ID   NKRF_MOUSE              Reviewed;         690 AA.
AC   Q8BY02; A2A3V7; Q8BJU5; Q9CRL2;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=NF-kappa-B-repressing factor;
DE            Short=NFkB-repressing factor;
DE   AltName: Full=Transcription factor NRF;
GN   Name=Nkrf; Synonyms=Nrf;
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, and Embryo;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
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).
CC   -!- FUNCTION: Enhances the ATPase activity of DHX15 by acting like a brace
CC       that tethers mobile sections of DHX15 together, stabilizing a
CC       functional conformation with high RNA affinity of DHX15. Involved in
CC       the constitutive silencing of the interferon beta promoter,
CC       independently of the virus-induced signals, and in the inhibition of
CC       the basal and cytokine-induced iNOS promoter activity. Also involved in
CC       the regulation of IL-8 transcription. May also act as a DNA-binding
CC       transcription regulator: interacts with a specific negative regulatory
CC       element (NRE) 5'-AATTCCTCTGA-3' to mediate transcriptional repression
CC       of certain NK-kappa-B responsive genes. {ECO:0000250|UniProtKB:O15226}.
CC   -!- SUBUNIT: Interacts with NF-kappa-B. Interacts with XRN2. Interacts (via
CC       G-patch domain) with DHX15; promoting the RNA helicase activity of
CC       DHX15. {ECO:0000250|UniProtKB:O15226}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:O15226}.
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DR   EMBL; AK020455; BAB32107.1; -; mRNA.
DR   EMBL; AK042690; BAC31334.1; -; mRNA.
DR   EMBL; AK079123; BAC37550.1; -; mRNA.
DR   EMBL; AL450399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC138828; AAI38829.1; -; mRNA.
DR   EMBL; BC138829; AAI38830.1; -; mRNA.
DR   RefSeq; NP_084167.2; NM_029891.2.
DR   AlphaFoldDB; Q8BY02; -.
DR   BioGRID; 218599; 6.
DR   IntAct; Q8BY02; 2.
DR   STRING; 10090.ENSMUSP00000061546; -.
DR   PhosphoSitePlus; Q8BY02; -.
DR   EPD; Q8BY02; -.
DR   MaxQB; Q8BY02; -.
DR   PaxDb; 10090-ENSMUSP00000061546; -.
DR   PeptideAtlas; Q8BY02; -.
DR   ProteomicsDB; 293570; -.
DR   Pumba; Q8BY02; -.
DR   Antibodypedia; 462; 242 antibodies from 30 providers.
DR   DNASU; 77286; -.
DR   Ensembl; ENSMUST00000057093.8; ENSMUSP00000061546.7; ENSMUSG00000044149.8.
DR   GeneID; 77286; -.
DR   KEGG; mmu:77286; -.
DR   UCSC; uc009sxw.1; mouse.
DR   AGR; MGI:1924536; -.
DR   CTD; 55922; -.
DR   MGI; MGI:1924536; Nkrf.
DR   VEuPathDB; HostDB:ENSMUSG00000044149; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000157256; -.
DR   HOGENOM; CLU_025268_0_0_1; -.
DR   InParanoid; Q8BY02; -.
DR   OMA; SVLWTNH; -.
DR   OrthoDB; 5317227at2759; -.
DR   PhylomeDB; Q8BY02; -.
DR   TreeFam; TF326321; -.
DR   BioGRID-ORCS; 77286; 1 hit in 81 CRISPR screens.
DR   ChiTaRS; Nkrf; mouse.
DR   PRO; PR:Q8BY02; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q8BY02; Protein.
DR   Bgee; ENSMUSG00000044149; Expressed in pontine nuclear group and 226 other cell types or tissues.
DR   ExpressionAtlas; Q8BY02; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   CDD; cd02640; R3H_NRF; 1.
DR   Gene3D; 3.30.160.20; -; 2.
DR   Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR034071; R3H_NRF.
DR   PANTHER; PTHR16148:SF15; NF-KAPPA-B-REPRESSING FACTOR; 1.
DR   PANTHER; PTHR16148; NF-KAPPA-B-REPRESSING FACTOR-RELATED; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR   SUPFAM; SSF82708; R3H domain; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   Genevisible; Q8BY02; MM.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..690
FT                   /note="NF-kappa-B-repressing factor"
FT                   /id="PRO_0000096870"
FT   DOMAIN          551..596
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   DOMAIN          600..664
FT                   /note="R3H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT   DNA_BIND        296..388
FT                   /evidence="ECO:0000250|UniProtKB:O15226"
FT   REGION          1..296
FT                   /note="Active repression domain"
FT                   /evidence="ECO:0000250|UniProtKB:O15226"
FT   REGION          27..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           25..45
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:O15226"
FT   COMPBIAS        133..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         618
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15226"
FT   CROSSLNK        68
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O15226"
FT   CROSSLNK        500
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O15226"
FT   CROSSLNK        666
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O15226"
FT   CROSSLNK        674
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O15226"
FT   CONFLICT        686
FT                   /note="M -> V (in Ref. 1; BAC37550)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   690 AA;  77739 MW;  0A99E1141183F999 CRC64;
     MEKILHMAEG IDIGEMPSYD LMLPKPSKGQ KRYLSTYDGQ NPPKKQAGSK FHVRARFEPV
     HFVASSSKAE RQEDPYGPQT KDVNGRTHFA SMPRNFYQDY TQDSFSIQDG NSQYCNSSGF
     IFTKDQPVAT NMYFDSGNPA PSSTSQQANC QPAPEPPPSQ MYPESLVAEK QYFIEKLTAT
     IWKNLSNPEM TSGSDKINYT YMLTRCIQAC KTNPEYIYAP LKEIPPADIP KNKKLLTDGY
     ACEVRCQNIY LTTGYAGSKN GSRDRATELA VKLLQKRIEV RVVRRKFKHI IGEDLVVCQI
     GMLSYEFPPA LKPPEDLVVL GKDASGQPIF NSSAKHWTNF VITENANDAI GILNNSASFN
     KMSIEYKYEM MPNRTWRCRV FLQDHCLAEG YGTKKTSKHA AADEALKVLQ KTQPTYPSVK
     SSQCHSGSSP KGSGKKKDIK DLVVYENSSN PVCTLNDTAQ FNRMTVEYVY ERMTGLRWKC
     KVILESEVIA EAVGVKKSVK YEAAGEAVKT LKKTQPTVIN NLKKGTVEDV ISRNEIQGRS
     AEEAYKQQIK EDNIGNQLLR KMGWTGGGLG KSGEGIREPI SVKEQHKREG LGLDVERVNK
     IAKRDIEQII RNYARSESHS DLTFSTELTN DERKQIHQIA QKYGLKSKSH GVGHDRYLVV
     GRKRRKEDLL DQLKQEGQVG HYELVMPQAN
//