ID   NANO1_XENBO             Reviewed;         128 AA.
AC   Q90ZZ5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Nanos homolog 1;
DE   AltName: Full=Xcat-2 protein;
GN   Name=nanos1; Synonyms=xcat-2;
OS   Xenopus borealis (Kenyan clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8354;
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).
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; AF256087; AAK49296.1; -; mRNA.
DR   AlphaFoldDB; Q90ZZ5; -.
DR   SMR; Q90ZZ5; -.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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   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; Repressor; RNA-binding; Translation regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..128
FT                   /note="Nanos homolog 1"
FT                   /id="PRO_0000410977"
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..56
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"
SQ   SEQUENCE   128 AA;  14145 MW;  AE1CBD3432CD990D CRC64;
     MDGGLCFDSW SDYLGLSSLI SRGLQPRGEG ENPSPRWNVS CPAPAEPLPS KEPEGRGYKG
     CGFCRSNKEA MSLYSSHRLR SLDGRVLCPV LRGYTCPLCG ANGDWAHTMR YCPLRQLLRN
     PQSPRNGQ