ID KHDC3_RAT Reviewed; 434 AA.
AC D3ZVV1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=KH domain-containing protein 3 {ECO:0000250|UniProtKB:Q587J8};
DE AltName: Full=Protein Filia {ECO:0000250|UniProtKB:Q9CWU5};
GN Name=Khdc3 {ECO:0000312|RGD:1311617};
GN Synonyms=Ecat1 {ECO:0000303|PubMed:17913455};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
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). Regulates
CC homologous recombination-mediated DNA repair via recruitment of RAD51
CC to sites of DNA double-strand breaks, and sustainment of PARP1
CC activity, which in turn modulates downstream ATM activation (By
CC similarity). Activation of ATM or ATR in response to DNA double-strand
CC breaks may be cell-type specific (By similarity). Its role in DNA
CC double-strand break repair is independent of its role in restarting
CC stalled replication forks (By similarity). As a member of the
CC subcortical maternal complex (SCMC), plays an essential role for
CC zygotes to progress beyond the first embryonic cell divisions via
CC regulation of actin dynamics (By similarity). Required for maintenance
CC of euploidy during cleavage-stage embryogenesis (By similarity).
CC Required for the formation of F-actin cytoplasmic lattices in oocytes
CC which in turn are responsible for symmetric division of zygotes via the
CC regulation of mitotic spindle formation and positioning (By
CC similarity). Ensures proper spindle assembly by regulating the
CC localization of AURKA via RHOA signaling and of PLK1 via a RHOA-
CC independent process (By similarity). Required for the localization of
CC MAD2L1 to kinetochores to enable spindle assembly checkpoint function
CC (By similarity). Promotes neural stem cell neurogenesis and neuronal
CC differentiation in the hippocampus (By similarity). May regulate normal
CC development of learning, memory and anxiety (By similarity). Capable of
CC binding RNA (By similarity). {ECO:0000250|UniProtKB:Q9CWU5}.
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). The SCMC
CC may facilitate translocation of its components between the nuclear and
CC cytoplasmic compartments (By similarity). Forms a scaffold complex with
CC OOEP/FLOPED, and interacts with BLM and TRIM25 at DNA replication forks
CC (By similarity). Interacts with PARP1; the interaction is increased
CC following the formation of DNA double-strand breaks (By similarity).
CC Interacts (via C-terminus) with NUMA1 (By similarity).
CC {ECO:0000250|UniProtKB:Q587J8, ECO:0000250|UniProtKB:Q9CWU5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q9CWU5}. Nucleus {ECO:0000250|UniProtKB:Q9CWU5}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9CWU5}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9CWU5}. Chromosome
CC {ECO:0000250|UniProtKB:Q587J8}. Note=Localized to centrosomes during
CC interphase and mitosis (By similarity). Localizes to sites of DNA
CC double-strand break repair (By similarity).
CC {ECO:0000250|UniProtKB:Q587J8, ECO:0000250|UniProtKB:Q9CWU5}.
CC -!- DOMAIN: Contains 1 atypical KH domain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KHDC1 family. {ECO:0000305}.
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DR EMBL; CH474041; EDL84106.1; -; Genomic_DNA.
DR RefSeq; NP_001100307.1; NM_001106837.1.
DR AlphaFoldDB; D3ZVV1; -.
DR SMR; D3ZVV1; -.
DR STRING; 10116.ENSRNOP00000074731; -.
DR PhosphoSitePlus; D3ZVV1; -.
DR PaxDb; 10116-ENSRNOP00000032705; -.
DR Ensembl; ENSRNOT00000113238.1; ENSRNOP00000088813.1; ENSRNOG00000054460.2.
DR Ensembl; ENSRNOT00055012060; ENSRNOP00055009562; ENSRNOG00055007243.
DR Ensembl; ENSRNOT00060027227; ENSRNOP00060021839; ENSRNOG00060015883.
DR Ensembl; ENSRNOT00065027405; ENSRNOP00065021534; ENSRNOG00065016463.
DR GeneID; 300826; -.
DR KEGG; rno:300826; -.
DR UCSC; RGD:1311617; rat.
DR AGR; RGD:1311617; -.
DR CTD; 66991; -.
DR RGD; 1311617; Khdc3.
DR eggNOG; ENOG502QQIF; Eukaryota.
DR GeneTree; ENSGT00940000162601; -.
DR HOGENOM; CLU_050702_0_0_1; -.
DR InParanoid; D3ZVV1; -.
DR OMA; AVWRADY; -.
DR OrthoDB; 5263669at2759; -.
DR PhylomeDB; D3ZVV1; -.
DR TreeFam; TF338690; -.
DR PRO; PR:D3ZVV1; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000054460; Expressed in thymus and 4 other cell types or tissues.
DR GO; GO:0045179; C:apical cortex; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0106333; C:subcortical maternal complex; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0051656; P:establishment of organelle localization; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:RGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; 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:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; 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; K Homology domain, type 1; 1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR031952; MOEP19_KH-like.
DR PANTHER; PTHR19447:SF15; KH DOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR19447; OOCYTE-EXPRESSED PROTEIN HOMOLOG-RELATED; 1.
DR Pfam; PF16005; MOEP19; 1.
PE 3: Inferred from homology;
KW Cell cycle; Chromosome; Cytoplasm; Cytoskeleton; Developmental protein;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..434
FT /note="KH domain-containing protein 3"
FT /id="PRO_0000407379"
FT DOMAIN 40..118
FT /note="KH; atypical"
FT REGION 1..39
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q9CWU5"
FT REGION 334..434
FT /note="Required for interaction with NUMA1 and regulation
FT of apoptosis in response to DNA damage"
FT /evidence="ECO:0000250|UniProtKB:Q9CWU5"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q587J8"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q587J8"
SQ SEQUENCE 434 AA; 47179 MW; 8A0F47AF5AF819AB CRC64;
MATLKTFRTL VQLKHKLGKA YEIVGEPRLP KWFHVEYLED PKKMYVEPTL VEIMFGKDGE
HIPHVECTLH VLIHVNVWGP EKQAEILIFG PPNFQKDVAQ MLSNVAHFCR MKLMEKEALE
AGVERRLMAA SKATTQPTPV KVRDAATQVA PVQVRDAAIQ PAPVKVRDAA TQVAPVQVHE
VATQPVPVQV RDAATQPVPV RVRDAATQPV PVRVRDAATQ PVPVRVRDAA TQPVPVRVRD
AATEPVPVQV RDAATQPAPV QVRDAATQPA PVQVRDAATQ PAPVQVRDAA TQPAPVQVRD
AATQPAPVQV RDAATQPAPV QVRDAATQPA PVQVREAATQ QTPVEVADDT QLVQLKAGEA
FAQHTSGKVH QDVNGQSPIE VCEGATQRHS VDASEALSQK CPEDLEGGDT ETSLDDSYVI
IRPSRAVWEP FVML
//
