NANO3_HUMAN
ID NANO3_HUMAN Reviewed; 173 AA.
AC P60323; Q495E5;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Nanos homolog 3;
DE Short=NOS-3;
GN Name=NANOS3; Synonyms=NOS3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-173 (ISOFORMS 1/2).
RX PubMed=8889548; DOI=10.1101/gr.6.9.791;
RA Bonaldo M.F., Lennon G., Soares M.B.;
RT "Normalization and subtraction: two approaches to facilitate gene
RT discovery.";
RL Genome Res. 6:791-806(1996).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=21421998; DOI=10.1093/hmg/ddr114;
RA Julaton V.T., Reijo Pera R.A.;
RT "NANOS3 function in human germ cell development.";
RL Hum. Mol. Genet. 20:2238-2250(2011).
CC -!- FUNCTION: Plays a role in the maintenance of the undifferentiated state
CC of germ cells regulating the spermatogonia cell cycle and inducing a
CC prolonged transit in G1 phase. Affects cell proliferation probably by
CC repressing translation of specific mRNAs. Maintains the germ cell
CC lineage by suppressing both Bax-dependent and -independent apoptotic
CC pathways. Essential in the early stage embryo to protect the migrating
CC primordial germ cells (PGCs) from apoptosis.
CC {ECO:0000269|PubMed:21421998}.
CC -!- SUBUNIT: Binds mRNA from germ cells. Interacts with PUM2 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P60323-2; Q96Q77: CIB3; NbExp=3; IntAct=EBI-18012223, EBI-10292696;
CC P60323-2; Q9NV31: IMP3; NbExp=3; IntAct=EBI-18012223, EBI-747481;
CC P60323-2; P40692: MLH1; NbExp=3; IntAct=EBI-18012223, EBI-744248;
CC P60323-2; P20618: PSMB1; NbExp=3; IntAct=EBI-18012223, EBI-372273;
CC P60323-2; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-18012223, EBI-750487;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21421998}. Cytoplasm
CC {ECO:0000269|PubMed:21421998}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:P60324}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:P60324}. Note=Co-localizes with PUM2, EIF2S1 and
CC TIAL1 in the stress granules. Co-localizes with DCP1A in the P-body.
CC {ECO:0000250|UniProtKB:P60324}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60323-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60323-2; Sequence=VSP_038695;
CC -!- TISSUE SPECIFICITY: Ovary, testis and brain (at protein level). In the
CC ovaries, expressed during multiple stages of oogenesis, including
CC primordial, primary, secondary and antral follicles with the highest
CC expression in the oocytes. In the testis, expressed in germ cells, type
CC A spermatogonia (SA), primary spermatocytes (S1), round spermatids (S3)
CC and elongated spermatids. {ECO:0000269|PubMed:21421998}.
CC -!- DEVELOPMENTAL STAGE: Fetal ovary and fetal testis (at protein level).
CC {ECO:0000269|PubMed:21421998}.
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; AC020916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101209; AAI01210.1; -; mRNA.
DR EMBL; BC101210; AAI01211.1; -; mRNA.
DR EMBL; BM702754; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS42511.1; -. [P60323-2]
DR RefSeq; NP_001092092.1; NM_001098622.2. [P60323-2]
DR AlphaFoldDB; P60323; -.
DR SMR; P60323; -.
DR BioGRID; 131219; 16.
DR ELM; P60323; -.
DR IntAct; P60323; 5.
DR iPTMnet; P60323; -.
DR PhosphoSitePlus; P60323; -.
DR SwissPalm; P60323; -.
DR BioMuta; NANOS3; -.
DR MassIVE; P60323; -.
DR PeptideAtlas; P60323; -.
DR PRIDE; P60323; -.
DR ProteomicsDB; 57192; -. [P60323-1]
DR ProteomicsDB; 57193; -. [P60323-2]
DR Antibodypedia; 26509; 131 antibodies from 28 providers.
DR DNASU; 342977; -.
DR Ensembl; ENST00000339133.6; ENSP00000341992.4; ENSG00000187556.8. [P60323-2]
DR Ensembl; ENST00000397555.3; ENSP00000380687.2; ENSG00000187556.8. [P60323-1]
DR Ensembl; ENST00000672749.1; ENSP00000500080.1; ENSG00000288505.1. [P60323-1]
DR Ensembl; ENST00000673200.1; ENSP00000500242.1; ENSG00000288505.1. [P60323-2]
DR GeneID; 342977; -.
DR KEGG; hsa:342977; -.
DR MANE-Select; ENST00000339133.6; ENSP00000341992.4; NM_001098622.3; NP_001092092.1. [P60323-2]
DR UCSC; uc002mxj.5; human. [P60323-1]
DR CTD; 342977; -.
DR DisGeNET; 342977; -.
DR GeneCards; NANOS3; -.
DR HGNC; HGNC:22048; NANOS3.
DR HPA; ENSG00000187556; Group enriched (brain, testis).
DR MIM; 608229; gene.
DR neXtProt; NX_P60323; -.
DR OpenTargets; ENSG00000187556; -.
DR PharmGKB; PA134867615; -.
DR VEuPathDB; HostDB:ENSG00000187556; -.
DR eggNOG; KOG4602; Eukaryota.
DR GeneTree; ENSGT00950000183135; -.
DR HOGENOM; CLU_094055_1_0_1; -.
DR InParanoid; P60323; -.
DR OMA; GYMSVYS; -.
DR OrthoDB; 1198436at2759; -.
DR PhylomeDB; P60323; -.
DR TreeFam; TF326882; -.
DR PathwayCommons; P60323; -.
DR SignaLink; P60323; -.
DR SIGNOR; P60323; -.
DR BioGRID-ORCS; 342977; 17 hits in 1062 CRISPR screens.
DR GenomeRNAi; 342977; -.
DR Pharos; P60323; Tbio.
DR PRO; PR:P60323; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P60323; protein.
DR Bgee; ENSG00000187556; Expressed in prefrontal cortex and 95 other tissues.
DR Genevisible; P60323; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS: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:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IDA:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; 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 Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Metal-binding; Nucleus; Oogenesis; Reference proteome; RNA-binding;
KW Spermatogenesis; Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..173
FT /note="Nanos homolog 3"
FT /id="PRO_0000207689"
FT ZN_FING 57..111
FT /note="Nanos-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT REGION 23..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..85
FT /note="C2HC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT MOTIF 93..109
FT /note="C2HC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT COMPBIAS 129..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT VAR_SEQ 42
FT /note="P -> PVSALEPMPAPESVPVPGPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038695"
SQ SEQUENCE 173 AA; 18844 MW; 14C18866070795D9 CRC64;
MGTFDLWTDY LGLAHLVRAL SGKEGPETRL SPQPEPEPML EPDQKRSLES SPAPERLCSF
CKHNGESRAI YQSHVLKDEA GRVLCPILRD YVCPQCGATR ERAHTRRFCP LTGQGYTSVY
SHTTRNSAGK KLVRPDKAKT QDTGHRRGGG GGAGFRGAGK SEPSPSCSPS MST
