NFIB_BOVIN
ID NFIB_BOVIN Reviewed; 420 AA.
AC Q0VCL6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Nuclear factor 1 B-type;
DE Short=NF1-B;
DE Short=Nuclear factor 1/B;
DE AltName: Full=Nuclear factor I/B;
DE Short=NF-I/B;
DE Short=NFI-B;
GN Name=NFIB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00436}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC120107; AAI20108.1; -; mRNA.
DR RefSeq; NP_001069572.1; NM_001076104.2.
DR AlphaFoldDB; Q0VCL6; -.
DR STRING; 9913.ENSBTAP00000011234; -.
DR PaxDb; Q0VCL6; -.
DR PRIDE; Q0VCL6; -.
DR Ensembl; ENSBTAT00000075331; ENSBTAP00000063855; ENSBTAG00000027442.
DR GeneID; 538474; -.
DR KEGG; bta:538474; -.
DR CTD; 4781; -.
DR VEuPathDB; HostDB:ENSBTAG00000027442; -.
DR VGNC; VGNC:32039; NFIB.
DR eggNOG; KOG3663; Eukaryota.
DR GeneTree; ENSGT00950000182916; -.
DR InParanoid; Q0VCL6; -.
DR OrthoDB; 967862at2759; -.
DR ChiTaRS; NFIB; cattle.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000027442; Expressed in intramuscular adipose tissue and 108 other tissues.
DR ExpressionAtlas; Q0VCL6; baseline and differential.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; DNA replication; DNA-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..420
FT /note="Nuclear factor 1 B-type"
FT /id="PRO_0000273723"
FT DNA_BIND 2..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..420
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..420
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 420 AA; 47499 MW; 685A0EF488320640 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 PQTSQSWYLG