MOE1_CAEEL
ID MOE1_CAEEL Reviewed; 407 AA.
AC G5EC86;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=CCCH-type zinc finger protein oma-1 {ECO:0000305};
DE AltName: Full=Maturation oocyte expansion protein 1 {ECO:0000303|PubMed:12296824};
DE AltName: Full=Oocyte maturation defective protein 1 {ECO:0000303|PubMed:11702779};
GN Name=oma-1 {ECO:0000303|PubMed:11702779, ECO:0000312|WormBase:C09G9.6};
GN Synonyms=moe-1 {ECO:0000303|PubMed:12296824, ECO:0000312|WormBase:C09G9.6};
GN ORFNames=C09G9.6 {ECO:0000312|WormBase:C09G9.6};
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 GLY-138; GLU-141; GLY-172 AND
RP PRO-240.
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, AND DISRUPTION
RP 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, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP PRO-240.
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, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-239; SER-302 AND
RP THR-339, AND MUTAGENESIS OF THR-239; PRO-240; SER-302 AND THR-339.
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION 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, PHOSPHORYLATION AT THR-239 AND SER-302, AND MUTAGENESIS OF
RP SER-238; THR-239 AND SER-302.
RX PubMed=16343905; DOI=10.1016/j.cub.2005.11.070;
RA Shirayama M., Soto M.C., Ishidate T., Kim S., Nakamura K., Bei Y.,
RA van den Heuvel S., Mello C.C.;
RT "The conserved kinases CDK-1, GSK-3, KIN-19, and MBK-2 promote OMA-1
RT destruction to regulate the oocyte-to-embryo transition in C. elegans.";
RL Curr. Biol. 16:47-55(2006).
RN [8] {ECO:0000305}
RP PHOSPHORYLATION, AND MUTAGENESIS OF PRO-240.
RX PubMed=16338136; DOI=10.1016/j.cub.2005.11.063;
RA Stitzel M.L., Pellettieri J., Seydoux G.;
RT "The C. elegans DYRK Kinase MBK-2 marks oocyte proteins for degradation in
RT response to meiotic maturation.";
RL Curr. Biol. 16:56-62(2006).
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TAF-4, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, 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 [10] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, 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 [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH IFET-1, 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 [12] {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 [13] {ECO:0000305}
RP FUNCTION.
RX PubMed=24014033; DOI=10.1074/jbc.m113.496547;
RA Kaymak E., Ryder S.P.;
RT "RNA recognition by the Caenorhabditis elegans oocyte maturation
RT determinant OMA-1.";
RL J. Biol. Chem. 288:30463-30472(2013).
RN [14] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CGH-1 AND CAR-1, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
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:18854162, PubMed:18417623, PubMed:19786575,
CC PubMed:20826530, PubMed:24014033). Acts as a ribonucleoprotein particle
CC component that may exert part of its function within cytoplasmic foci
CC of unfertilized oocytes (PubMed:25261697). Acts redundantly with oma-2
CC to control the temporal expression and distribution of maternal
CC proteins 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:19786575, PubMed:20826530, PubMed:25261697). Recruits the
CC translational repressor ifet-1 to the 3'-UTR of mei-1 and zif-1 to
CC negatively regulate their translation (PubMed:19786575,
CC PubMed:20826530). By suppressing the translation of the E3 ligase zif-
CC 1, may in turn play a role in the stabilization of zif-1 targets such
CC as the maternal transcriptional repressor protein pie-1
CC (PubMed:16343905, PubMed:20826530). Following fertilization, sequesters
CC the transcription initiation factor, taf-4, in the cytoplasm, which
CC prevents its nuclear localization and thus allows for transcriptional
CC suppression in early embryos, but not in oocytes (PubMed:18854162).
CC Also, together with oma-2, is involved in P-granule distribution during
CC embryonic development (PubMed:16611242). {ECO:0000269|PubMed:11702779,
CC ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695,
CC ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:16343905,
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:24014033,
CC ECO:0000269|PubMed:25261697}.
CC -!- SUBUNIT: Interacts with taf-4 (via C-terminus) (PubMed:18854162).
CC Interacts with ifet-1 (PubMed:19786575). Component of a
CC ribonucleoprotein particle complex that interacts with cgh-1 and car-1
CC in an RNA-dependent manner (PubMed:25261697). Association with many
CC proteins is dependent on the presence of RNA (PubMed:25261697).
CC {ECO:0000269|PubMed:18854162, ECO:0000269|PubMed:19786575,
CC ECO:0000269|PubMed:25261697}.
CC -!- INTERACTION:
CC G5EC86; O61707: taf-4; NbExp=5; IntAct=EBI-327483, EBI-2023840;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11702779,
CC ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695,
CC ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:16611242,
CC ECO:0000269|PubMed:18854162}. Cytoplasmic granule
CC {ECO:0000269|PubMed:12296824, ECO:0000269|PubMed:12781695,
CC ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:25261697}. Nucleus
CC {ECO:0000269|PubMed:18854162}. Note=Expressed in cytoplasmic P-granules
CC in developing oocytes, and remains in P-granules following
CC fertilization when cytoplasmic expression is abolished
CC (PubMed:12296824, PubMed:12781695, PubMed:16611242, PubMed:25261697).
CC When phosphorylated, increased levels in the cytoplasm of embryos after
CC meiosis II and before anaphase of the first mitotic division
CC (PubMed:16289132). {ECO:0000269|PubMed:12296824,
CC ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16289132,
CC ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:18854162,
CC ECO:0000269|PubMed:25261697}.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in the hermaphrodite gonad
CC (PubMed:11702779, PubMed:12296824, PubMed:16611242). Expressed prior to
CC oocyte division (PubMed:11702779). Widely distributed throughout
CC gonadal oocytes from the mitotic stage to the developing diakinesis
CC stage (PubMed:12296824). Expressed in sperm (PubMed:25261697).
CC {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:12296824,
CC ECO:0000269|PubMed:16611242, ECO:0000269|PubMed:25261697}.
CC -!- DEVELOPMENTAL STAGE: Expressed in newly fertilized embryos, but is
CC rapidly degraded after initiation of the first mitotic division
CC (PubMed:12781695, PubMed:16611242, PubMed:18417623). Highly expressed
CC in one-cell embryos (PubMed:18854162). Expressed in P-granules in
CC blastula-stage embryos (PubMed:16611242). Weak, if any, expression
CC during larval stages (PubMed:11702779). {ECO:0000269|PubMed:11702779,
CC ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16611242,
CC ECO:0000269|PubMed:18417623, ECO:0000269|PubMed:18854162}.
CC -!- PTM: Phosphorylation by mbk-2 and by gsk-3 are required for its rapid
CC degradation following meiosis II. {ECO:0000269|PubMed:16289132,
CC ECO:0000269|PubMed:16338136, ECO:0000269|PubMed:16343905}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:12296824,
CC PubMed:12781695). Double knockout with oma-2 results in sterility due
CC to an oocyte maturation defect (PubMed:11702779). The oocyte maturation
CC defect is due to a meiotic defect in oocytes in which the maturation
CC process is initiated, but there is no progression beyond the prophase
CC stage of meiosis and therefore the cell division process is not
CC completed (PubMed:11702779). Animals also have a larger number of
CC oocytes which are larger in size, but the oocytes cannot be fertilized
CC and accumulate within the gonad (PubMed:11702779). Double RNAi-mediated
CC knockdown with oma-2 in embryos results in more widely distributed P-
CC granules compared to wild-type embryos, and an irregular distribution
CC of germline proteins including pgl-1, mex-1 and pie-1
CC (PubMed:16611242). Double RNAi-mediated knockdown with oma-2 in larva
CC at the L4 stage of development results in 93% embryonic lethality
CC following the first mitotic cleavage in offspring (PubMed:16611242).
CC Double RNAi-mediated knockdown with oma-2 in adults results in a 60%
CC reduction in number of eggs laid (PubMed:12296824). These animals also
CC have an expanded proximal gonad arm which contains larger number of
CC proximal oocytes which in turn contain a larger number of germinal
CC vesicles and higher expression of maternal mRNAs including nos-2
CC (PubMed:12296824, PubMed:18417623). Furthermore, after the diakinesis
CC stage following meiosis I, the germinal vesicles have dispersed
CC chromosomes and an abnormal distribution of P-granules
CC (PubMed:12296824). Embryos also display cell division (PubMed:19786575,
CC PubMed:20826530). In addition, there is increased expression of target
CC transcripts such as taf-4 and mei-1 which also exhibit an altered
CC localization in oocytes and embryos (PubMed:18854162, PubMed:19786575,
CC PubMed:25261697). Reduced expression of the maternal transcriptional
CC repressor protein pie-1 (PubMed:20826530). Double RNAi-mediated
CC knockdown with moe-3 results in a 20% reduction in number of eggs laid
CC (PubMed:12296824). Triple RNAi-mediated knockdown with oma-2 and moe-3
CC results in an 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; BX284604; CAA90977.1; -; Genomic_DNA.
DR PIR; T19155; T19155.
DR RefSeq; NP_501542.1; NM_069141.3.
DR AlphaFoldDB; G5EC86; -.
DR IntAct; G5EC86; 1.
DR STRING; 6239.C09G9.6; -.
DR iPTMnet; G5EC86; -.
DR EPD; G5EC86; -.
DR PaxDb; G5EC86; -.
DR PeptideAtlas; G5EC86; -.
DR EnsemblMetazoa; C09G9.6.1; C09G9.6.1; WBGene00003864.
DR GeneID; 177703; -.
DR KEGG; cel:CELE_C09G9.6; -.
DR CTD; 177703; -.
DR WormBase; C09G9.6; CE03005; WBGene00003864; oma-1.
DR eggNOG; KOG1677; Eukaryota.
DR GeneTree; ENSGT00970000196212; -.
DR HOGENOM; CLU_062303_0_0_1; -.
DR InParanoid; G5EC86; -.
DR OMA; EDIAFNQ; -.
DR OrthoDB; 1158075at2759; -.
DR PhylomeDB; G5EC86; -.
DR PRO; PR:G5EC86; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003864; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:WormBase.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IGI:UniProtKB.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:UniProtKB.
DR GO; GO:0061031; P:endodermal digestive tract morphogenesis; IMP: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:0042664; P:negative regulation of endodermal cell fate specification; IMP:UniProtKB.
DR GO; GO:1904145; P:negative regulation of meiotic cell cycle process involved in oocyte maturation; IGI:UniProtKB.
DR GO; GO:0042662; P:negative regulation of mesodermal cell fate specification; IMP:UniProtKB.
DR GO; GO:0060280; P:negative regulation of ovulation; IGI:UniProtKB.
DR GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IMP: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:0043282; P:pharyngeal muscle development; IMP:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP: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:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; IGI:UniProtKB.
DR GO; GO:1903224; P:regulation of endodermal cell differentiation; IGI:UniProtKB.
DR GO; GO:0042661; P:regulation of mesodermal cell fate specification; 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; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Ribonucleoprotein; RNA-binding; Translation regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..407
FT /note="CCCH-type zinc finger protein oma-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438916"
FT ZN_FING 112..140
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 154..182
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..80
FT /note="Required for taf-4 binding"
FT /evidence="ECO:0000269|PubMed:18854162"
FT MOD_RES 239
FT /note="Phosphothreonine; by mbk-2 and GSK3"
FT /evidence="ECO:0000269|PubMed:16289132,
FT ECO:0000269|PubMed:16343905"
FT MOD_RES 302
FT /note="Phosphoserine; by mbk-2"
FT /evidence="ECO:0000269|PubMed:16289132,
FT ECO:0000269|PubMed:16343905"
FT MOD_RES 339
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000269|PubMed:16289132"
FT MUTAGEN 138
FT /note="G->E: In te36; sterile."
FT /evidence="ECO:0000269|PubMed:11702779"
FT MUTAGEN 141
FT /note="E->K: In te21; sterile."
FT /evidence="ECO:0000269|PubMed:11702779"
FT MUTAGEN 172
FT /note="G->A: In te22; sterile."
FT /evidence="ECO:0000269|PubMed:11702779"
FT MUTAGEN 238
FT /note="S->A: Severely reduced phosphorylation by mbk-2;
FT when associated with A-239."
FT /evidence="ECO:0000269|PubMed:16343905"
FT MUTAGEN 239
FT /note="T->A: Reduced phosphorylation by mbk-2. Severely
FT reduced phosphorylation by mbk-2; when associated with A-
FT 238 or A-302. Reduced phosphorylation by GSK3. Severely
FT reduced phosphorylation by GSK3; when associated with A-
FT 339."
FT /evidence="ECO:0000269|PubMed:16289132"
FT MUTAGEN 239
FT /note="T->D,E: Slight reduction in phosphorylation by gsk-
FT 3."
FT /evidence="ECO:0000269|PubMed:16289132"
FT MUTAGEN 240
FT /note="P->L: In zu405; gain of function mutation and
FT maternal-effect embryonic lethal due to improper
FT degradation of the oma-1 protein in the embryo. Reduced
FT phosphorylation by mbk-2. Severely reduced phosphorylation
FT by mbk-2; when associated with A-302."
FT /evidence="ECO:0000269|PubMed:11702779,
FT ECO:0000269|PubMed:12781695, ECO:0000269|PubMed:16289132,
FT ECO:0000269|PubMed:16338136, ECO:0000269|PubMed:16343905"
FT MUTAGEN 302
FT /note="S->A: Reduced phosphorylation by mbk-2. Severely
FT reduced phosphorylation by mbk-2; when associated with A-
FT 239 or L-240."
FT /evidence="ECO:0000269|PubMed:16289132,
FT ECO:0000269|PubMed:16343905"
FT MUTAGEN 339
FT /note="T->A: Reduced phosphorylation by GSK3. Severely
FT reduced phosphorylation by GSK3; when associated with A-
FT 239."
FT /evidence="ECO:0000269|PubMed:16289132"
SQ SEQUENCE 407 AA; 44500 MW; 272229D1C0920738 CRC64;
MNVNGENNEK IDEHHLESSL AGVPTLPVSP LDHAKDLSQT NPNAQIGDLV TQTANLIAIK
KQLLEDIAFN QHIQSMQVRA IQSFPQNNQV APPFQQFDPR RRGLARMQKP ESYKTVICQA
WLESKTCSFA DNCRFAHGEE ELRPTFVEPL QNNKYKTKLC DKYTTTGLCP YGKRCLFIHP
DHGPNAYIRA DKLLEVSQRH ALADIRDQME QHIMTNGRIA APPLSAIQHP LEMFARPSTP
DEPAAKLPLG PTPVSTRGPR YELPTKELHD AEGAMTYPPS RWPLDPSMFA LDAWNMAHRP
ASPLDSMVLG SAPNAGSFGM LGKQNTPGGV SGYSSAGSTP SQDLSSSSLN AASAAAAAAY
FANSAVAQSL LMKSVATDPM MSCNGPFSPM PGFDQLAENM TKHLNLW
