NANO3_MOUSE
ID NANO3_MOUSE Reviewed; 178 AA.
AC P60324; Q0VDU6;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Nanos homolog 3;
DE Short=NOS-3;
GN Name=Nanos3; Synonyms=Nos3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal gonad;
RX PubMed=12947200; DOI=10.1126/science.1085222;
RA Tsuda M., Sasaoka Y., Kiso M., Abe K., Haraguchi S., Kobayashi S., Saga Y.;
RT "Conserved role of nanos proteins in germ cell development.";
RL Science 301:1239-1241(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17138666; DOI=10.1242/dev.02697;
RA Suzuki A., Tsuda M., Saga Y.;
RT "Functional redundancy among Nanos proteins and a distinct role of Nanos2
RT during male germ cell development.";
RL Development 134:77-83(2007).
RN [4]
RP FUNCTION.
RX PubMed=18436203; DOI=10.1016/j.ydbio.2008.03.020;
RA Suzuki H., Tsuda M., Kiso M., Saga Y.;
RT "Nanos3 maintains the germ cell lineage in the mouse by suppressing both
RT Bax-dependent and -independent apoptotic pathways.";
RL Dev. Biol. 318:133-142(2008).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP PUM2.
RX PubMed=18089289; DOI=10.1016/j.ydbio.2007.11.011;
RA Lolicato F., Marino R., Paronetto M.P., Pellegrini M., Dolci S.,
RA Geremia R., Grimaldi P.;
RT "Potential role of Nanos3 in maintaining the undifferentiated spermatogonia
RT population.";
RL Dev. Biol. 313:725-738(2008).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19861488; DOI=10.1530/rep-09-0373;
RA Yamaji M., Tanaka T., Shigeta M., Chuma S., Saga Y., Saitou M.;
RT "Functional reconstruction of NANOS3 expression in the germ cell lineage by
RT a novel transgenic reporter reveals distinct subcellular localizations of
RT NANOS3.";
RL Reproduction 139:381-393(2010).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21421998; DOI=10.1093/hmg/ddr114;
RA Julaton V.T., Reijo Pera R.A.;
RT "NANOS3 function in human germ cell development.";
RL Hum. Mol. Genet. 20:2238-2250(2011).
CC -!- FUNCTION: Plays a role in the maintenance of the undifferentiated state
CC of germ cells regulating the spermatogonia cell cycle and inducing a
CC prolonged transit in G1 phase. Affects cell proliferation probably by
CC repressing translation of specific mRNAs. Maintains the germ cell
CC lineage by suppressing both Bax-dependent and -independent apoptotic
CC pathways. Essential in the early stage embryo to protect the migrating
CC primordial germ cells (PGCs) from apoptosis.
CC {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:17138666,
CC ECO:0000269|PubMed:18089289, ECO:0000269|PubMed:18436203}.
CC -!- SUBUNIT: Binds mRNA from germ cells. Interacts with PUM2.
CC {ECO:0000269|PubMed:18089289}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19861488,
CC ECO:0000269|PubMed:21421998}. Cytoplasm {ECO:0000269|PubMed:19861488,
CC ECO:0000269|PubMed:21421998}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:19861488}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:19861488}. Note=Co-localizes with PUM2, EIF2S1 and
CC TIAL1 in the stress granules. Co-localizes with DCP1A in the P-body.
CC {ECO:0000269|PubMed:19861488}.
CC -!- TISSUE SPECIFICITY: Expressed in undifferentiated spermatogonial cells.
CC {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:18089289,
CC ECO:0000269|PubMed:19861488}.
CC -!- DEVELOPMENTAL STAGE: Found in the male and female gonads of early
CC embryo and, after birth, it is found only in the testis. Expressed in
CC primordial germ cells (PGCs) until 14.5 dpc in male gonad and until
CC 13.5 dpc in female gonad; after this age its expression disappears and
CC then it is found after birth only in male germ cells.
CC {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:17138666,
CC ECO:0000269|PubMed:18089289, ECO:0000269|PubMed:19861488}.
CC -!- DOMAIN: The Nanos-type zinc finger is composed of two C2HC motifs, each
CC motif binding one molecule of zinc. It is essential for the translation
CC repression activity of the protein. {ECO:0000255|PROSITE-
CC ProRule:PRU00855}.
CC -!- SIMILARITY: Belongs to the nanos family. {ECO:0000255|PROSITE-
CC ProRule:PRU00855}.
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DR EMBL; AB095973; BAC82558.1; -; mRNA.
DR EMBL; BC119513; AAI19514.1; -; mRNA.
DR CCDS; CCDS22470.1; -.
DR RefSeq; NP_918948.1; NM_194059.2.
DR AlphaFoldDB; P60324; -.
DR SMR; P60324; -.
DR BioGRID; 232660; 2.
DR STRING; 10090.ENSMUSP00000067385; -.
DR iPTMnet; P60324; -.
DR PhosphoSitePlus; P60324; -.
DR PaxDb; P60324; -.
DR PRIDE; P60324; -.
DR Antibodypedia; 26509; 131 antibodies from 28 providers.
DR DNASU; 244551; -.
DR Ensembl; ENSMUST00000070102; ENSMUSP00000067385; ENSMUSG00000056155.
DR GeneID; 244551; -.
DR KEGG; mmu:244551; -.
DR UCSC; uc009mme.1; mouse.
DR CTD; 342977; -.
DR MGI; MGI:2675387; Nanos3.
DR VEuPathDB; HostDB:ENSMUSG00000056155; -.
DR eggNOG; KOG4602; Eukaryota.
DR GeneTree; ENSGT00950000183135; -.
DR HOGENOM; CLU_094055_1_0_1; -.
DR InParanoid; P60324; -.
DR OMA; GYMSVYS; -.
DR OrthoDB; 1198436at2759; -.
DR PhylomeDB; P60324; -.
DR TreeFam; TF326882; -.
DR BioGRID-ORCS; 244551; 2 hits in 73 CRISPR screens.
DR PRO; PR:P60324; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P60324; protein.
DR Bgee; ENSMUSG00000056155; Expressed in morula and 59 other tissues.
DR ExpressionAtlas; P60324; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0007281; P:germ cell development; ISS:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0048477; P:oogenesis; IMP:MGI.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IDA:UniProtKB.
DR Gene3D; 4.10.60.30; -; 1.
DR InterPro; IPR008705; Nanos/Xcar2.
DR InterPro; IPR038129; Nanos_sf.
DR InterPro; IPR024161; Znf_nanos-typ.
DR PANTHER; PTHR12887; PTHR12887; 1.
DR Pfam; PF05741; zf-nanos; 1.
DR PROSITE; PS51522; ZF_NANOS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Metal-binding; Nucleus;
KW Oogenesis; Reference proteome; RNA-binding; Spermatogenesis;
KW Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..178
FT /note="Nanos homolog 3"
FT /id="PRO_0000207690"
FT ZN_FING 56..110
FT /note="Nanos-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT REGION 25..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 57..84
FT /note="C2HC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT MOTIF 92..108
FT /note="C2HC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
SQ SEQUENCE 178 AA; 19241 MW; 4E582B698FC715E7 CRC64;
MGTFNLWTDY LGLARLVGAL HKEEELDVRL DPKPEPKPSS ESQQASKESS AAPERLCSFC
KHNGESRAIY QSHVLKDEAG RVLCPILRDY VCPQCGATQE HAHTRRFCPL TSQGYTSVYC
YTTRNSAGKK LTRPDKAKTQ DAGHRLGGEA AAGVYAGSKS GRKPPGPSPS ACCPSTTA
