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NFIC_PIG
ID   NFIC_PIG                Reviewed;         506 AA.
AC   P21999;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Nuclear factor 1 C-type;
DE            Short=NF1-C;
DE            Short=Nuclear factor 1/C;
DE   AltName: Full=CCAAT-box-binding transcription factor;
DE            Short=CTF;
DE   AltName: Full=Nuclear factor I/C;
DE            Short=NF-I/C;
DE            Short=NFI-C;
DE   AltName: Full=TGGCA-binding protein;
GN   Name=NFIC; Synonyms=NFI;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2513876; DOI=10.1021/bi00446a034;
RA   Meisterernst M., Rogge L., Foeckler R., Karaghiosoff M., Winnacker E.L.;
RT   "Structural and functional organization of a porcine gene coding for
RT   nuclear factor I.";
RL   Biochemistry 28:8191-8200(1989).
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=P21999-1; 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:P08651}.
CC   -!- SIMILARITY: Belongs to the CTF/NF-I family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00436}.
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DR   EMBL; J02875; AAA31093.1; -; Genomic_DNA.
DR   PIR; A33416; A33416.
DR   AlphaFoldDB; P21999; -.
DR   PRIDE; P21999; -.
DR   InParanoid; P21999; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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   3: Inferred from homology;
KW   Acetylation; Activator; Alternative splicing; DNA replication; DNA-binding;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..506
FT                   /note="Nuclear factor 1 C-type"
FT                   /id="PRO_0000100201"
FT   DNA_BIND        1..195
FT                   /note="CTF/NF-I"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT   REGION          261..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           404..412
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   COMPBIAS        266..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         300
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P70255"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70255"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         365
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         365
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         395
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         451
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         473
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         475
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
FT   MOD_RES         485
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08651"
SQ   SEQUENCE   506 AA;  55462 MW;  6315A9474807F4C0 CRC64;
     MYSSPLCLTQ DEFHPFIEAL LPHVRAFAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE
     LLGEKAEVKQ KWASRLLAKL RKDIRPECRE DFVLAITGKK APGCVLSNPD QKGKMRRIDC
     LRQADKVWRL DLVMVILFKG IPLESTDGER LVKAAQCGHP VLCVQPHHIG VAVKELDLYL
     AYFVRERDAE QSGSPRAGMG SDQEDSKPIT LDTTDFQESF VTSGVFSVTE LIQVSRTPVV
     TGTGPNFSLG ELQGHMAYDL NPASTGMRRT LPSTSSSGSK RHKSGSMEED VDTSPGGDYY
     TSPSSPTSSN RNWTEDMEGG ISSPVKKTEM DKSPFNSPSP QDSPRLSSFT QHHRPVIAVH
     SGIARSPHPS SALHFPTTSI LPQTASTYFP HTAIRYPPHL NPQDPLKDLV SLACDPASQQ
     PGPLNGSGQL KMSSHCLSAQ MLAPPPPGLP RLALPPATKP TSEGGSSSPT SPSYSTPGTS
     PANRSFVGLG PRDPTGIYQA QSWYLG
 
 
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