NANOS_DROME
ID NANOS_DROME Reviewed; 401 AA.
AC P25724; Q9VDZ6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein nanos;
GN Name=nos; ORFNames=CG5637;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1908748; DOI=10.1016/0092-8674(91)90110-k;
RA Wang C.I., Lehmann R.;
RT "Nanos is the localized posterior determinant in Drosophila.";
RL Cell 66:637-647(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP MUTAGENESIS OF CYS-319; HIS-335; SER-336; VAL-337; ARG-338; PRO-347;
RP LEU-349; ARG-350; VAL-353; CYS-357; GLY-361; ALA-364; HIS-365; THR-377 AND
RP MET-378.
RX PubMed=10581288; DOI=10.1093/genetics/153.4.1825;
RA Arrizabalaga G., Lehmann R.;
RT "A selective screen reveals discrete functional domains in Drosophila
RT Nanos.";
RL Genetics 153:1825-1838(1999).
RN [5]
RP INTERACTION WITH PUM.
RX PubMed=10541556; DOI=10.1101/gad.13.20.2704;
RA Sonoda J., Wharton R.P.;
RT "Recruitment of Nanos to hunchback mRNA by Pumilio.";
RL Genes Dev. 13:2704-2712(1999).
RN [6]
RP INTERACTION WITH CUP.
RX PubMed=11060247; DOI=10.1242/dev.127.23.5225;
RA Verrotti A.C., Wharton R.P.;
RT "Nanos interacts with cup in the female germline of Drosophila.";
RL Development 127:5225-5232(2000).
RN [7]
RP INTERACTION WITH BRAT AND PUM.
RX PubMed=11274060; DOI=10.1101/gad.870801;
RA Sonoda J., Wharton R.P.;
RT "Drosophila Brain tumor is a translational repressor.";
RL Genes Dev. 15:762-773(2001).
RN [8]
RP REVIEW.
RX PubMed=11700288; DOI=10.1146/annurev.genet.35.102401.090756;
RA Johnstone O., Lasko P.;
RT "Translational regulation and RNA localization in Drosophila oocytes and
RT embryos.";
RL Annu. Rev. Genet. 35:365-406(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17178403; DOI=10.1016/j.neuron.2006.10.028;
RA Barbee S.A., Estes P.S., Cziko A.M., Hillebrand J., Luedeman R.A.,
RA Coller J.M., Johnson N., Howlett I.C., Geng C., Ueda R., Brand A.H.,
RA Newbury S.F., Wilhelm J.E., Levine R.B., Nakamura A., Parker R.,
RA Ramaswami M.;
RT "Staufen- and FMRP-containing neuronal RNPs are structurally and
RT functionally related to somatic P bodies.";
RL Neuron 52:997-1009(2006).
RN [10]
RP STRUCTURE BY NMR OF THE NANOS-ZINC-FINGER, AND MUTAGENESIS OF CYS-319 AND
RP CYS-354.
RX PubMed=9049312; DOI=10.1093/emboj/16.4.834;
RA Curtis D., Treiber D.K., Tao F., Zamore P.D., Williamson J.R., Lehmann R.;
RT "A CCHC metal-binding domain in Nanos is essential for translational
RT regulation.";
RL EMBO J. 16:834-843(1997).
CC -!- FUNCTION: Maternal RNA-binding protein that is required for germ cells
CC proliferation and self-renewal. Acts by forming a complex with pum and
CC brat that regulates translation and mRNA stability. The complex binds
CC to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA
CC 3'-UTR and prevents its translation. Controls posterior development.
CC Rescuing factor for the abdominal defect of posterior group mutants.
CC The other posterior group genes are not required for nanos function but
CC rather play a role in localization or distribution of nanos protein.
CC -!- SUBUNIT: Interacts with pum and brat. Acts via the formation of a
CC quaternary complex composed of pum, nos, brat and the 3'-UTR mRNA of
CC hb. Interacts with cup. Binds RNA with no specificity.
CC {ECO:0000269|PubMed:10541556, ECO:0000269|PubMed:11060247,
CC ECO:0000269|PubMed:11274060}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC {ECO:0000269|PubMed:17178403}.
CC -!- TISSUE SPECIFICITY: Posterior part of the embryo. While the transcript
CC is present throughout the embryo, nos translation is controlled by smg,
CC and the protein is found in pole plasm and pole cells.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Present during oogenesis and
CC early stages of embryogenesis.
CC -!- DOMAIN: The Nanos-type zinc finger is composed of two C2HC motifs, each
CC motif binding one molecule of zinc. The presence of the zinc molecules
CC is essential for the translation repression activity of the protein.
CC -!- SIMILARITY: Belongs to the nanos family. {ECO:0000255|PROSITE-
CC ProRule:PRU00855}.
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DR EMBL; M72421; AAA28715.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55641.1; -; Genomic_DNA.
DR PIR; A40042; A40042.
DR RefSeq; NP_476658.1; NM_057310.4.
DR PDB; 5KL1; X-ray; 3.70 A; B=289-401.
DR PDB; 5KL8; X-ray; 4.00 A; B=289-401.
DR PDBsum; 5KL1; -.
DR PDBsum; 5KL8; -.
DR AlphaFoldDB; P25724; -.
DR SASBDB; P25724; -.
DR SMR; P25724; -.
DR BioGRID; 67295; 67.
DR DIP; DIP-23696N; -.
DR IntAct; P25724; 2.
DR STRING; 7227.FBpp0083146; -.
DR PaxDb; P25724; -.
DR ABCD; P25724; 4 sequenced antibodies.
DR DNASU; 42297; -.
DR EnsemblMetazoa; FBtr0083732; FBpp0083146; FBgn0002962.
DR GeneID; 42297; -.
DR KEGG; dme:Dmel_CG5637; -.
DR UCSC; CG5637-RA; d. melanogaster.
DR FlyBase; FBgn0002962; nos.
DR VEuPathDB; VectorBase:FBgn0002962; -.
DR eggNOG; KOG4602; Eukaryota.
DR InParanoid; P25724; -.
DR OrthoDB; 1125594at2759; -.
DR PhylomeDB; P25724; -.
DR SignaLink; P25724; -.
DR BioGRID-ORCS; 42297; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42297; -.
DR PRO; PR:P25724; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002962; Expressed in cleaving embryo and 17 other tissues.
DR ExpressionAtlas; P25724; baseline and differential.
DR Genevisible; P25724; DM.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0045495; C:pole plasm; TAS:FlyBase.
DR GO; GO:0098975; C:postsynapse of neuromuscular junction; IMP:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; TAS:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0008354; P:germ cell migration; TAS:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IDA:FlyBase.
DR GO; GO:0006378; P:mRNA polyadenylation; TAS:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:FlyBase.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; NAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007280; P:pole cell migration; TAS:FlyBase.
DR GO; GO:0035282; P:segmentation; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
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 3D-structure; Cytoplasm; Developmental protein; Differentiation;
KW Metal-binding; Oogenesis; Reference proteome; RNA-binding; Spermatogenesis;
KW Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..401
FT /note="Protein nanos"
FT /id="PRO_0000207684"
FT ZN_FING 318..372
FT /note="Nanos-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT REGION 181..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 319..346
FT /note="C2HC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT MOTIF 354..370
FT /note="C2HC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT COMPBIAS 191..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT MUTAGEN 319
FT /note="C->Y: Strong defects in abdomen and oogenesis.
FT Reduces binding of zinc. Complete loss of zinc-binding and
FT loss of function; when associated with Y-354."
FT /evidence="ECO:0000269|PubMed:10581288,
FT ECO:0000269|PubMed:9049312"
FT MUTAGEN 322
FT /note="C->S: Strong defects in abdomen and oogenesis."
FT MUTAGEN 335
FT /note="H->Y: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 336
FT /note="S->L: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 337
FT /note="V->E: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 338
FT /note="R->Q: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 347
FT /note="P->S: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 349
FT /note="L->R: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 350
FT /note="R->G: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 353
FT /note="V->M: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 354
FT /note="C->Y: Strong defects in abdomen and oogenesis.
FT Reduces binding of zinc. Complete loss of zinc-binding and
FT loss of function; when associated with Y-319."
FT /evidence="ECO:0000269|PubMed:9049312"
FT MUTAGEN 357
FT /note="C->Y: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 361
FT /note="G->E: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 364
FT /note="A->T: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 365
FT /note="H->Y: Strong defects in abdomen and oogenesis."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 377
FT /note="T->I: Strong defects in oogenesis. Weak defects in
FT abdomen."
FT /evidence="ECO:0000269|PubMed:10581288"
FT MUTAGEN 378
FT /note="M->K: Strong defects in abdomen."
FT /evidence="ECO:0000269|PubMed:10581288"
SQ SEQUENCE 401 AA; 43428 MW; FA4ACFC2FFC01A75 CRC64;
MFRSNLEGSG AAAVGVANPP SLAQSGKIFQ LQDNFSAFHA RGGLNILGLQ DMYLDTSGAN
SSATLSPPIT PVTPDPSTSA QSTHFPFLAD SAATANSLLM QRQYHYHLLL QQQQQLAMAQ
HQLALAASAA AASASHQQTD EIARSLKIFA QVTTGAAENA AGSMQDVMQE FATNGYASDD
LGRMSYGSAP PQVQMPPQQQ HQQQQGLHLP LGRNPAQLQT NGGNLMPIPL ATHWLNNYRE
HLNNVWRNMS YIPAAPNTMG LQAQTAATVS TNLGVGMGLG LPVQGEQLRG ASNSSNNNNN
NNKVYKRYNS KAKEISRHCV FCENNNEPEA VINSHSVRDN FNRVLCPKLR TYVCPICGAS
GDSAHTIKYC PKKPIITMED AIKAESFRLA KSSYYKQQMK V
