NANO1_XENTR
ID NANO1_XENTR Reviewed; 128 AA.
AC Q90ZZ6; B7ZTT7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Nanos homolog 1;
DE AltName: Full=Xcat-2 protein;
GN Name=nanos1; Synonyms=xcat-2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=21195170; DOI=10.1016/j.mod.2010.12.001;
RA Lai F., Zhou Y., Luo X., Fox J., King M.L.;
RT "Nanos1 functions as a translational repressor in the Xenopus germline.";
RL Mech. Dev. 128:153-163(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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. Essential for
CC the development of primordial germ cells (PGCs) by ensuring their
CC proper migration and survival (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ccnb1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Note=During early cleavage and blastula stages
CC found close to the cell periphery in a germ plasm-like pattern. From
CC gastrula stage on, detected predominantly in a perinuclear region (By
CC similarity). {ECO:0000250}.
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; AF256086; AAK49295.1; -; mRNA.
DR EMBL; BC160384; AAI60384.1; -; mRNA.
DR EMBL; BC170990; AAI70990.1; -; mRNA.
DR RefSeq; NP_988857.1; NM_203526.1.
DR AlphaFoldDB; Q90ZZ6; -.
DR SMR; Q90ZZ6; -.
DR ELM; Q90ZZ6; -.
DR STRING; 8364.ENSXETP00000052998; -.
DR PaxDb; Q90ZZ6; -.
DR GeneID; 394451; -.
DR KEGG; xtr:394451; -.
DR CTD; 340719; -.
DR Xenbase; XB-GENE-868377; nanos1.
DR eggNOG; KOG4602; Eukaryota.
DR HOGENOM; CLU_094055_1_1_1; -.
DR InParanoid; Q90ZZ6; -.
DR OrthoDB; 1633105at2759; -.
DR PhylomeDB; Q90ZZ6; -.
DR TreeFam; TF326882; -.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0060293; C:germ plasm; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS: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; ISS:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; ISS: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..128
FT /note="Nanos homolog 1"
FT /id="PRO_0000410979"
FT ZN_FING 60..114
FT /note="Nanos-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT REGION 7..23
FT /note="Essential for its translational repressor activity"
FT /evidence="ECO:0000250"
FT REGION 23..58
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 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 41
FT /note="S -> Y (in Ref. 2; AAI70990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 14140 MW; E79556DEF1C0880B CRC64;
MDGGLCFNSW SDYLGLSSLI SRGLQPREGG ESPRPRWKAS SPTPAEPLPS KAAEAHGHKG
CGFCRSNREA QSLYSSHRLR APDGRVLCPV LRGYTCPLCG ANGDWAHTMR YCPLRHFLRH
PHSPRDGQ
