NONO_PONAB
ID NONO_PONAB Reviewed; 471 AA.
AC Q5RFL9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Non-POU domain-containing octamer-binding protein;
DE Short=NonO protein;
GN Name=NONO;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA- and RNA binding protein, involved in several nuclear
CC processes. Binds the conventional octamer sequence in double-stranded
CC DNA. Also binds single-stranded DNA and RNA at a site independent of
CC the duplex site. Involved in pre-mRNA splicing, probably as a
CC heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to
CC a purine-rich sequence located on the 3' side of U5 snRNA stem 1b.
CC Together with PSPC1, required for the formation of nuclear
CC paraspeckles. The SFPQ-NONO heteromer associated with MATR3 may play a
CC role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer
CC may be involved in DNA unwinding by modulating the function of
CC topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA
CC non-homologous end joining (NHEJ) required for double-strand break
CC repair and V(D)J recombination and may stabilize paired DNA ends. In
CC vitro, the complex strongly stimulates DNA end joining, binds directly
CC to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5
CC (Ku) dimer to establish a functional preligation complex. NONO is
CC involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex
CC binds to the CYP17 promoter and regulates basal and cAMP-dependent
CC transcriptional activity. NONO binds to an enhancer element in long
CC terminal repeats of endogenous intracisternal A particles (IAPs) and
CC activates transcription. Regulates the circadian clock by repressing
CC the transcriptional activator activity of the CLOCK-ARNTL/BMAL1
CC heterodimer (By similarity). Important for the functional organization
CC of GABAergic synapses. Plays a specific and important role in the
CC regulation of synaptic RNAs and GPHN/gephyrin scaffold structure,
CC through the regulation of GABRA2 transcript. Plays a key role during
CC neuronal differentiation by recruiting TET1 to genomic loci and thereby
CC regulating 5-hydroxymethylcytosine levels. Plays a role in the
CC regulation of DNA virus-mediated innate immune response by assembling
CC into the HDP-RNP complex, a complex that serves as a platform for IRF3
CC phosphorylation and subsequent innate immune response activation
CC through the cGAS-STING pathway. {ECO:0000250|UniProtKB:Q15233,
CC ECO:0000250|UniProtKB:Q5FVM4, ECO:0000250|UniProtKB:Q99K48}.
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 (By similarity). 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}.
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; CR857136; CAH89438.1; -; mRNA.
DR RefSeq; NP_001124612.1; NM_001131140.1.
DR AlphaFoldDB; Q5RFL9; -.
DR BMRB; Q5RFL9; -.
DR SMR; Q5RFL9; -.
DR STRING; 9601.ENSPPYP00000022896; -.
DR Ensembl; ENSPPYT00000023859; ENSPPYP00000022896; ENSPPYG00000020451.
DR GeneID; 100171449; -.
DR KEGG; pon:100171449; -.
DR CTD; 4841; -.
DR eggNOG; KOG0115; Eukaryota.
DR GeneTree; ENSGT00940000154442; -.
DR InParanoid; Q5RFL9; -.
DR OrthoDB; 1274880at2759; -.
DR Proteomes; UP000001595; Chromosome X.
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; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042382; C:paraspeckles; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002218; P:activation of innate immune response; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; ISS: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; IEA:Ensembl.
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: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 2: Evidence at transcript 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..471
FT /note="Non-POU domain-containing octamer-binding protein"
FT /id="PRO_0000081685"
FT DOMAIN 74..141
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 148..229
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..373
FT /note="DBHS"
FT /evidence="ECO:0000250"
FT REGION 443..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 268..372
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 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT MOD_RES 198
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT MOD_RES 295
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K48"
FT MOD_RES 371
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K48"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT MOD_RES 456
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 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT CROSSLNK 190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15233"
SQ SEQUENCE 471 AA; 54232 MW; 26BBD3828F5B9E49 CRC64;
MQSNKTFNLE KQNHTPRKHH QHHHQQQHHQ QQQQQPPPPP IPANGQQASS QNEGLTIDLK
NFRKPGEKTF TQRSRLFVGN LPPDITEEEM RKLFEKYGKA GEVFIHKDKG FGFIRLETRT
LAEIAKVELD NMPLRGKQLR VRFACHSASL TVRNLPQYVS NELLEEAFSV FGQVERAVVI
VDDRGRPSGK GIVEFSGKPA ARKALDRCSE GSFLLTTFPR PVTVEPMDQL DDEEGLPEKL
VIKNQQFHKE REQPPRFAQP GSFEYEYAMR WKALIEMEKQ QQDQVDRNIK EAREKLEMEM
EAARHEHQVM LMRQDLMRRQ EELRRMEELH NQEVQKRKQL ELRQEEERRR REEEMRRQQE
EMMRRQQEGF KGTFPDAREQ EIRMGQMAMG GAMGINNRGA MPPAPVPAGT PAPPGPATMM
PDGTLGLTPP TTERFGQAAT MEGIGAIGGT PPAFNRAAPG AEFAPNKRRR Y
