NANO1_XENLA
ID NANO1_XENLA Reviewed; 128 AA.
AC Q07937;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Nanos homolog 1;
DE AltName: Full=Xcat-2 protein;
GN Name=nanos1; Synonyms=xcat-2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8223259; DOI=10.1242/dev.117.1.377;
RA Mosquera L., Forristall C., Zhou Y., King M.L.;
RT "A mRNA localized to the vegetal cortex of Xenopus oocytes encodes a
RT protein with a nanos-like zinc finger domain.";
RL Development 117:377-386(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH CCNB1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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. {ECO:0000269|PubMed:21195170}.
CC -!- SUBUNIT: Interacts with ccnb1. {ECO:0000269|PubMed:21195170}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000269|PubMed:21195170}. Note=During early cleavage and
CC blastula stages found close to the cell periphery in a germ plasm-like
CC pattern. From gastrula stage on, detected predominantly in a
CC perinuclear region.
CC -!- TISSUE SPECIFICITY: Ovary and testis. {ECO:0000269|PubMed:21195170,
CC ECO:0000269|PubMed:8223259}.
CC -!- DEVELOPMENTAL STAGE: Very abundant in the oocyte and early embryo and
CC reduced to very low levels by gastrulation.
CC {ECO:0000269|PubMed:21195170, ECO:0000269|PubMed:8223259}.
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; X72340; CAA51067.1; -; mRNA.
DR PIR; I51603; I51603.
DR RefSeq; NP_001081503.1; NM_001088034.1.
DR AlphaFoldDB; Q07937; -.
DR SMR; Q07937; -.
DR MINT; Q07937; -.
DR GeneID; 397875; -.
DR KEGG; xla:397875; -.
DR CTD; 397875; -.
DR Xenbase; XB-GENE-6252322; nanos1.L.
DR OMA; GYMSVYS; -.
DR OrthoDB; 1633105at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 397875; Expressed in oocyte and 7 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0060293; C:germ plasm; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030371; F:translation repressor activity; IDA: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 1: Evidence at protein 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_0000410978"
FT ZN_FING 56..110
FT /note="Nanos-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT REGION 7..23
FT /note="Essential for its translational repressor activity"
FT REGION 25..52
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 128 AA; 14327 MW; D842849EA021CDFD CRC64;
MDGGLCFDSW SDYLGLSSLI SRGLQPQREG ERPRWDVLSP ASAEPLPSNE SVGHKGCGFC
RSNREALSLY TSHRLRALDG RVLCPVLRGY TCPLCGANGD WAHTMRYCPL RRLLRDPQSN
SNNPKLRH
