NFIB_MOUSE
ID NFIB_MOUSE Reviewed; 570 AA.
AC P97863; P70252; P70253; P70254; Q9R1G4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Nuclear factor 1 B-type;
DE Short=NF1-B;
DE Short=Nuclear factor 1/B;
DE AltName: Full=CCAAT-box-binding transcription factor;
DE Short=CTF;
DE AltName: Full=Nuclear factor I/B;
DE Short=NF-I/B;
DE Short=NFI-B;
DE AltName: Full=TGGCA-binding protein;
GN Name=Nfib;
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 [MRNA] (ISOFORM 3).
RC STRAIN=BALB/cJ; TISSUE=Liver, and Skeletal muscle;
RX PubMed=9056636;
RX DOI=10.1002/(sici)1097-0177(199703)208:3<313::aid-aja3>3.0.co;2-l;
RA Chaudhry A.Z., Lyons G.E., Gronostajski R.M.;
RT "Expression patterns of the four nuclear factor I genes during mouse
RT embryogenesis indicate a potential role in development.";
RL Dev. Dyn. 208:313-325(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2 AND 3).
RC STRAIN=NIH Swiss;
RX PubMed=12568726; DOI=10.1016/s0378-1119(02)01204-0;
RA Gruender A., Qian F., Ebel T.T., Mincheva A., Lichter P., Kruse U.,
RA Sippel A.E.;
RT "Genomic organization, splice products and mouse chromosomal localization
RT of genes for transcription factor Nuclear Factor One.";
RL Gene 304:171-181(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-187.
RC STRAIN=129;
RX PubMed=10087299; DOI=10.1007/s003359901008;
RA Fletcher C.F., Jenkins N.A., Copeland N.G., Chaudhry A.Z.,
RA Gronostajski R.M.;
RT "Exon structure of the nuclear factor I DNA-binding domain from C. elegans
RT to mammals.";
RL Mamm. Genome 10:390-396(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15632069; DOI=10.1128/mcb.25.2.685-698.2005;
RA Steele-Perkins G., Plachez C., Butz K.G., Yang G., Bachurski C.J.,
RA Kinsman S.L., Litwack E.D., Richards L.J., Gronostajski R.M.;
RT "The transcription factor gene Nfib is essential for both lung maturation
RT and brain development.";
RL Mol. Cell. Biol. 25:685-698(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286; SER-292; SER-295 AND
RP SER-312, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-335 AND ARG-388, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30388402; DOI=10.1016/j.ajhg.2018.10.006;
RA Schanze I., Bunt J., Lim J.W.C., Schanze D., Dean R.J., Alders M.,
RA Blanchet P., Attie-Bitach T., Berland S., Boogert S., Boppudi S.,
RA Bridges C.J., Cho M.T., Dobyns W.B., Donnai D., Douglas J., Earl D.L.,
RA Edwards T.J., Faivre L., Fregeau B., Genevieve D., Gerard M., Gatinois V.,
RA Holder-Espinasse M., Huth S.F., Izumi K., Kerr B., Lacaze E., Lakeman P.,
RA Mahida S., Mirzaa G.M., Morgan S.M., Nowak C., Peeters H., Petit F.,
RA Pilz D.T., Puechberty J., Reinstein E., Riviere J.B., Santani A.B.,
RA Schneider A., Sherr E.H., Smith-Hicks C., Wieland I., Zackai E., Zhao X.,
RA Gronostajski R.M., Zenker M., Richards L.J.;
RT "NFIB haploinsufficiency is associated with intellectual disability and
RT macrocephaly.";
RL Am. J. Hum. Genet. 103:752-768(2018).
CC -!- FUNCTION: Transcriptional activator of GFAP, essential for proper brain
CC development (PubMed:15632069, PubMed:30388402). Recognizes and binds
CC the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and
CC cellular promoters and in the origin of replication of adenovirus type
CC 2. These proteins are individually capable of activating transcription
CC and replication (PubMed:30388402). {ECO:0000269|PubMed:15632069,
CC ECO:0000269|PubMed:30388402}.
CC -!- SUBUNIT: Binds DNA as a homodimer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P97863-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97863-2; Sequence=VSP_003547;
CC Name=3;
CC IsoId=P97863-3; Sequence=VSP_003548, VSP_003549;
CC -!- TISSUE SPECIFICITY: Highest expression in lung, skeletal muscle and
CC heart. Lower levels in liver, kidney and brain. Very low levels in
CC testis and spleen.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:O00712}.
CC -!- DISRUPTION PHENOTYPE: NFIB knockout results in failure of lung
CC maturation, and severe defects in development of the corpus callosum,
CC specific midline glial populations, the hippocampus and the pons. GFAP
CC expression is reduced in brains of NFIB-null mice (PubMed:15632069).
CC Conditional NFIB knockdown in the telencephalon results in significant
CC enlargement of the cerebral cortex with preservation of overall brain
CC structure and inter-hemispheric connectivity (PubMed:30388402).
CC {ECO:0000269|PubMed:15632069, ECO:0000269|PubMed:30388402}.
CC -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00436}.
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DR EMBL; U57634; AAB49929.1; -; mRNA.
DR EMBL; Y07685; CAA68949.1; -; mRNA.
DR EMBL; Y07686; CAA68950.1; -; mRNA.
DR EMBL; Y07687; CAA68951.1; -; mRNA.
DR EMBL; BC014290; AAH14290.1; -; mRNA.
DR EMBL; AF111264; AAD39099.1; -; Genomic_DNA.
DR CCDS; CCDS38790.1; -. [P97863-3]
DR CCDS; CCDS51213.1; -. [P97863-1]
DR RefSeq; NP_001106680.1; NM_001113209.2. [P97863-1]
DR RefSeq; NP_032713.3; NM_008687.6. [P97863-3]
DR AlphaFoldDB; P97863; -.
DR SMR; P97863; -.
DR BioGRID; 201747; 3.
DR IntAct; P97863; 2.
DR MINT; P97863; -.
DR STRING; 10090.ENSMUSP00000052863; -.
DR iPTMnet; P97863; -.
DR PhosphoSitePlus; P97863; -.
DR jPOST; P97863; -.
DR MaxQB; P97863; -.
DR PaxDb; P97863; -.
DR PRIDE; P97863; -.
DR ProteomicsDB; 287497; -. [P97863-1]
DR ProteomicsDB; 287498; -. [P97863-2]
DR ProteomicsDB; 287499; -. [P97863-3]
DR Antibodypedia; 1309; 221 antibodies from 30 providers.
DR DNASU; 18028; -.
DR Ensembl; ENSMUST00000050872; ENSMUSP00000052863; ENSMUSG00000008575. [P97863-1]
DR Ensembl; ENSMUST00000064770; ENSMUSP00000067629; ENSMUSG00000008575. [P97863-3]
DR GeneID; 18028; -.
DR KEGG; mmu:18028; -.
DR UCSC; uc008tjz.2; mouse. [P97863-1]
DR UCSC; uc008tkd.3; mouse. [P97863-2]
DR CTD; 4781; -.
DR MGI; MGI:103188; Nfib.
DR VEuPathDB; HostDB:ENSMUSG00000008575; -.
DR eggNOG; KOG3663; Eukaryota.
DR GeneTree; ENSGT00950000182916; -.
DR HOGENOM; CLU_012576_3_0_1; -.
DR InParanoid; P97863; -.
DR OMA; TEAFCKS; -.
DR PhylomeDB; P97863; -.
DR TreeFam; TF313889; -.
DR BioGRID-ORCS; 18028; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Nfib; mouse.
DR PRO; PR:P97863; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P97863; protein.
DR Bgee; ENSMUSG00000008575; Expressed in rostral migratory stream and 285 other tissues.
DR ExpressionAtlas; P97863; baseline and differential.
DR Genevisible; P97863; MM.
DR GO; GO:0044300; C:cerebellar mossy fiber; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:MGI.
DR GO; GO:0021960; P:anterior commissure morphogenesis; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0060689; P:cell differentiation involved in salivary gland development; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0060486; P:club cell differentiation; IMP:UniProtKB.
DR GO; GO:0071679; P:commissural neuron axon guidance; IMP:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0002067; P:glandular epithelial cell differentiation; IMP:MGI.
DR GO; GO:0010001; P:glial cell differentiation; IMP:UniProtKB.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0061141; P:lung ciliated cell differentiation; IMP:UniProtKB.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:MGI.
DR GO; GO:2000795; P:negative regulation of epithelial cell proliferation involved in lung morphogenesis; IMP:UniProtKB.
DR GO; GO:2000791; P:negative regulation of mesenchymal cell proliferation involved in lung development; IMP:UniProtKB.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:MGI.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0021740; P:principal sensory nucleus of trigeminal nerve development; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0060662; P:salivary gland cavitation; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0060509; P:type I pneumocyte differentiation; IMP:UniProtKB.
DR GO; GO:0060510; P:type II pneumocyte differentiation; IMP:UniProtKB.
DR InterPro; IPR000647; CTF/NFI.
DR InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR PANTHER; PTHR11492; PTHR11492; 1.
DR Pfam; PF00859; CTF_NFI; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR SMART; SM00523; DWA; 1.
DR PROSITE; PS00349; CTF_NFI_1; 1.
DR PROSITE; PS51080; CTF_NFI_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA replication; DNA-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..570
FT /note="Nuclear factor 1 B-type"
FT /id="PRO_0000100197"
FT DNA_BIND 1..195
FT /note="CTF/NF-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT REGION 252..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 397..405
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:O00712"
FT COMPBIAS 252..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00712"
FT MOD_RES 286
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00712"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00712"
FT MOD_RES 335
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 388
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 416..498
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003547"
FT VAR_SEQ 416..420
FT /note="PNSSG -> SWYLG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9056636"
FT /id="VSP_003548"
FT VAR_SEQ 421..570
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9056636"
FT /id="VSP_003549"
FT VARIANT 131
FT /note="D -> G (in strain: NIH Swiss)"
SQ SEQUENCE 570 AA; 63507 MW; D94AB4400A2811CC CRC64;
MMYSPICLTQ DEFHPFIEAL LPHVRAIAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE
LLSEKPEIKQ KWASRLLAKL RKDIRQEYRE DFVLTVTGKK HPCCVLSNPD QKGKIRRIDC
LRQADKVWRL DLVMVILFKG IPLESTDGER LMKSPHCTNP ALCVQPHHIT VSVKELDLFL
AYYVQEQDSG QSGSPSHSDP AKNPPGYLED SFVKSGVFNV SELVRVSRTP ITQGTGVNFP
IGEIPSQPYY HDMNSGVNLQ RSLSSPPSSK RPKTISIDEN MEPSPTGDFY PSPNSPAAGS
RTWHERDQDM SSPTTMKKPE KPLFSSTSPQ DSSPRLSTFP QHHHPGIPGV AHSVISTRTP
PPPSPLPFPT QAILPPAPSS YFSHPTIRYP PHLNPQDTLK NYVPSYDPSS PQTSQPNSSG
QVVGKVPGHF TPVLAPSPHP SAVRPVTLTM TDTKPITTST EGEAASPTAT TYTASGTSQA
NRYVGLSPRD PSFLHQQQLR ICDWTMNQNG RHLYPSTSED TLGITWQSPG TWASLVPFQV
SNRTPILPAN VQNYGLNIIG EPFLQAETSN
