OOEP_MOUSE
ID OOEP_MOUSE Reviewed; 164 AA.
AC Q9CWE6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Oocyte-expressed protein homolog;
DE AltName: Full=Factor located in oocytes permitting embryonic development;
DE Short=Floped;
DE AltName: Full=Oocyte- and embryo-specific protein 19;
DE Short=mOEP19;
DE AltName: Full=STAT3 downstream gene and differentiation regulator;
GN Name=Ooep; Synonyms=Oep19, Sddr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Oocyte;
RA Chertihin O.I., Digilio L.C., Jha K.N., Herr J.C.;
RT "MOEP19 is mouse oocyte and embryo specific protein that persists in the
RT apical cortex of blastomeres defining cell polarity.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miura M., Takao Y., Koide H., Yokota T.;
RT "STAT3 downstream gene, Sddr (STAT3 downstream gene and differentiation
RT regulator), inhibits differentiation of ES cells.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE SCMC COMPLEX WITH KHDC3; NLRP5 AND TLE6,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18804437; DOI=10.1016/j.devcel.2008.07.010;
RA Li L., Baibakov B., Dean J.;
RT "A subcortical maternal complex essential for preimplantation mouse
RT embryogenesis.";
RL Dev. Cell 15:416-425(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25208553; DOI=10.1038/ncomms5887;
RA Yu X.J., Yi Z., Gao Z., Qin D., Zhai Y., Chen X., Ou-Yang Y., Wang Z.B.,
RA Zheng P., Zhu M.S., Wang H., Sun Q.Y., Dean J., Li L.;
RT "The subcortical maternal complex controls symmetric division of mouse
RT zygotes by regulating F-actin dynamics.";
RL Nat. Commun. 5:4887-4887(2014).
RN [7]
RP IDENTIFICATION IN THE SCMC COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=28992324; DOI=10.1093/jmcb/mjx035;
RA Gao Z., Zhang X., Yu X., Qin D., Xiao Y., Yu Y., Xiang Y., Nie X., Lu X.,
RA Liu W., Yi Z., Li L.;
RT "Zbed3 participates in the subcortical maternal complex and regulates the
RT distribution of organelles.";
RL J. Mol. Cell Biol. 10:74-88(2018).
RN [8]
RP FUNCTION, INTERACTION WITH KHD3C; BLM AND TRIM25, AND SUBCELLULAR LOCATION.
RX PubMed=29125140; DOI=10.1038/cr.2017.139;
RA Zhao B., Zhang W., Cun Y., Li J., Liu Y., Gao J., Zhu H., Zhou H.,
RA Zhang R., Zheng P.;
RT "Mouse embryonic stem cells have increased capacity for replication fork
RT restart driven by the specific Filia-Floped protein complex.";
RL Cell Res. 28:69-89(2018).
RN [9]
RP FUNCTION, INDUCTION BY ETOPOSIDE, AND DISRUPTION PHENOTYPE.
RX PubMed=29955025; DOI=10.24272/j.issn.2095-8137.2018.067;
RA He D.J., Wang L., Zhang Z.B., Guo K., Li J.Z., He X.C., Cui Q.H., Zheng P.;
RT "Maternal gene Ooep may participate in homologous recombination-mediated
RT DNA double-strand break repair in mouse oocytes.";
RL Dong Wu Xue Yan Jiu 39:387-395(2018).
RN [10]
RP INTERACTION WITH TLE6 AND NLRP4F, AND DEVELOPMENTAL STAGE.
RX PubMed=31575650; DOI=10.1242/dev.183616;
RA Qin D., Gao Z., Xiao Y., Zhang X., Ma H., Yu X., Nie X., Fan N., Wang X.,
RA Ouyang Y., Sun Q.Y., Yi Z., Li L.;
RT "The subcortical maternal complex protein Nlrp4f is involved in cytoplasmic
RT lattice formation and organelle distribution.";
RL Development 146:0-0(2019).
CC -!- FUNCTION: As part of the OOEP-KHDC3 scaffold, recruits BLM and TRIM25
CC to DNA replication forks, thereby promoting the ubiquitination of BLM
CC by TRIM25, enhancing BLM retainment at replication forks and therefore
CC promoting stalled replication fork restart (PubMed:29125140).
CC Positively regulates the homologous recombination-mediated DNA double-
CC strand break (DSB) repair pathway by regulating ATM activation and
CC RAD51 recruitment to DSBs in oocytes (PubMed:29955025). Thereby
CC contributes to oocyte survival and the resumption and completion of
CC meiosis (PubMed:29955025). As a member of the subcortical maternal
CC complex (SCMC), plays an essential role for zygotes to progress beyond
CC the first embryonic cell divisions via regulation of actin dynamics
CC (PubMed:18804437, PubMed:25208553). Required for the formation of F-
CC actin cytoplasmic lattices in oocytes which in turn are responsible for
CC symmetric division of zygotes via the regulation of mitotic spindle
CC formation and positioning (PubMed:25208553).
CC {ECO:0000269|PubMed:18804437, ECO:0000269|PubMed:25208553,
CC ECO:0000269|PubMed:29125140, ECO:0000269|PubMed:29955025}.
CC -!- SUBUNIT: Component of the subcortical maternal complex (SCMC), at least
CC composed of NLRP5, KHDC3, OOEP, and TLE6 (PubMed:18804437,
CC PubMed:28992324). Within the complex, interacts with NLRP5, KHDC3 and
CC TLE6 (PubMed:18804437, PubMed:31575650). The SCMC may facilitate
CC translocation of its components between the nuclear and cytoplasmic
CC compartments (By similarity). As part of the SCMC interacts with the
CC SCMC-associated protein NLRP4F (PubMed:31575650). Forms a scaffold
CC complex with KHDC3/FILIA, and interacts with BLM and TRIM25 at DNA
CC replication forks (PubMed:29125140). {ECO:0000250|UniProtKB:A6NGQ2,
CC ECO:0000269|PubMed:18804437, ECO:0000269|PubMed:28992324,
CC ECO:0000269|PubMed:29125140, ECO:0000269|PubMed:31575650}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18804437}. Nucleus
CC {ECO:0000269|PubMed:29125140}. Note=In the subcortical cytoplasm of
CC early embryos from the 1-cell to the blastocyst stages
CC (PubMed:18804437, PubMed:25208553). From the 2-cell stage, still
CC detected in the subcortex, but excluded from cell-cell contact regions
CC (PubMed:18804437). Expression largely disappears in blastocysts
CC (PubMed:25208553). {ECO:0000269|PubMed:18804437,
CC ECO:0000269|PubMed:25208553}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries, where it is restricted to
CC growing oocytes, with greatest levels in fully grown oocytes.
CC {ECO:0000269|PubMed:18804437}.
CC -!- DEVELOPMENTAL STAGE: Transcripts first detected at 15.5 dpc and peak 1
CC week after birth (PubMed:18804437). Transcripts accumulate during
CC oogenesis (PubMed:18804437). During meiotic maturation, the vast
CC majority of the transcripts are degraded and virtually none is detected
CC by 2-cell stage embryogenesis (PubMed:18804437). The protein however
CC persists during preimplantation up to the blastocyst stage
CC (PubMed:18804437). At 2-cell stage, excluded from cell-cell contact
CC regions (PubMed:18804437). Continuous exclusion from these regions
CC during preimplantation development leads to the absence of the protein
CC from the inner cells of the morula and the inner cell mass of the
CC blastocyst (PubMed:18804437). Expressed in ovaries at postnatal day 2
CC (P2), expression peaks at P10, expression is then slightly decreased at
CC P17 and further decreased at P21 (PubMed:31575650).
CC {ECO:0000269|PubMed:18804437, ECO:0000269|PubMed:31575650}.
CC -!- INDUCTION: Induced by etoposide. {ECO:0000269|PubMed:29955025}.
CC -!- DOMAIN: Contains an atypical KH domain with amino acid changes at
CC critical sites, suggesting that it may not bind RNA.
CC -!- DISRUPTION PHENOTYPE: Embryonic death at 2.5 dpc (PubMed:18804437).
CC Progression from embryonic 1- to 2-cell stage delayed 6-8 hours. Less
CC than 20% of the embryos progress beyond 2-cell stage (PubMed:18804437).
CC Embryos form unequal sized blastomeres due to smaller, dysmorphic, and
CC displaced mitotic spindles resulting in asymmetric division
CC (PubMed:25208553). Decrease in thickness of subcortical F-actin in
CC zygotes, thickening of F-actin bundles in the cytoplasm and loss of F-
CC actin cytoplasmic lattices (PubMed:25208553). Decrease in CFL1/Cofilin-
CC 1 expression in the subcortex and diffused distribution in the
CC cytoplasm of zygotes (PubMed:25208553). Decrease in expression of the
CC SCMC component ZBED3 in oocytes (PubMed:28992324). Oocytes exhibit
CC greater amounts of DNA damage and show an inability to repair DNA
CC double strand breaks (PubMed:29955025). Increase in oocyte apoptosis
CC upon treatment with the DNA cross-linking agent cisplatin
CC (PubMed:29955025). Increased number of oocytes in primordial and
CC primary follicles in 4 week old mice, however this number is decreased
CC in 16 week old mice (PubMed:29955025). 4 hour delay in reaching 50%
CC germinal vesicle breakdown (GVB) with a 20% decrease in the number of
CC oocytes that complete GVB. 2 hour delay in reaching 50% polar body
CC extrusion (PBE) with a decrease of 20% in the number of oocytes that
CC complete PBE (PubMed:29955025). {ECO:0000269|PubMed:18804437,
CC ECO:0000269|PubMed:25208553, ECO:0000269|PubMed:28992324,
CC ECO:0000269|PubMed:29955025}.
CC -!- SIMILARITY: Belongs to the KHDC1 family. {ECO:0000305}.
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DR EMBL; DQ238107; ABB30176.1; -; mRNA.
DR EMBL; AB283026; BAF76743.1; -; mRNA.
DR EMBL; AK010809; BAB27195.1; -; mRNA.
DR EMBL; AK133554; BAE21721.1; -; mRNA.
DR EMBL; AK135950; BAE22739.1; -; mRNA.
DR EMBL; AK136199; BAE22871.1; -; mRNA.
DR EMBL; AK145510; BAE26478.1; -; mRNA.
DR EMBL; BC062245; AAH62245.1; -; mRNA.
DR CCDS; CCDS23361.1; -.
DR RefSeq; NP_080756.1; NM_026480.3.
DR AlphaFoldDB; Q9CWE6; -.
DR SMR; Q9CWE6; -.
DR BioGRID; 212570; 3.
DR CORUM; Q9CWE6; -.
DR IntAct; Q9CWE6; 3.
DR STRING; 10090.ENSMUSP00000034900; -.
DR REPRODUCTION-2DPAGE; Q9CWE6; -.
DR PaxDb; Q9CWE6; -.
DR PRIDE; Q9CWE6; -.
DR ProteomicsDB; 293517; -.
DR Antibodypedia; 65863; 16 antibodies from 7 providers.
DR Ensembl; ENSMUST00000034900; ENSMUSP00000034900; ENSMUSG00000032346.
DR GeneID; 67968; -.
DR KEGG; mmu:67968; -.
DR UCSC; uc009quh.2; mouse.
DR CTD; 441161; -.
DR MGI; MGI:1915218; Ooep.
DR VEuPathDB; HostDB:ENSMUSG00000032346; -.
DR eggNOG; ENOG502RU0M; Eukaryota.
DR GeneTree; ENSGT00940000162097; -.
DR HOGENOM; CLU_146793_0_0_1; -.
DR InParanoid; Q9CWE6; -.
DR OMA; PWIRTRP; -.
DR OrthoDB; 1476034at2759; -.
DR PhylomeDB; Q9CWE6; -.
DR TreeFam; TF338690; -.
DR BioGRID-ORCS; 67968; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ooep; mouse.
DR PRO; PR:Q9CWE6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CWE6; protein.
DR Bgee; ENSMUSG00000032346; Expressed in primary oocyte and 64 other tissues.
DR Genevisible; Q9CWE6; MM.
DR GO; GO:0045179; C:apical cortex; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0106333; C:subcortical maternal complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0009880; P:embryonic pattern specification; IDA:MGI.
DR GO; GO:0051293; P:establishment of spindle localization; IMP:UniProtKB.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IDA:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:MGI.
DR GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR CDD; cd12795; FILIA_N_like; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR031952; MOEP19_KH-like.
DR InterPro; IPR040068; OOEP.
DR PANTHER; PTHR19447:SF14; PTHR19447:SF14; 1.
DR Pfam; PF16005; MOEP19; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..164
FT /note="Oocyte-expressed protein homolog"
FT /id="PRO_0000328803"
FT DOMAIN 44..105
FT /note="KH; atypical"
SQ SEQUENCE 164 AA; 18460 MW; 95B121777F282D39 CRC64;
MASHTADADA KPDSDSQKLL NVLPVSLRLR TRPWWFPIQE VSNPLVLYME AWVAERVIGT
DQAEISEIEW MCQALLTVDS VNSGNLAEIT IFGQPSAQTR MKNILLNMAA WHKENELQRA
VKVKEVEEFL KIRASSILSK LSKKGLKLAG FPLPLEGRET QMES
