ID NONO_RAT Reviewed; 476 AA. AC Q5FVM4; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 3. DT 02-SEP-2026, entry version 148. DE RecName: Full=Non-POU domain-containing octamer-binding protein; DE Short=NonO protein; GN Name=Nono; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Spleen; 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 [2] RP FUNCTION IN CIRCADIAN RHYTHMS, AND INTERACTION WITH PER1. RX PubMed=15860628; DOI=10.1126/science.1107373; RA Brown S.A., Ripperger J., Kadener S., Fleury-Olela F., Vilbois F., RA Rosbash M., Schibler U.; RT "PERIOD1-associated proteins modulate the negative limb of the mammalian RT circadian oscillator."; RL Science 308:693-696(2005). CC -!- FUNCTION: DNA- and RNA binding protein, involved in several nuclear CC processes (By similarity). Binds the conventional octamer sequence in CC double-stranded DNA (By similarity). Also binds single-stranded DNA and CC RNA at a site independent of the duplex site (By similarity). Involved CC in pre-mRNA splicing, probably as a heterodimer with SFPQ (By CC similarity). Interacts with U5 snRNA, probably by binding to a purine- CC rich sequence located on the 3' side of U5 snRNA stem 1b (By CC similarity). Together with PSPC1, required for the formation of nuclear CC paraspeckles (By similarity). The SFPQ-NONO heteromer associated with CC MATR3 may play a role in nuclear retention of defective RNAs (By CC similarity). The SFPQ-NONO heteromer may be involved in DNA unwinding CC by modulating the function of topoisomerase I/TOP1 (By similarity). The CC SFPQ-NONO heteromer may be involved in DNA non-homologous end joining CC (NHEJ) required for double-strand break repair and V(D)J recombination CC and may stabilize paired DNA ends (By similarity). In vitro, the CC complex strongly stimulates DNA end joining, binds directly to the DNA CC substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to CC establish a functional preligation complex (By similarity). NONO is CC involved in transcriptional regulation (By similarity). The SFPQ-NONO- CC NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP- CC dependent transcriptional activity (By similarity). NONO binds to an CC enhancer element in long terminal repeats of endogenous intracisternal CC A particles (IAPs) and activates transcription (By similarity). CC Regulates the circadian clock by repressing the transcriptional CC activator activity of the CLOCK-BMAL1 heterodimer (PubMed:15860628). CC Important for the functional organization of GABAergic synapses (By CC similarity). Plays a specific and important role in the regulation of CC synaptic RNAs and GPHN/gephyrin scaffold structure, through the CC regulation of GABRA2 transcript (By similarity). Plays a key role CC during neuronal differentiation by recruiting TET1 to genomic loci and CC thereby regulating 5-hydroxymethylcytosine levels (By similarity). CC Plays a role in the regulation of DNA virus-mediated innate immune CC response by assembling into the HDP-RNP complex, a complex that serves CC as a platform for IRF3 phosphorylation and subsequent innate immune CC response activation through the cGAS-STING pathway (By similarity). CC {ECO:0000250|UniProtKB:Q15233, ECO:0000250|UniProtKB:Q99K48, CC ECO:0000269|PubMed:15860628}. CC -!- SUBUNIT: Monomer and component of the SFPQ-NONO complex, which is CC probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) CC subunits. NONO is a component of spliceosome and U5.4/6 snRNP complexes CC (By similarity). Interacts with CPNE4 (via VWFA domain) (By CC similarity). Forms heterodimers with PSPC1; this involves formation of CC a coiled coil domain by helices from both proteins. Part of complex CC consisting of SFPQ, NONO and MATR3. Part of a complex consisting of CC SFPQ, NONO and NR5A1. Part of a complex consisting of SFPQ, NONO and CC TOP1. Interacts with SPI1 and SPIB. Interacts with RNF43 (By CC similarity). Interacts with PER1 and PER2 (PubMed:15860628). Part of CC the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, CC paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 CC RNA. Interacts (via second RRM domain) with WASL; the interaction is CC direct. Component of a multiprotein complex with WASL and SFPQ (By CC similarity). Interacts with ERCC6 (By similarity). Interacts (via DNA- CC binding domain) with TET1 (By similarity). CC {ECO:0000250|UniProtKB:Q15233, ECO:0000250|UniProtKB:Q99K48, CC ECO:0000269|PubMed:15860628}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15233}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:Q15233}. Nucleus speckle CC {ECO:0000250|UniProtKB:Q15233}. Chromosome CC {ECO:0000250|UniProtKB:Q99K48}. Note=Detected in punctate subnuclear CC structures often located adjacent to splicing speckles, called CC paraspeckles. {ECO:0000250|UniProtKB:Q15233}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC089880; AAH89880.1; -; mRNA. DR RefSeq; NP_001012356.1; NM_001012356.1. DR AlphaFoldDB; Q5FVM4; -. DR BMRB; Q5FVM4; -. DR SMR; Q5FVM4; -. DR BioGRID; 261496; 3. DR CORUM; Q5FVM4; -. DR FunCoup; Q5FVM4; 3648. DR IntAct; Q5FVM4; 3. DR MINT; Q5FVM4; -. DR STRING; 10116.ENSRNOP00000004911; -. DR GlyGen; Q5FVM4; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q5FVM4; -. DR PhosphoSitePlus; Q5FVM4; -. DR SwissPalm; Q5FVM4; -. DR jPOST; Q5FVM4; -. DR PaxDb; 10116-ENSRNOP00000004911; -. DR Ensembl; ENSRNOT00000004911.7; ENSRNOP00000004911.4; ENSRNOG00000003689.8. DR Ensembl; ENSRNOT00055051206; ENSRNOP00055042181; ENSRNOG00055029571. DR Ensembl; ENSRNOT00060046815; ENSRNOP00060038934; ENSRNOG00060027002. DR Ensembl; ENSRNOT00065029057; ENSRNOP00065023020; ENSRNOG00065017402. DR GeneID; 317259; -. DR KEGG; rno:317259; -. DR UCSC; RGD:1549738; rat. DR AGR; RGD:1549738; -. DR CTD; 4841; -. DR RGD; 1549738; Nono. DR eggNOG; KOG0115; Eukaryota. DR GeneTree; ENSGT00940000154442; -. DR HOGENOM; CLU_027185_2_0_1; -. DR InParanoid; Q5FVM4; -. DR OMA; HGMAMNR; -. DR OrthoDB; 10067824at2759; -. DR PhylomeDB; Q5FVM4; -. DR PRO; PR:Q5FVM4; -. DR Proteomes; UP000002494; Chromosome X. DR Bgee; ENSRNOG00000003689; Expressed in thymus and 20 other cell types or tissues. DR ExpressionAtlas; Q5FVM4; baseline and differential. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0001650; C:fibrillar center; ISO:RGD. DR GO; GO:0016363; C:nuclear matrix; ISO:RGD. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISO:RGD. DR GO; GO:0005654; C:nucleoplasm; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0042382; C:paraspeckles; ISO:RGD. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD. DR GO; GO:0003682; F:chromatin binding; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0106222; F:lncRNA binding; IDA:RGD. DR GO; GO:0002218; P:activation of innate immune response; ISO:RGD. DR GO; GO:1904385; P:cellular response to angiotensin; IMP:RGD. DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD. DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:RGD. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd12946; NOPS_p54nrb_PSF_PSPC1; 1. DR CDD; cd12588; RRM1_p54nrb; 1. DR FunFam; 3.30.70.330:FF:000226; Non-POU domain-containing octamer-binding protein; 1. DR FunFam; 3.30.70.330:FF:000043; paraspeckle component 1 isoform X1; 1. DR Gene3D; 3.30.70.330; -; 2. DR Gene3D; 6.10.250.1170; -; 1. DR InterPro; IPR012975; NOPS. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR034552; p54nrb_RRM1. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR23189; RNA RECOGNITION MOTIF-CONTAINING; 1. DR Pfam; PF08075; NOPS; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 2. PE 1: Evidence at protein level; KW Acetylation; Activator; Biological rhythms; Chromosome; Coiled coil; KW DNA damage; DNA recombination; DNA repair; DNA-binding; Immunity; KW Innate immunity; Isopeptide bond; Methylation; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; RNA-binding; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..476 FT /note="Non-POU domain-containing octamer-binding protein" FT /id="PRO_0000081686" FT DOMAIN 80..147 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 154..235 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 1..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 60..379 FT /note="DBHS" FT /evidence="ECO:0000250" FT REGION 448..476 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 274..378 FT /evidence="ECO:0000255" FT COMPBIAS 1..10 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 14..27 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 28..40 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q99K48" FT MOD_RES 5 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 6 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 11 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 203 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 267 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 300 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K48" FT MOD_RES 376 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K48" FT MOD_RES 433 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 445 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 455 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 461 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 5 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 65 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 101 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 104 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 131 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 195 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 203 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 248 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 254 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 376 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 472 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" SQ SEQUENCE 476 AA; 54925 MW; 47521721B46E5597 CRC64; MQSNKTFNLE KQNHTPRKHH QHHHQQHHQQ QQQQQQQQQQ QPPPPIPANG QQASSQNEGL TIDLKNFRKP GEKTFTQRSR LFVGNLPPDI TEEEMRKLFE KYGKAGEVFI HKDKGFGFIR LETRTLAEIA KVELDNMPLR GKQLRVRFAC HSASLTVRNL PQYVSNELLE EAFSVFGQVE RAVVIVDDRG RPSGKGIVEF SGKPAARKAL DRCSEGSFLL TTFPRPVTVE PMDQLDDEEG LPEKLVIKNQ QFHKEREQPP RFAQPGSFEY EYAMRWKALI EMEKQQQDQV DRNIKEAREK LEMEMEAARH EHQVMLMRQD LMRRQEELRR MEELHNQEVQ KRKQLELRQE EERRRREEEM RRQQEEMMRR QQEGFKGTFP DAREQEIRMG QMAMGGAMGI NNRGAMPPAP VPPGTPAPPG PAAMMPDGTL GLTPPTTERF GQAATMEGIG AIGGTPPAFN RPAPGAEFAP NKRRRY //