NFIA_RAT
ID NFIA_RAT Reviewed; 509 AA.
AC P09414; Q54A99; Q63782;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 160.
DE RecName: Full=Nuclear factor 1 A-type;
DE Short=NF1-A;
DE Short=Nuclear factor 1/A;
DE AltName: Full=CCAAT-box-binding transcription factor;
DE Short=CTF;
DE AltName: Full=Nuclear factor I/A;
DE Short=NF-I/A;
DE Short=NFI-A;
DE AltName: Full=TGGCA-binding protein;
GN Name=Nfia; Synonyms=Nf1l21;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8832903; DOI=10.1007/bf00997237;
RA Monaci P., Nuzzo M., Stampfli S., Tollervey D., de Simone V., Nicosia A.;
RT "A complex interplay of positive and negative elements is responsible for
RT the different transcriptional activity of liver NF1 variants.";
RL Mol. Biol. Rep. 21:147-158(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9089412; DOI=10.1093/oxfordjournals.jbchem.a021595;
RA Osada S., Daimon S., Ikeda T., Nishihara T., Yano K., Yamasaki M.,
RA Imagawa M.;
RT "Nuclear factor 1 family proteins bind to the silencer element in the rat
RT glutathione transferase P gene.";
RL J. Biochem. 121:355-363(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11835404; DOI=10.1002/jcb.10082;
RA Misawa H., Yamaguchi M.;
RT "Identification of transcription factor in the promoter region of rat
RT regucalcin gene: binding of nuclear factor I-A1 to TTGGC motif.";
RL J. Cell. Biochem. 84:795-802(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-509, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=3053160; DOI=10.1002/j.1460-2075.1988.tb03178.x;
RA Paonessa G., Gounari F., Frank R., Cortese R.;
RT "Purification of a NF1-like DNA-binding protein from rat liver and cloning
RT of the corresponding cDNA.";
RL EMBO J. 7:3115-3123(1988).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-280; SER-287;
RP SER-300; SER-305 AND SER-319, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: 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 -!- SUBUNIT: Binds DNA as a homodimer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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:Q12857}.
CC -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00436}.
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DR EMBL; X84209; CAA58995.1; -; mRNA.
DR EMBL; D78017; BAA11203.1; -; mRNA.
DR EMBL; AB060652; BAB43904.1; -; mRNA.
DR EMBL; X13167; CAA31565.1; -; mRNA.
DR PIR; JC5428; JC5428.
DR RefSeq; NP_037120.1; NM_012988.2.
DR AlphaFoldDB; P09414; -.
DR STRING; 10116.ENSRNOP00000004017; -.
DR iPTMnet; P09414; -.
DR PhosphoSitePlus; P09414; -.
DR jPOST; P09414; -.
DR PaxDb; P09414; -.
DR PeptideAtlas; P09414; -.
DR GeneID; 25492; -.
DR KEGG; rno:25492; -.
DR UCSC; RGD:3170; rat.
DR CTD; 4774; -.
DR RGD; 3170; Nfia.
DR eggNOG; KOG3663; Eukaryota.
DR InParanoid; P09414; -.
DR OrthoDB; 967862at2759; -.
DR PhylomeDB; P09414; -.
DR PRO; PR:P09414; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0060074; P:synapse maturation; ISO:RGD.
DR GO; GO:0072189; P:ureter development; ISO:RGD.
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; Direct protein sequencing; DNA replication; DNA-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..509
FT /note="Nuclear factor 1 A-type"
FT /id="PRO_0000100193"
FT DNA_BIND 1..194
FT /note="CTF/NF-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT REGION 189..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 394..402
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT COMPBIAS 259..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..457
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT MOD_RES 389
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q02780"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12857"
SQ SEQUENCE 509 AA; 55976 MW; 59120C7090229F87 CRC64;
MYSPLCLTQD EFHPFIEALL PHVRAFAYTW FNLQARKRKY FKKHEKRMSK EEERAVKDEL
LSEKPEVKQK WASRLLAKLR KDIRPEYRED FVLTVTGKKP PCCVLSNPDQ KGKMRRIDCL
RQADKVWRLD LVMVILFKGI PLESTDGERL VKSPQCSNPG LCVQPHHIGV SVKELDLYLA
YFVHAADSSQ SESPSQPSDA DIKDQPENGH LGFQDSFVTS GVFSVTELVR VSQTPIAAGT
GPNFSLSDLE SSSYYSMSPG AMRRSLPSTS STSSTKRLKS VEDEMDSPGE EPFYTGQGRS
PGSGSQSSGW HEVEPGMPSP TTLKKSEKSG FSSPSPSQTS SLGTAFTQHH RPVITGPRAS
PHATPSTLHF PTSPIIQQPG PYFSHPAIRY HPQETLKEFV QLVCPDAGQQ AGQVGFLNPN
GSSQGKVHNP FLPTPMLPPP PPPPMARPVP LPMPDTKPPT TSTEGGAASP TSPTYSTPST
SPANRFVSVG PRDPSFVNIP QQTQSWYLG
