ID OOEP_HUMAN Reviewed; 149 AA. AC A6NGQ2; A6NIN5; A9UIB7; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 25-MAY-2022, entry version 101. DE RecName: Full=Oocyte-expressed protein homolog; DE AltName: Full=KH homology domain-containing protein 2; DE AltName: Full=Oocyte- and embryo-specific protein 19; DE Short=hOEP19; GN Name=OOEP; Synonyms=C6orf156, KHDC2, OEP19; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-92. RA Chertihin O., Herr J.C.; RT "Human oocyte and embryo protein (HOEP19)."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] RP IDENTIFICATION. RX PubMed=17913455; DOI=10.1016/j.ygeno.2007.06.003; RA Pierre A., Gautier M., Callebaut I., Bontoux M., Jeanpierre E., RA Pontarotti P., Monget P.; RT "Atypical structure and phylogenomic evolution of the new eutherian RT oocyte- and embryo-expressed KHDC1/DPPA5/ECAT1/OOEP gene family."; RL Genomics 90:583-594(2007). RN [4] RP INTERACTION WITH TLE6. RX PubMed=26537248; DOI=10.1186/s13059-015-0792-0; RA Alazami A.M., Awad S.M., Coskun S., Al-Hassan S., Hijazi H., RA Abdulwahab F.M., Poizat C., Alkuraya F.S.; RT "TLE6 mutation causes the earliest known human embryonic lethality."; RL Genome Biol. 16:R240.1-R240.8(2015). RN [5] RP IDENTIFICATION IN THE SCMC COMPLEX, SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RX PubMed=25542835; DOI=10.1093/molehr/gau116; RA Zhu K., Yan L., Zhang X., Lu X., Wang T., Yan J., Liu X., Qiao J., Li L.; RT "Identification of a human subcortical maternal complex."; RL Mol. Hum. Reprod. 21:320-329(2015). CC -!- FUNCTION: As part of the OOEP-KHDC3L 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 (By similarity). Positively CC regulates the homologous recombination-mediated DNA double-strand break CC (DSB) repair pathway by regulating ATM activation and RAD51 recruitment CC to DSBs in oocytes (By similarity). Thereby contributes to oocyte CC survival and the resumption and completion of meiosis (By similarity). CC As a member of the subcortical maternal complex (SCMC), plays an CC essential role for zygotes to progress beyond the first embryonic cell CC divisions via regulation of actin dynamics (By similarity). Required CC for the formation of F-actin cytoplasmic lattices in oocytes which in CC turn are responsible for symmetric division of zygotes via the CC regulation of mitotic spindle formation and positioning (By CC similarity). {ECO:0000250|UniProtKB:Q9CWE6}. CC -!- SUBUNIT: Component of the subcortical maternal complex (SCMC), at least CC composed of NLRP5, KHDC3L, OOEP, and TLE6 isoform 1 (PubMed:26537248, CC PubMed:25542835). Within the complex, interacts with NLRP5, KHDC3L and CC TLE6 isoform 1 (PubMed:26537248, PubMed:25542835). As part of the SCMC CC interacts with the SCMC-associated protein NLRP4F (By similarity). The CC SCMC may facilitate translocation of its components between the nuclear CC and cytoplasmic compartments (PubMed:25542835). Forms a scaffold CC complex with KHDC3L/FILIA, and interacts with BLM and TRIM25 at DNA CC replication forks (By similarity). {ECO:0000250|UniProtKB:Q9CWE6, CC ECO:0000269|PubMed:25542835, ECO:0000269|PubMed:26537248}. CC -!- INTERACTION: CC A6NGQ2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-18583589, EBI-11096309; CC A6NGQ2; P09917: ALOX5; NbExp=3; IntAct=EBI-18583589, EBI-79934; CC A6NGQ2; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-18583589, EBI-8643161; CC A6NGQ2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-18583589, EBI-744099; CC A6NGQ2; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-18583589, EBI-8472129; CC A6NGQ2; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-18583589, EBI-2341787; CC A6NGQ2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-18583589, EBI-741158; CC A6NGQ2; P14678-2: SNRPB; NbExp=3; IntAct=EBI-18583589, EBI-372475; CC A6NGQ2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-18583589, EBI-11955057; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25542835}. Nucleus CC {ECO:0000269|PubMed:25542835}. CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes of the fetal ovary CC (PubMed:25542835). Expressed primarily with other SCMC components in CC the subcortex of oocytes and early embryos (PubMed:25542835). CC Expression is excluded from cell-cell contact regions after the 2-cell CC stage (PubMed:25542835). {ECO:0000269|PubMed:25542835}. CC -!- DOMAIN: Contains an atypical KH domain with amino acid changes at CC critical sites, suggesting that it may not bind RNA. CC -!- SIMILARITY: Belongs to the KHDC1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU290647; ABX84389.1; -; mRNA. DR EMBL; AC019205; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS47451.1; -. DR RefSeq; NP_001073976.1; NM_001080507.2. DR AlphaFoldDB; A6NGQ2; -. DR SMR; A6NGQ2; -. DR BioGRID; 137219; 10. DR CORUM; A6NGQ2; -. DR IntAct; A6NGQ2; 9. DR STRING; 9606.ENSP00000359384; -. DR BioMuta; OOEP; -. DR jPOST; A6NGQ2; -. DR MassIVE; A6NGQ2; -. DR PaxDb; A6NGQ2; -. DR PeptideAtlas; A6NGQ2; -. DR PRIDE; A6NGQ2; -. DR Antibodypedia; 65863; 16 antibodies from 7 providers. DR DNASU; 441161; -. DR Ensembl; ENST00000370359.6; ENSP00000359384.5; ENSG00000203907.10. DR GeneID; 441161; -. DR KEGG; hsa:441161; -. DR MANE-Select; ENST00000370359.6; ENSP00000359384.5; NM_001080507.3; NP_001073976.1. DR UCSC; uc003pgu.5; human. DR CTD; 441161; -. DR GeneCards; OOEP; -. DR HGNC; HGNC:21382; OOEP. DR HPA; ENSG00000203907; Tissue enriched (testis). DR MIM; 611689; gene. DR neXtProt; NX_A6NGQ2; -. DR OpenTargets; ENSG00000203907; -. DR PharmGKB; PA162398414; -. DR VEuPathDB; HostDB:ENSG00000203907; -. DR eggNOG; ENOG502RU0M; Eukaryota. DR GeneTree; ENSGT00940000162097; -. DR HOGENOM; CLU_146793_0_0_1; -. DR InParanoid; A6NGQ2; -. DR OMA; RVRPWWF; -. DR OrthoDB; 1476034at2759; -. DR PhylomeDB; A6NGQ2; -. DR TreeFam; TF338690; -. DR PathwayCommons; A6NGQ2; -. DR SignaLink; A6NGQ2; -. DR BioGRID-ORCS; 441161; 11 hits in 1061 CRISPR screens. DR ChiTaRS; OOEP; human. DR GenomeRNAi; 441161; -. DR Pharos; A6NGQ2; Tdark. DR PRO; PR:A6NGQ2; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; A6NGQ2; protein. DR Bgee; ENSG00000203907; Expressed in oocyte and 99 other tissues. DR ExpressionAtlas; A6NGQ2; baseline and differential. DR Genevisible; A6NGQ2; HS. DR GO; GO:0045179; C:apical cortex; IBA:GO_Central. DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0106333; C:subcortical maternal complex; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB. DR GO; GO:0009880; P:embryonic pattern specification; IBA:GO_Central. DR GO; GO:0051293; P:establishment of spindle localization; ISS:UniProtKB. DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IBA:GO_Central. DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISS:UniProtKB. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB. DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; ISS:UniProtKB. DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB. DR GO; GO:0070201; P:regulation of establishment of protein localization; ISS:UniProtKB. DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB. DR GO; GO:0031297; P:replication fork processing; ISS: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..149 FT /note="Oocyte-expressed protein homolog" FT /id="PRO_0000328802" FT DOMAIN 49..110 FT /note="KH; atypical" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 18 FT /note="A -> T (in dbSNP:rs2280286)" FT /id="VAR_042523" FT VARIANT 92 FT /note="V -> A (in dbSNP:rs496530)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_042524" SQ SEQUENCE 149 AA; 17170 MW; E7C726FB46909404 CRC64; MVDDAGAAES QRGKQTPAHS LEQLRRLPLP PPQIRIRPWW FPVQELRDPL VFYLEAWLAD ELFGPDRAII PEMEWTSQAL LTVDIVDSGN LVEITVFGRP RVQNRVKSML LCLAWFHREH RARAEKMKHL EKNLKAHASD PHSPQDPVA //