KHDC3_MACMU
ID KHDC3_MACMU Reviewed; 206 AA.
AC F6SZT2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=KH domain-containing protein 3 {ECO:0000305};
DE AltName: Full=ES cell-associated transcript 1 protein {ECO:0000250|UniProtKB:Q587J8};
DE AltName: Full=KHDC3-like protein {ECO:0000250|UniProtKB:Q587J8};
GN Name=KHDC3L; Synonyms=ECAT1 {ECO:0000250|UniProtKB:Q587J8};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000312|Proteomes:UP000006718};
RN [1] {ECO:0000312|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000312|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=33115731; DOI=10.1126/sciadv.aba0682;
RA Li J., Shang Y., Wang L., Zhao B., Sun C., Li J., Liu S., Li C., Tang M.,
RA Meng F.L., Zheng P.;
RT "Genome integrity and neurogenesis of postnatal hippocampal neural
RT stem/progenitor cells require a unique regulator Filia.";
RL Sci. Adv. 6:0-0(2020).
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:33115731). 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
CC (PubMed:33115731). Activation of ATM or ATR in response to DNA double-
CC strand breaks may be cell-type specific (By similarity). Its role in
CC DNA 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. May regulate normal development of
CC learning, memory and anxiety (By similarity). Capable of binding RNA
CC (By similarity). {ECO:0000250|UniProtKB:D3ZVV1,
CC ECO:0000250|UniProtKB:Q9CWU5, ECO:0000269|PubMed:33115731}.
CC -!- SUBUNIT: Component of the subcortical maternal complex (SCMC), at least
CC composed of NLRP5, KHDC3L, OOEP, and TLE6 (By similarity). Within the
CC complex, interacts with NLRP5, KHDC3L and TLE6 (By similarity). The
CC SCMC may facilitate translocation of its components between the nuclear
CC and cytoplasmic compartments (By similarity). Forms a scaffold complex
CC with OOEP/FLOPED, and interacts with BLM and TRIM25 at DNA replication
CC forks (By similarity). Interacts with PARP1; the interaction is
CC increased following the formation of DNA double-strand breaks (By
CC similarity). Interacts with NUMA1 (By similarity).
CC {ECO:0000250|UniProtKB:D3ZVV1, ECO:0000250|UniProtKB:Q587J8,
CC 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 -!- DEVELOPMENTAL STAGE: Expressed in fetal neural stem progenitor cells in
CC the brain (at protein levels). {ECO:0000269|PubMed:33115731}.
CC -!- INDUCTION: Induced by etoposide and hydroxy urea in neural stem cells.
CC {ECO:0000269|PubMed:33115731}.
CC -!- DOMAIN: Contains 1 atypical KH domain. {ECO:0000250}.
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 SMR; F6SZT2; -.
DR STRING; 9544.ENSMMUP00000013185; -.
DR Ensembl; ENSMMUT00000014079; ENSMMUP00000013185; ENSMMUG00000010084.
DR VEuPathDB; HostDB:ENSMMUG00000010084; -.
DR VGNC; VGNC:73951; KHDC3L.
DR eggNOG; ENOG502QQIF; Eukaryota.
DR GeneTree; ENSGT00940000162601; -.
DR HOGENOM; CLU_115458_0_0_1; -.
DR InParanoid; F6SZT2; -.
DR OrthoDB; 913590at2759; -.
DR TreeFam; TF338690; -.
DR Proteomes; UP000006718; Chromosome 4.
DR Bgee; ENSMMUG00000010084; Expressed in spermatid and 3 other tissues.
DR GO; GO:0045179; C:apical cortex; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0106333; C:subcortical maternal complex; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
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 Pfam; PF16005; MOEP19; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Cytoplasm; Cytoskeleton; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..206
FT /note="KH domain-containing protein 3"
FT /id="PRO_0000453456"
FT DOMAIN 40..103
FT /note="KH; atypical"
FT /evidence="ECO:0000250|UniProtKB:Q587J8"
FT REGION 1..40
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q9CWU5"
FT REGION 144..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q587J8"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CWU5"
SQ SEQUENCE 206 AA; 23241 MW; B81A620C46FF55AE CRC64;
MDTPRRFPTL VQLMQPKAMP VEVLGHLPKR FSWFHSEFLK NPKVVRLEVW LVEKIFGRDR
ERIPHVQGMS QILIHVNRLD PNGEAEILVF GRPSYQEDTI KMIMNLADYH RQLQAKGSGK
ALAQDVATKK AEIQLSSTEV REAGTQRSVE VREVGTQGSP VEVRETGTQQ SLEAANQSGT
QRSPEAASKA VTQRFSEDTR APVTRL
