NANO1_MOUSE
ID NANO1_MOUSE Reviewed; 267 AA.
AC Q80WY3; Q3UTS9; Q8BIJ9;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Nanos homolog 1;
DE Short=NOS-1;
GN Name=Nanos1; Synonyms=Nos;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [MRNA] OF 49-267, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=12834871; DOI=10.1016/s0925-4773(03)00043-1;
RA Haraguchi S., Tsuda M., Kitajima S., Sasaoka Y., Nomura-Kitabayashid A.,
RA Kurokawa K., Saga Y.;
RT "nanos1: a mouse nanos gene expressed in the central nervous system is
RT dispensable for normal development.";
RL Mech. Dev. 120:721-731(2003).
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 (By similarity).
CC Not essential for normal development. {ECO:0000250,
CC ECO:0000269|PubMed:12834871}.
CC -!- SUBUNIT: Interacts with PUM2, SNAPIN and CTNNB1. Interacts (via N-
CC terminal region) with CTNND1. Interacts with DDX20 (via N-terminal
CC region) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8WY41}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8WY41}. Note=Colocalizes with SNAPIN and PUM2
CC in the perinuclear region of germ cells.
CC {ECO:0000250|UniProtKB:Q8WY41}.
CC -!- TISSUE SPECIFICITY: Expressed in the oocyte. Transiently expressed in
CC eight-cell embryos. At 12.5 dpc, it is re-expressed in the central
CC nervous system and the expression continues in the adult brain, in
CC which the hippocampal formation is the predominant region. Expressed in
CC the seminiferous tubules of mature testis, but not in the primordial
CC germ cells. {ECO:0000269|PubMed:12834871}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:12834871}.
CC -!- DOMAIN: The N-terminal region and C-terminal zinc-finger RNA-binding
CC domain are both necessary for interaction with SNAPIN. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC76003.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK139148; BAE23901.1; -; mRNA.
DR EMBL; BC056473; AAH56473.2; -; mRNA.
DR EMBL; BC085512; AAH85512.1; -; mRNA.
DR EMBL; CD350545; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB095029; BAC76003.1; ALT_INIT; mRNA.
DR CCDS; CCDS29941.1; -.
DR RefSeq; NP_848508.2; NM_178421.3.
DR AlphaFoldDB; Q80WY3; -.
DR SMR; Q80WY3; -.
DR STRING; 10090.ENSMUSP00000096874; -.
DR iPTMnet; Q80WY3; -.
DR PhosphoSitePlus; Q80WY3; -.
DR MaxQB; Q80WY3; -.
DR PaxDb; Q80WY3; -.
DR PRIDE; Q80WY3; -.
DR ProteomicsDB; 287435; -.
DR Antibodypedia; 32079; 309 antibodies from 33 providers.
DR DNASU; 332397; -.
DR Ensembl; ENSMUST00000088237; ENSMUSP00000096874; ENSMUSG00000072437.
DR GeneID; 332397; -.
DR KEGG; mmu:332397; -.
DR UCSC; uc008ibw.1; mouse.
DR CTD; 340719; -.
DR MGI; MGI:2669254; Nanos1.
DR VEuPathDB; HostDB:ENSMUSG00000072437; -.
DR eggNOG; KOG4602; Eukaryota.
DR GeneTree; ENSGT00950000183135; -.
DR HOGENOM; CLU_094055_0_0_1; -.
DR InParanoid; Q80WY3; -.
DR OMA; ALGPPDY; -.
DR OrthoDB; 1633105at2759; -.
DR PhylomeDB; Q80WY3; -.
DR TreeFam; TF326882; -.
DR BioGRID-ORCS; 332397; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Nanos1; mouse.
DR PRO; PR:Q80WY3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q80WY3; protein.
DR Bgee; ENSMUSG00000072437; Expressed in rostral migratory stream and 148 other tissues.
DR Genevisible; Q80WY3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS: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; ISS:UniProtKB.
DR GO; GO:0098749; P:cerebellar neuron development; IMP:MGI.
DR GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IGI:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IGI:MGI.
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; Reference proteome; Repressor; RNA-binding;
KW Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..267
FT /note="Nanos homolog 1"
FT /id="PRO_0000207686"
FT ZN_FING 188..242
FT /note="Nanos-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT REGION 40..56
FT /note="Essential for its translational repressor activity"
FT /evidence="ECO:0000250"
FT REGION 57..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 189..216
FT /note="C2HC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT MOTIF 224..240
FT /note="C2HC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT CONFLICT 111
FT /note="P -> T (in Ref. 3; BAC76003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 28151 MW; 76D1E41CACBF76E8 CRC64;
MEAFPWAPRS PRRARAPAPM ALVPSARYVS ASGPVHPQPF SSWNDYLGLA TLITRASDRG
SPHEGPGPTA AGPTMGPPED DEDDDGEEPE AGGRYLGGAL ELRALELCAG PAEPGLLEER
FAELNPFAGR AAAVLLGCAP TASTTAAAAS TAEVTPREEP SPAWAAEPRL HAASGATAAR
LLKPELQVCV FCRNNKEAVA LYTTHILKGP DGRVLCPVLR RYTCPLCGAS GDNAHTIKYC
PLSKVPPPTV RPPPRSNRDS LPSKKLR
