NANO1_HUMAN
ID NANO1_HUMAN Reviewed; 292 AA.
AC Q8WY41;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Nanos homolog 1;
DE Short=NOS-1;
DE AltName: Full=EC_Rep1a;
GN Name=NANOS1; Synonyms=NOS1;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH PUM2.
RC TISSUE=Testis;
RX PubMed=12690449; DOI=10.1007/s00427-003-0303-2;
RA Jaruzelska J., Kotecki M., Kusz K., Spik A., Firpo M., Reijo Pera R.A.;
RT "Conservation of a Pumilio-Nanos complex from Drosophila germ plasm to
RT human germ cells.";
RL Dev. Genes Evol. 213:120-126(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
RP INTERACTION WITH CTNND1 AND CTNNB1, AND TISSUE SPECIFICITY.
RX PubMed=17047063; DOI=10.1158/0008-5472.can-05-3096;
RA Strumane K., Bonnomet A., Stove C., Vandenbroucke R., Nawrocki-Raby B.,
RA Bruyneel E., Mareel M., Birembaut P., Berx G., van Roy F.;
RT "E-cadherin regulates human Nanos1, which interacts with p120ctn and
RT induces tumor cell migration and invasion.";
RL Cancer Res. 66:10007-10015(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18223680; DOI=10.1038/sj.onc.1211035;
RA Bonnomet A., Polette M., Strumane K., Gilles C., Dalstein V., Kileztky C.,
RA Berx G., van Roy F., Birembaut P., Nawrocki-Raby B.;
RT "The E-cadherin-repressed hNanos1 gene induces tumor cell invasion by
RT upregulating MT1-MMP expression.";
RL Oncogene 27:3692-3699(2008).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH PUM2 AND
RP SNAPIN.
RX PubMed=19168546; DOI=10.1093/molehr/gap004;
RA Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C.,
RA Kupryjanczyk J., Jaruzelska J.;
RT "The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins
RT in human male germ cells.";
RL Mol. Hum. Reprod. 15:173-179(2009).
RN [6]
RP INTERACTION WITH DDX20.
RX PubMed=21800163; DOI=10.1007/s00418-011-0842-y;
RA Ginter-Matuszewska B., Kusz K., Spik A., Grzeszkowiak D., Rembiszewska A.,
RA Kupryjanczyk J., Jaruzelska J.;
RT "NANOS1 and PUMILIO2 bind microRNA biogenesis factor GEMIN3, within
RT chromatoid body in human germ cells.";
RL Histochem. Cell Biol. 136:279-287(2011).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL 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).
RN [8]
RP VARIANTS SPGF12 SER-78 DEL AND ALA-173 DEL, AND VARIANTS THR-34; HIS-246
RP AND TYR-276.
RX PubMed=23315541; DOI=10.1136/jmedgenet-2012-101230;
RA Kusz-Zamelczyk K., Sajek M., Spik A., Glazar R., Jedrzejczak P.,
RA Latos-Bielenska A., Kotecki M., Pawelczyk L., Jaruzelska J.;
RT "Mutations of NANOS1, a human homologue of the Drosophila morphogen, are
RT associated with a lack of germ cells in testes or severe oligo-astheno-
RT teratozoospermia.";
RL J. Med. Genet. 50:187-193(2013).
CC -!- FUNCTION: May act as a translational repressor which regulates
CC translation of specific mRNAs by forming a complex with PUM2 that
CC associates with the 3'-UTR of mRNA targets. Capable of interfering with
CC the proadhesive and anti-invasive functions of E-cadherin. Up-regulates
CC the production of MMP14 to promote tumor cell invasion.
CC {ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:18223680}.
CC -!- SUBUNIT: Interacts with PUM2, SNAPIN and CTNNB1. Interacts (via N-
CC terminal region) with CTNND1. Interacts with DDX20 (via N-terminal
CC region). {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:17047063,
CC ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21800163}.
CC -!- INTERACTION:
CC Q8WY41; O60716-21: CTNND1; NbExp=2; IntAct=EBI-9630165, EBI-9634525;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:17047063,
CC ECO:0000269|PubMed:19168546}. Cytoplasm {ECO:0000269|PubMed:12690449,
CC ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:19168546}.
CC Note=Colocalizes with SNAPIN and PUM2 in the perinuclear region of germ
CC cells. {ECO:0000269|PubMed:12690449, ECO:0000269|PubMed:19168546}.
CC -!- TISSUE SPECIFICITY: Testis and ovary (at protein level). Predominantly
CC expressed in testis. Specifically expressed during germline
CC development. In adult tissues, it is mainly expressed in spermatogonia,
CC the stem cells of the germline. Also expressed during meiosis in
CC spermatocytes. Not present in late, post-meiotic stage germ cells.
CC Expressed in fetal ovaries, while it is weakly or not expressed in
CC mature postmeiotic oocytes, suggesting that it may be expressed in
CC premeiotic female germ cells. Expressed at high levels only in the E-
CC cadherin deficient cell lines. Highly expressed in lung carcinomas and
CC mostly detected in invasive tumor cells and its expression correlates
CC with tumor aggressiveness. {ECO:0000269|PubMed:12690449,
CC ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:18223680,
CC ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21421998}.
CC -!- DEVELOPMENTAL STAGE: Fetal ovary and fetal testis (at protein level).
CC {ECO:0000269|PubMed:21421998}.
CC -!- INDUCTION: Down-regulated by E-cadherin. {ECO:0000269|PubMed:17047063}.
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 -!- DOMAIN: The N-terminal region and C-terminal zinc-finger RNA-binding
CC domain are both necessary for interaction with SNAPIN.
CC -!- DISEASE: Spermatogenic failure 12 (SPGF12) [MIM:615413]: An infertility
CC disorder caused by spermatogenesis defects. It results in decreased
CC sperm motility, concentration, and multiple sperm structural defects.
CC Non-obstructive azoospermia, oligozoospermia and oligo-astheno-
CC teratozoospermia are features observed in SPGF12 patients.
CC {ECO:0000269|PubMed:23315541}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the nanos family. {ECO:0000255|PROSITE-
CC ProRule:PRU00855}.
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DR EMBL; AF275269; AAL36982.2; -; mRNA.
DR EMBL; AF458985; AAQ04765.1; -; mRNA.
DR EMBL; AL157788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS7607.1; -.
DR RefSeq; NP_955631.1; NM_199461.3.
DR PDB; 4CQO; X-ray; 2.80 A; B/D=40-56.
DR PDBsum; 4CQO; -.
DR AlphaFoldDB; Q8WY41; -.
DR SMR; Q8WY41; -.
DR BioGRID; 131092; 28.
DR ELM; Q8WY41; -.
DR IntAct; Q8WY41; 1.
DR STRING; 9606.ENSP00000393275; -.
DR iPTMnet; Q8WY41; -.
DR PhosphoSitePlus; Q8WY41; -.
DR BioMuta; NANOS1; -.
DR DMDM; 41688589; -.
DR MassIVE; Q8WY41; -.
DR PaxDb; Q8WY41; -.
DR PeptideAtlas; Q8WY41; -.
DR PRIDE; Q8WY41; -.
DR ProteomicsDB; 75126; -.
DR Antibodypedia; 32079; 309 antibodies from 33 providers.
DR DNASU; 340719; -.
DR Ensembl; ENST00000425699.3; ENSP00000393275.1; ENSG00000188613.7.
DR GeneID; 340719; -.
DR KEGG; hsa:340719; -.
DR MANE-Select; ENST00000425699.3; ENSP00000393275.1; NM_199461.4; NP_955631.1.
DR UCSC; uc009xzf.2; human.
DR CTD; 340719; -.
DR DisGeNET; 340719; -.
DR GeneCards; NANOS1; -.
DR HGNC; HGNC:23044; NANOS1.
DR HPA; ENSG00000188613; Tissue enhanced (skeletal).
DR MalaCards; NANOS1; -.
DR MIM; 608226; gene.
DR MIM; 615413; phenotype.
DR neXtProt; NX_Q8WY41; -.
DR OpenTargets; ENSG00000188613; -.
DR Orphanet; 399805; Male infertility with azoospermia or oligozoospermia due to single gene mutation.
DR Orphanet; 399808; Male infertility with teratozoospermia due to single gene mutation.
DR PharmGKB; PA134876543; -.
DR VEuPathDB; HostDB:ENSG00000188613; -.
DR eggNOG; KOG4602; Eukaryota.
DR GeneTree; ENSGT00950000183135; -.
DR HOGENOM; CLU_094055_0_0_1; -.
DR InParanoid; Q8WY41; -.
DR OMA; ALGPPDY; -.
DR OrthoDB; 1633105at2759; -.
DR PhylomeDB; Q8WY41; -.
DR TreeFam; TF326882; -.
DR PathwayCommons; Q8WY41; -.
DR SignaLink; Q8WY41; -.
DR SIGNOR; Q8WY41; -.
DR BioGRID-ORCS; 340719; 26 hits in 1061 CRISPR screens.
DR ChiTaRS; NANOS1; human.
DR GenomeRNAi; 340719; -.
DR Pharos; Q8WY41; Tbio.
DR PRO; PR:Q8WY41; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8WY41; protein.
DR Bgee; ENSG00000188613; Expressed in secondary oocyte and 135 other tissues.
DR ExpressionAtlas; Q8WY41; baseline and differential.
DR Genevisible; Q8WY41; HS.
DR GO; GO:0005737; C:cytoplasm; 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:0016477; P:cell migration; IDA:UniProtKB.
DR GO; GO:0098749; P:cerebellar neuron development; IEA:Ensembl.
DR GO; GO:0010631; P:epithelial cell migration; IDA:UniProtKB.
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:0010608; P:post-transcriptional regulation of gene expression; IDA:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR Gene3D; 4.10.60.30; -; 1.
DR IDEAL; IID00517; -.
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 3D-structure; Cytoplasm; Disease variant; Metal-binding;
KW Reference proteome; Repressor; RNA-binding; Translation regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..292
FT /note="Nanos homolog 1"
FT /id="PRO_0000207685"
FT ZN_FING 213..267
FT /note="Nanos-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..56
FT /note="Essential for its translational repressor activity"
FT /evidence="ECO:0000250"
FT REGION 68..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 214..241
FT /note="C2HC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT MOTIF 249..265
FT /note="C2HC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT COMPBIAS 73..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT VARIANT 34
FT /note="P -> T (in dbSNP:rs191267549)"
FT /evidence="ECO:0000269|PubMed:23315541"
FT /id="VAR_070569"
FT VARIANT 78
FT /note="Missing (in SPGF12)"
FT /evidence="ECO:0000269|PubMed:23315541"
FT /id="VAR_070570"
FT VARIANT 173
FT /note="Missing (in SPGF12; dbSNP:rs538539239)"
FT /evidence="ECO:0000269|PubMed:23315541"
FT /id="VAR_070571"
FT VARIANT 246
FT /note="R -> H (found in a patient affected by oligo-
FT astheno-teratozoospermia also carrying Y-276 on the same
FT allele; unknown pathological significance;
FT dbSNP:rs587777767)"
FT /evidence="ECO:0000269|PubMed:23315541"
FT /id="VAR_070572"
FT VARIANT 276
FT /note="R -> Y (found in a patient affected by oligo-
FT astheno-teratozoospermia also carrying H-246 on the same
FT allele; requires 2 nucleotide substitutions; unknown
FT pathological significance; dbSNP:rs587777768)"
FT /evidence="ECO:0000269|PubMed:23315541"
FT /id="VAR_070573"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:4CQO"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:4CQO"
SQ SEQUENCE 292 AA; 30230 MW; 1E41AAE68992CDD7 CRC64;
MEAFPWAPRS PRRGRAPPPM ALVPSARYVS APGPAHPQPF SSWNDYLGLA TLITKAVDGE
PRFGCARGGN GGGGSPPSSS SSSCCSPHTG AGPGALGPAL GPPDYDEDDD DDSDEPGSRG
RYLGSALELR ALELCAGPAE AGLLEERFAE LSPFAGRAAA VLLGCAPAAA AAATTTSEAT
PREERAPAWA AEPRLHAASG AAAARLLKPE LQVCVFCRNN KEAMALYTTH ILKGPDGRVL
CPVLRRYTCP LCGASGDNAH TIKYCPLSKV PPPPARPPPR SARDGPPGKK LR
