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OOEP_PAPAN
ID   OOEP_PAPAN              Reviewed;         149 AA.
AC   A9X185;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Oocyte-expressed protein homolog;
GN   Name=OOEP;
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA   Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA   Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA   Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA   Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA   Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA   Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA   Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA   Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA   Tsipouri V., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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 (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, KHDC3, OOEP, and TLE6 (By similarity). Within the
CC       complex, interacts with NLRP5, KHDC3 and TLE6 (By similarity). As part
CC       of the SCMC interacts with the SCMC-associated protein NLRP4F (By
CC       similarity). The SCMC may facilitate translocation of its components
CC       between the nuclear and cytoplasmic compartments (By similarity). Forms
CC       a scaffold complex with KHDC3/FILIA, and interacts with BLM and TRIM25
CC       at DNA replication forks (By similarity).
CC       {ECO:0000250|UniProtKB:A6NGQ2, ECO:0000250|UniProtKB:Q9CWE6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CWE6}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9CWE6}.
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; DP000541; ABY40780.1; -; Genomic_DNA.
DR   RefSeq; NP_001162409.1; NM_001168938.1.
DR   AlphaFoldDB; A9X185; -.
DR   SMR; A9X185; -.
DR   STRING; 9555.ENSPANP00000015997; -.
DR   GeneID; 100137404; -.
DR   KEGG; panu:100137404; -.
DR   CTD; 441161; -.
DR   eggNOG; ENOG502RU0M; Eukaryota.
DR   OrthoDB; 1476034at2759; -.
DR   Proteomes; UP000028761; Unplaced.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR   GO; GO:0051293; P:establishment of spindle localization; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..149
FT                   /note="Oocyte-expressed protein homolog"
FT                   /id="PRO_0000328804"
FT   DOMAIN          49..110
FT                   /note="KH; atypical"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   149 AA;  17021 MW;  F401728DB7125F05 CRC64;
     MVDDAGTAES QRGKQTPADS LEQLRMLPLP PPQIRIRPWW FPVQELRDPL VFYLEAWLAD
     ELFGPDRAMI PEMEWTSQAL MTVDIVDSGN LVEITVFGRP SVQNRVKSML LCLASFHREH
     RARAEKMKHL EKNLKAHASD PHSPQDPVA
 
 
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