11702779).
CC {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:12296824,
CC ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16611242}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:12296824). Double
CC knockout with oma-1 results in sterility due to an oocyte maturation
CC defect (PubMed:11702779). The oocyte maturation defect is due to a
CC meiotic defect in oocytes in which the maturation process is initiated,
CC but there is no progression beyond the prophase stage of meiosis and
CC therefore the cell division process is not completed (PubMed:11702779).
CC Animals also have a larger number of oocytes which are larger in size,
CC but the oocytes cannot be fertilized and accumulate within the gonad
CC (PubMed:11702779). Double RNAi-mediated knockdown with oma-1 in embryos
CC results in more widely distributed P-granules compared to wild-type
CC embryos, and an irregular distribution of germline proteins including
CC pgl-1, mex-1 and pie-1 (PubMed:16611242). Double RNAi-mediated
CC knockdown with oma-1 in larva at the L4 stage of development results in
CC 93% embryonic lethality following the first mitotic cleavage in
CC offspring (PubMed:16611242). Double RNAi-mediated knockdown with oma-1
CC in adults results in a 60% reduction in number of eggs laid
CC (PubMed:12296824). These animals also have an expanded proximal gonad
CC arm which contains larger number of proximal oocytes which in turn
CC contain a larger number of germinal vesicles and higher expression of
CC maternal mRNAs including nos-2 (PubMed:12296824, PubMed:18417623).
CC Furthermore, after the diakinesis stage following meiosis I, the
CC germinal vesicles have dispersed chromosomes and an abnormal
CC distribution of P-granules (PubMed:12296824). Embryos also display cell
CC division (PubMed:19786575, PubMed:20826530). In addition, there is
CC increased expression of target transcripts such as taf-4 and mei-1
CC which also exhibit an altered localization in oocytes and embryos
CC (PubMed:18854162, PubMed:19786575, PubMed:25261697). Reduced expression
CC of the maternal transcriptional repressor protein pie-1
CC (PubMed:20826530). Triple RNAi-mediated knockdown with oma-1 and moe-3
CC results in a 85% reduction in number of eggs laid (PubMed:12296824).
CC {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:12296824,
CC ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:18417623,
CC ECO:0000269|PubMed:18854162, ECO:0000269|PubMed:19786575,
CC ECO:0000269|PubMed:20826530, ECO:0000269|PubMed:25261697}.
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DR EMBL; BX284605; CCD64069.1; -; Genomic_DNA.
DR PIR; T28994; T28994.
DR RefSeq; NP_505069.1; NM_072668.5.
DR AlphaFoldDB; Q23359; -.
DR DIP; DIP-26006N; -.
DR IntAct; Q23359; 19.
DR STRING; 6239.ZC513.6; -.
DR iPTMnet; Q23359; -.
DR EPD; Q23359; -.
DR PaxDb; Q23359; -.
DR PeptideAtlas; Q23359; -.
DR EnsemblMetazoa; ZC513.6.1; ZC513.6.1; WBGene00003865.
DR GeneID; 179183; -.
DR KEGG; cel:CELE_ZC513.6; -.
DR UCSC; ZC513.6; c. elegans.
DR CTD; 179183; -.
DR WormBase; ZC513.6; CE07613; WBGene00003865; oma-2.
DR eggNOG; KOG1677; Eukaryota.
DR GeneTree; ENSGT00970000196212; -.
DR HOGENOM; CLU_062303_0_0_1; -.
DR InParanoid; Q23359; -.
DR OMA; HIMTGGR; -.
DR OrthoDB; 1213902at2759; -.
DR PhylomeDB; Q23359; -.
DR SignaLink; Q23359; -.
DR PRO; PR:Q23359; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003865; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IGI:UniProtKB.
DR GO; GO:0051303; P:establishment of chromosome localization; IGI:UniProtKB.
DR GO; GO:0051078; P:meiotic nuclear membrane disassembly; IGI:UniProtKB.
DR GO; GO:1904145; P:negative regulation of meiotic cell cycle process involved in oocyte maturation; IGI:UniProtKB.
DR GO; GO:0060280; P:negative regulation of ovulation; IGI:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IMP:WormBase.
DR GO; GO:0001555; P:oocyte growth; IGI:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IGI:WormBase.
DR GO; GO:0048601; P:oocyte morphogenesis; IGI:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; IGI:UniProtKB.
DR GO; GO:1905516; P:positive regulation of fertilization; IGI:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IGI:UniProtKB.
DR GO; GO:1904146; P:positive regulation of meiotic cell cycle process involved in oocyte maturation; IGI:UniProtKB.
DR GO; GO:0060282; P:positive regulation of oocyte development; IGI:UniProtKB.
DR GO; GO:1900195; P:positive regulation of oocyte maturation; IGI:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; IGI:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Ribonucleoprotein; RNA-binding; Translation regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..393
FT /note="CCCH-type zinc finger protein oma-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438917"
FT ZN_FING 105..133
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 147..175
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 327
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000305|PubMed:16289132"
FT MUTAGEN 162
FT /note="C->Y: In te50; sterile."
FT /evidence="ECO:0000269|PubMed:11702779"
FT MUTAGEN 327
FT /note="T->A: Reduced phosphorylation by GSK3."
FT /evidence="ECO:0000269|PubMed:16289132"
SQ SEQUENCE 393 AA; 43585 MW; 9F561F431776B38E CRC64;
MDMLKENVIQ NNEARTESSV EPSHPDMMET VPEEQQKPIS HIDDLLSETA NLMAVKEQLL
KEIAENEHIH SMQMRALQNL PQEAILPLQY HADPRRRHRM QKPESYKTVI CQAWLESKTC
AFAENCRFAH GEEELRPSLI EARQNNKYRT KLCDKYTTTG LCPYGKRCLF IHPDNGPNAY
IRADKLFEVS QRHALADLRD QMEHHIMNGG RSTAGPQQFD MFARPCTPDE PAANMPLGPT
PVSIRGPRYE LPSKKPLETE EAGNRPPSSW PLDPSTFFAL DSLNMATRPI SPFESMLIGA
AGNMQYSMLG KQSTPGGVSG YSSSGSTPSQ DSDSSPLTAA SAAADAACQA NSESAQSILL
KSINNPMIGN ETTLPIPGLD QLAMDIAKHL ELW
