NFIB_MESAU
ID NFIB_MESAU Reviewed; 561 AA.
AC P13622;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 112.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3194401; DOI=10.1073/pnas.85.23.8963;
RA Gil G., Smith J.R., Goldstein J.L., Slaughter C.A., Orth K., Brown M.S.,
RA Osborne T.F.;
RT "Multiple genes encode nuclear factor 1-like proteins that bind to the
RT promoter for 3-hydroxy-3-methylglutaryl-coenzyme A reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8963-8967(1988).
CC -!- FUNCTION: Transcriptional activator of GFAP, essential for proper brain
CC development. Recognizes and binds the palindromic sequence 5'-
CC TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the
CC origin of replication of adenovirus type 2. These proteins are
CC individually capable of activating transcription and replication.
CC {ECO:0000250|UniProtKB:P97863}.
CC -!- SUBUNIT: Binds DNA as a homodimer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=P13622-1; Sequence=Displayed;
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 -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00436}.
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DR EMBL; J04122; AAA37082.1; -; mRNA.
DR PIR; A31256; A31256.
DR RefSeq; NP_001268624.1; NM_001281695.1. [P13622-1]
DR AlphaFoldDB; P13622; -.
DR SMR; P13622; -.
DR STRING; 10036.XP_005082225.1; -.
DR GeneID; 101825256; -.
DR CTD; 4781; -.
DR eggNOG; KOG3663; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0044300; C:cerebellar mossy fiber; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0021960; P:anterior commissure morphogenesis; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0060486; P:club cell differentiation; ISS:UniProtKB.
DR GO; GO:0071679; P:commissural neuron axon guidance; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0061141; P:lung ciliated cell differentiation; ISS:UniProtKB.
DR GO; GO:2000795; P:negative regulation of epithelial cell proliferation involved in lung morphogenesis; ISS:UniProtKB.
DR GO; GO:2000791; P:negative regulation of mesenchymal cell proliferation involved in lung development; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0021740; P:principal sensory nucleus of trigeminal nerve development; ISS:UniProtKB.
DR GO; GO:0060509; P:type I pneumocyte differentiation; ISS:UniProtKB.
DR GO; GO:0060510; P:type II pneumocyte differentiation; ISS: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 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA replication; DNA-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..561
FT /note="Nuclear factor 1 B-type"
FT /id="PRO_0000100196"
FT DNA_BIND 1..195
FT /note="CTF/NF-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT REGION 189..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..445
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:0000250|UniProtKB:P97863"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00712"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00712"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00712"
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:0000250|UniProtKB:P97863"
FT MOD_RES 388
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P97863"
SQ SEQUENCE 561 AA; 62718 MW; F634FDB26705A07C CRC64;
MMYSPICLTQ DEFHPFIEAL LPHVRAIAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE
LLSEKPEIKQ KWASRLLAKL RKDIRQEYRE DFVLTVTGKK HPCCVLSNPD QKGKIRRIDC
LRQADKVWRL DLVMVILFKG IPLESTDGER LMKSPHCTNP ALCVQPHHIT VSVKELDLFL
AYYVQEQDSG QSGSPSHNDP 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 EAYTASGTSQ ASRYVGLNPR
DPSFLHQQQL RICDWTMNQN GRHLYPSTSE DTLGITWQSP GTWASLVPFQ VSNRTPILPA
NVQNYGLNII GEPFLQAETS N
