NANO1_DANRE
ID NANO1_DANRE Reviewed; 228 AA.
AC E7FDB3;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Nanos homolog 1;
GN Name=nanos1; ORFNames=wu:fb76c12;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11691838; DOI=10.1101/gad.212401;
RA Koeprunner M., Thisse C., Thisse B., Raz E.;
RT "A zebrafish nanos-related gene is essential for the development of
RT primordial germ cells.";
RL Genes Dev. 15:2877-2885(2001).
CC -!- FUNCTION: Acts as a translational repressor. Can mediate repression
CC affecting different steps in the translation process: cap-driven, IRES-
CC driven, polyadenylated RNAs or nonpolyadenylated RNAs (By similarity).
CC Essential for the development of primordial germ cells (PGCs) by
CC ensuring their proper migration and survival. {ECO:0000250,
CC ECO:0000269|PubMed:11691838}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11691838}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:11691838}.
CC -!- TISSUE SPECIFICITY: 3'-UTR is sufficient for directing specific
CC expression of this protein in the primordial germ cells (PGCs).
CC {ECO:0000269|PubMed:11691838}.
CC -!- DEVELOPMENTAL STAGE: Present in oocytes and in embryos before the
CC 4- and 256-cell stages. Levels decline and it is barely detectable by
CC the fifth day of development. {ECO:0000269|PubMed:11691838}.
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; CABZ01002992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001292590.1; NM_001305661.1.
DR AlphaFoldDB; E7FDB3; -.
DR SMR; E7FDB3; -.
DR ELM; E7FDB3; -.
DR STRING; 7955.ENSDARP00000098689; -.
DR PaxDb; E7FDB3; -.
DR Ensembl; ENSDART00000189628; ENSDARP00000149427; ENSDARG00000109337.
DR GeneID; 322903; -.
DR KEGG; dre:322903; -.
DR CTD; 340719; -.
DR ZFIN; ZDB-GENE-030131-1623; nanos1.
DR eggNOG; KOG4602; Eukaryota.
DR GeneTree; ENSGT00950000183135; -.
DR HOGENOM; CLU_094055_0_0_1; -.
DR InParanoid; E7FDB3; -.
DR OMA; SYDYTFN; -.
DR OrthoDB; 1633105at2759; -.
DR PhylomeDB; E7FDB3; -.
DR TreeFam; TF326882; -.
DR PRO; PR:E7FDB3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000109337; Expressed in larva and 26 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0060293; C:germ plasm; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Reference proteome; Repressor; RNA-binding;
KW Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..228
FT /note="Nanos homolog 1"
FT /id="PRO_0000409447"
FT ZN_FING 150..204
FT /note="Nanos-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT REGION 19..34
FT /note="Essential for its translational repressor activity"
FT /evidence="ECO:0000250"
FT MOTIF 151..178
FT /note="C2HC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT MOTIF 186..202
FT /note="C2HC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
SQ SEQUENCE 228 AA; 24861 MW; 52353442B33480D0 CRC64;
MDFLNHNYLS ARASYDYTFN FWNDYLGLST LVTKNSKHSV PQNPNSITES LKATLGLDDS
PPCPCVMGEG DSGGHLDSCC CPPPASISIL DLKERFSILS PFQNQNQGSL LSSSQEREIG
IGGGFAGFDL FGVERKMRKP AARNKQEPKI CVFCRNNGAP EEVYGSHVLK TPDGRVVCPI
LRAYTCPLCS ANGDNAHTIK YCPLSKDQPA QRVLKGGRAV GGKRVKIF
