NONO_RAT
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 03-AUG-2022, entry version 131.
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-ARNTL/BMAL1 heterodimer
CC (PubMed:15860628). Important for the functional organization of
CC GABAergic synapses (By similarity). Plays a specific and important role
CC in the regulation of synaptic RNAs and GPHN/gephyrin scaffold
CC structure, through the regulation of GABRA2 transcript (By similarity).
CC Plays a key role during neuronal differentiation by recruiting TET1 to
CC genomic loci and thereby regulating 5-hydroxymethylcytosine levels (By
CC similarity). Plays a role in the regulation of DNA virus-mediated
CC innate immune response by assembling into the HDP-RNP complex, a
CC complex that serves as a platform for IRF3 phosphorylation and
CC subsequent innate immune response activation through the cGAS-STING
CC pathway (By similarity). {ECO:0000250|UniProtKB:Q15233,
CC ECO:0000250|UniProtKB:Q99K48, 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. Interacts with RNF43 (By similarity).
CC Interacts with PER1 and PER2 (PubMed:15860628). Part of the HDP-RNP
CC complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle
CC proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. Interacts
CC (via second RRM domain) with WASL; the interaction is direct. Component
CC of a multiprotein complex with WASL and SFPQ (By similarity). Interacts
CC with ERCC6 (By similarity). Interacts (via DNA-binding domain) with
CC TET1 (By similarity). {ECO:0000250|UniProtKB:Q15233,
CC ECO:0000250|UniProtKB:Q99K48, 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}.
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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 IntAct; Q5FVM4; 3.
DR MINT; Q5FVM4; -.
DR STRING; 10116.ENSRNOP00000004911; -.
DR iPTMnet; Q5FVM4; -.
DR PhosphoSitePlus; Q5FVM4; -.
DR SwissPalm; Q5FVM4; -.
DR jPOST; Q5FVM4; -.
DR PaxDb; Q5FVM4; -.
DR PRIDE; Q5FVM4; -.
DR Ensembl; ENSRNOT00000004911; ENSRNOP00000004911; ENSRNOG00000003689.
DR GeneID; 317259; -.
DR KEGG; rno:317259; -.
DR UCSC; RGD:1549738; rat.
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; NHTPRKQ; -.
DR OrthoDB; 1274880at2759; -.
DR PhylomeDB; Q5FVM4; -.
DR TreeFam; TF315795; -.
DR ChiTaRS; Nono; rat.
DR PRO; PR:Q5FVM4; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000003689; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q5FVM4; baseline and differential.
DR Genevisible; Q5FVM4; RN.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002218; P:activation of innate immune response; ISO:RGD.
DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12588; RRM1_p54nrb; 1.
DR Gene3D; 3.30.70.330; -; 2.
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 Pfam; PF08075; NOPS; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 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 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
