OOEP_HUMAN
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 03-AUG-2022, entry version 102.
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}.
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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 93 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
