NFIA_CHICK
ID NFIA_CHICK Reviewed; 522 AA.
AC P17923;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=NFI-A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Embryo;
RX PubMed=2339052; DOI=10.1093/nar/18.9.2607;
RA Rupp R.A.W., Kruse U., Multhaup G., Goebel U., Beyreuther K., Sippel A.E.;
RT "Chicken NFI/TGGCA proteins are encoded by at least three independent
RT genes: NFI-A, NFI-B and NFI-C with homologues in mammalian genomes.";
RL Nucleic Acids Res. 18:2607-2616(1990).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=P17923-1; 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:Q12857}.
CC -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00436}.
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DR EMBL; X51486; CAA35853.1; -; mRNA.
DR PIR; S09996; S09996.
DR AlphaFoldDB; P17923; -.
DR STRING; 9031.ENSGALP00000017752; -.
DR PaxDb; P17923; -.
DR PRIDE; P17923; -.
DR Ensembl; ENSGALT00000089894; ENSGALP00000061058; ENSGALG00000010924. [P17923-1]
DR VEuPathDB; HostDB:geneid_396210; -.
DR eggNOG; KOG3663; Eukaryota.
DR GeneTree; ENSGT00950000182916; -.
DR InParanoid; P17923; -.
DR PhylomeDB; P17923; -.
DR PRO; PR:P17923; -.
DR Proteomes; UP000000539; Chromosome 8.
DR Bgee; ENSGALG00000010924; Expressed in cerebellum and 11 other tissues.
DR ExpressionAtlas; P17923; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:UniProt.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Direct protein sequencing;
KW DNA replication; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..522
FT /note="Nuclear factor 1 A-type"
FT /id="PRO_0000100194"
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..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 407..415
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 293..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..470
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 57474 MW; C51F3E5FE6077740 CRC64;
MYSPLCLTQD EFHPFIEALL PHVRAFAYTW FNLQARKRKY FKKHEKRMSK EEERAVKDEL
LSEKPEVKQK WASRLLAKLR KDIRPEFRED FVLTVTGKKP PCCVLSNPDQ KGKMRRIDCL
RQADKVWRLD LVMVILFKGI PLESTDGERL VKSPQCSNPG LCVQPHHIGV SVKELDLYLA
YFVHAADSSQ SESPSQPSEA DIKDQPENGH LGFQDSFVTS GVFSVTELVR VSQTPIAAGT
GPNFSLSDLE SSSYYSMSPG AMRRSLPSTS STSSTKRIKS VEDEMDSPGE EPFYTSQGRS
PGSGSQSSGW HEVEPGYLRN PEHRGALHGM PSPTALKKSE KSGFSSPSPS QTSSLGTAFT
QHHRPVITGP RASPHATPST LHFPTSPIIQ QPGPYFSHPA IRYHPQETLK EFVQLVCPDA
GQQAGQVGFL NPNGSSQGKV HNPFLPTPML PPPPPPPMAR PVPLPVPDTK PPTTSTEGGA
TSPTSPTYST PSTSPANRFV SVGPRDPSFV NIPQQTQSWY LG
