NANO2_MOUSE
ID NANO2_MOUSE Reviewed; 136 AA.
AC P60322; F8VQ09;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Nanos homolog 2;
DE Short=NOS-2;
GN Name=Nanos2; Synonyms=Nos2;
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, AND TISSUE 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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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=18281459; DOI=10.1101/gad.1612708;
RA Suzuki A., Saga Y.;
RT "Nanos2 suppresses meiosis and promotes male germ cell differentiation.";
RL Genes Dev. 22:430-435(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19745153; DOI=10.1126/science.1172645;
RA Sada A., Suzuki A., Suzuki H., Saga Y.;
RT "The RNA-binding protein NANOS2 is required to maintain murine
RT spermatogonial stem cells.";
RL Science 325:1394-1398(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CNOT1; CNOT3; CNOT6L;
RP CNOT7 AND CNOT9, AND DEVELOPMENTAL STAGE.
RX PubMed=20133598; DOI=10.1073/pnas.0908664107;
RA Suzuki A., Igarashi K., Aisaki K., Kanno J., Saga Y.;
RT "NANOS2 interacts with the CCR4-NOT deadenylation complex and leads to
RT suppression of specific RNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3594-3599(2010).
CC -!- FUNCTION: Plays a key role in the sexual differentiation of germ cells
CC by promoting the male fate but suppressing the female fate. Represses
CC the female fate pathways by suppressing meiosis, which in turn results
CC in the promotion of the male fate. Maintains the suppression of meiosis
CC by preventing STRA8 expression, which is required for premeiotic DNA
CC replication, after CYP26B1 is decreased. Regulates the localization of
CC the CCR4-NOT deadenylation complex to P-bodies and plays a role in
CC recruiting the complex to trigger the degradation of mRNAs involved in
CC meiosis. Required for the maintenance of the spermatogonial stem cell
CC population. Not essential for the assembly of P-bodies but is required
CC for the maintenance of their normal state.
CC {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:17138666,
CC ECO:0000269|PubMed:18281459, ECO:0000269|PubMed:19745153,
CC ECO:0000269|PubMed:20133598}.
CC -!- SUBUNIT: Interacts with CNOT1, CNOT3, CNOT6L, CNOT7 and CNOT9.
CC {ECO:0000269|PubMed:20133598}.
CC -!- INTERACTION:
CC P60322; Q6ZQ08: Cnot1; NbExp=3; IntAct=EBI-6507212, EBI-682479;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20133598}.
CC Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Note=More abundant in perinuclear region of the
CC cytoplasm of the germ cells of the adult testis (By similarity).
CC Localizes at P-bodies during gonocyte development. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in male germ cells.
CC Expressed in self-renewing spermatogonial stem cells and developing
CC gonads. {ECO:0000269|PubMed:12947200, ECO:0000269|PubMed:19745153}.
CC -!- DEVELOPMENTAL STAGE: First detectable at 13.5 dpc in the male
CC gonocytes, levels increase until about 16.5 dpc and then slightly
CC decrease by 17.5 dpc (at protein level). Expression is maintained in
CC all male gonocytes during embryogenesis, but becomes confined to a
CC small population of the spermatogonia after birth.
CC {ECO:0000269|PubMed:17138666, ECO:0000269|PubMed:20133598}.
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 -!- DISRUPTION PHENOTYPE: Mice show a gradual loss of the germ cell
CC population within a few cycles of spermatogenesis which is caused by
CC the depletion of spermatogonial stem cells that produce differentiating
CC spermatogenic cells. {ECO:0000269|PubMed:19745153}.
CC -!- SIMILARITY: Belongs to the nanos family. {ECO:0000255|PROSITE-
CC ProRule:PRU00855}.
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DR EMBL; AB095972; BAC82557.1; -; mRNA.
DR EMBL; AC170864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS20883.1; -.
DR RefSeq; NP_918953.2; NM_194064.2.
DR AlphaFoldDB; P60322; -.
DR SMR; P60322; -.
DR BioGRID; 237543; 1.
DR DIP; DIP-59508N; -.
DR ELM; P60322; -.
DR IntAct; P60322; 7.
DR STRING; 10090.ENSMUSP00000069765; -.
DR BindingDB; P60322; -.
DR SwissPalm; P60322; -.
DR jPOST; P60322; -.
DR PaxDb; P60322; -.
DR PRIDE; P60322; -.
DR Antibodypedia; 31412; 259 antibodies from 30 providers.
DR DNASU; 378430; -.
DR Ensembl; ENSMUST00000063563; ENSMUSP00000069765; ENSMUSG00000051965.
DR GeneID; 378430; -.
DR KEGG; mmu:378430; -.
DR UCSC; uc009fjz.1; mouse.
DR CTD; 339345; -.
DR MGI; MGI:2676627; Nanos2.
DR VEuPathDB; HostDB:ENSMUSG00000051965; -.
DR eggNOG; KOG4602; Eukaryota.
DR GeneTree; ENSGT00950000183135; -.
DR HOGENOM; CLU_094055_1_1_1; -.
DR InParanoid; P60322; -.
DR OMA; RHVYASH; -.
DR OrthoDB; 1198436at2759; -.
DR PhylomeDB; P60322; -.
DR TreeFam; TF326882; -.
DR BioGRID-ORCS; 378430; 3 hits in 72 CRISPR screens.
DR PRO; PR:P60322; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P60322; protein.
DR Bgee; ENSMUSG00000051965; Expressed in animal zygote and 31 other tissues.
DR ExpressionAtlas; P60322; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0048477; P:oogenesis; IBA:GO_Central.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP: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;
KW Reference proteome; RNA-binding; Spermatogenesis; Translation regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..136
FT /note="Nanos homolog 2"
FT /id="PRO_0000207688"
FT ZN_FING 60..114
FT /note="Nanos-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT REGION 27..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 61..88
FT /note="C2HC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT MOTIF 96..112
FT /note="C2HC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT COMPBIAS 27..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT CONFLICT 46
FT /note="S -> T (in Ref. 1; BAC82557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 15597 MW; 6D58AF6DD7DD63B1 CRC64;
MDLPPFDMWR DYFNLSQVVM DIIQSRKQRQ EGEVAEEPNS RPQEKSEQDL EGYPGCLPTI
CNFCKHNGES RHVYTSHQLK TPEGVVVCPI LRHYVCPLCG ATGDQAHTLK YCPLNSSQQS
LYRRSGRNSA GRRVKR
