NFIC_MOUSE
ID NFIC_MOUSE Reviewed; 439 AA.
AC P70255; O09072; P70256; Q3U2I9; Q99MA3; Q99MA4; Q99MA5; Q99MA6; Q99MA7;
AC Q99MA8; Q9R1G3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 186.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=NIH Swiss;
RX PubMed=12568726; DOI=10.1016/s0378-1119(02)01204-0;
RA Gruender A., Qian F., Ebel T.T., Mincheva A., Lichter P., Kruse U.,
RA Sippel A.E.;
RT "Genomic organization, splice products and mouse chromosomal localization
RT of genes for transcription factor Nuclear Factor One.";
RL Gene 304:171-181(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Liver, and Skeletal muscle;
RX PubMed=9056636;
RX DOI=10.1002/(sici)1097-0177(199703)208:3<313::aid-aja3>3.0.co;2-l;
RA Chaudhry A.Z., Lyons G.E., Gronostajski R.M.;
RT "Expression patterns of the four nuclear factor I genes during mouse
RT embryogenesis indicate a potential role in development.";
RL Dev. Dyn. 208:313-325(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 179-439 (ISOFORMS 1; 3; 4; 5; 6 AND 7).
RC STRAIN=CD-1; TISSUE=Mammary gland;
RA Kane R., Martin F.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE OF 11-187.
RC STRAIN=129;
RX PubMed=10087299; DOI=10.1007/s003359901008;
RA Fletcher C.F., Jenkins N.A., Copeland N.G., Chaudhry A.Z.,
RA Gronostajski R.M.;
RT "Exon structure of the nuclear factor I DNA-binding domain from C. elegans
RT to mammals.";
RL Mamm. Genome 10:390-396(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-333; SER-339 AND
RP SER-343, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300; SER-302; SER-305;
RP SER-323; SER-333; SER-337; SER-339 AND SER-343, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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=7;
CC Name=1; Synonyms=C1A, C2;
CC IsoId=P70255-1; Sequence=Displayed;
CC Name=2; Synonyms=C1B;
CC IsoId=P70255-2; Sequence=VSP_003557;
CC Name=3; Synonyms=C5;
CC IsoId=P70255-3; Sequence=VSP_007559;
CC Name=4; Synonyms=C8;
CC IsoId=P70255-4; Sequence=VSP_007557;
CC Name=5; Synonyms=C9;
CC IsoId=P70255-5; Sequence=VSP_007558;
CC Name=6; Synonyms=C10;
CC IsoId=P70255-6; Sequence=VSP_007556;
CC Name=7; Synonyms=C11;
CC IsoId=P70255-7; Sequence=VSP_007556, VSP_007559;
CC -!- TISSUE SPECIFICITY: Highest levels in skeletal muscle. Lower levels in
CC heart, liver, kidney, lung and brain. Very low levels in testis and
CC spleen.
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; Y07692; CAA68956.1; -; mRNA.
DR EMBL; Y07693; CAA68957.1; -; mRNA.
DR EMBL; U57635; AAB49930.1; -; mRNA.
DR EMBL; AK087539; BAC39918.1; -; mRNA.
DR EMBL; AK155258; BAE33151.1; -; mRNA.
DR EMBL; AF358455; AAK21331.1; -; mRNA.
DR EMBL; AF358456; AAK21332.1; -; mRNA.
DR EMBL; AF358457; AAK21333.1; -; mRNA.
DR EMBL; AF358458; AAK21334.1; -; mRNA.
DR EMBL; AF358459; AAK21335.1; -; mRNA.
DR EMBL; AF358460; AAK21336.1; -; mRNA.
DR EMBL; AF111265; AAD39100.1; -; Genomic_DNA.
DR CCDS; CCDS24058.1; -. [P70255-1]
DR CCDS; CCDS35999.1; -. [P70255-3]
DR RefSeq; NP_032714.1; NM_008688.3. [P70255-1]
DR RefSeq; XP_006513398.1; XM_006513335.3. [P70255-2]
DR AlphaFoldDB; P70255; -.
DR BioGRID; 201748; 4.
DR IntAct; P70255; 1.
DR STRING; 10090.ENSMUSP00000020461; -.
DR iPTMnet; P70255; -.
DR PhosphoSitePlus; P70255; -.
DR EPD; P70255; -.
DR jPOST; P70255; -.
DR MaxQB; P70255; -.
DR PaxDb; P70255; -.
DR PeptideAtlas; P70255; -.
DR PRIDE; P70255; -.
DR ProteomicsDB; 293543; -. [P70255-1]
DR ProteomicsDB; 293544; -. [P70255-2]
DR ProteomicsDB; 293545; -. [P70255-3]
DR ProteomicsDB; 293546; -. [P70255-4]
DR ProteomicsDB; 293547; -. [P70255-5]
DR ProteomicsDB; 293548; -. [P70255-6]
DR ProteomicsDB; 293549; -. [P70255-7]
DR Antibodypedia; 23195; 306 antibodies from 31 providers.
DR DNASU; 18029; -.
DR Ensembl; ENSMUST00000020461; ENSMUSP00000020461; ENSMUSG00000055053. [P70255-1]
DR Ensembl; ENSMUST00000078185; ENSMUSP00000077317; ENSMUSG00000055053. [P70255-4]
DR Ensembl; ENSMUST00000105321; ENSMUSP00000100958; ENSMUSG00000055053. [P70255-3]
DR Ensembl; ENSMUST00000117966; ENSMUSP00000113046; ENSMUSG00000055053. [P70255-2]
DR GeneID; 18029; -.
DR KEGG; mmu:18029; -.
DR UCSC; uc007ghx.1; mouse. [P70255-4]
DR UCSC; uc007ghy.1; mouse. [P70255-1]
DR UCSC; uc007gia.1; mouse. [P70255-2]
DR CTD; 4782; -.
DR MGI; MGI:109591; Nfic.
DR VEuPathDB; HostDB:ENSMUSG00000055053; -.
DR eggNOG; KOG3663; Eukaryota.
DR GeneTree; ENSGT00950000182916; -.
DR HOGENOM; CLU_012576_3_0_1; -.
DR InParanoid; P70255; -.
DR OMA; AQDEFHP; -.
DR OrthoDB; 967862at2759; -.
DR PhylomeDB; P70255; -.
DR TreeFam; TF313889; -.
DR BioGRID-ORCS; 18029; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Nfic; mouse.
DR PRO; PR:P70255; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P70255; protein.
DR Bgee; ENSMUSG00000055053; Expressed in tarsal region and 245 other tissues.
DR ExpressionAtlas; P70255; baseline and differential.
DR Genevisible; P70255; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
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 Acetylation; Activator; Alternative splicing; DNA replication; DNA-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..439
FT /note="Nuclear factor 1 C-type"
FT /id="PRO_0000100200"
FT DNA_BIND 1..195
FT /note="CTF/NF-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00436"
FT REGION 265..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..439
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 267..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 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:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
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 VAR_SEQ 1..10
FT /note="MYSSPLCLTQ -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12568726"
FT /id="VSP_003557"
FT VAR_SEQ 247..374
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_007556"
FT VAR_SEQ 320..361
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_007557"
FT VAR_SEQ 362..423
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_007558"
FT VAR_SEQ 424..439
FT /note="PALRPTRPLQTVPLWD -> SWYLG (in isoform 3 and isoform
FT 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_007559"
SQ SEQUENCE 439 AA; 48768 MW; F794131A7A1B686A CRC64;
MYSSPLCLTQ DEFHPFIEAL LPHVRAFAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE
LLGEKAEVKQ KWASRLLAKL RKDIRPECRE DFVLAVTGKK APGCVLSNPD QKGKMRRIDC
LRQADKVWRL DLVMVILFKG IPLESTDGER LVKAAACAHP VLCVQPHHIG VAVKELDLYL
AYFVRERDAE QSSSPRTGVG SDQEDSKPIT LDTTDFQESF VTSGVFSVTE LIQVSRTPVV
TGTGPNFSLG ELQGHLAYDL NPASAGMRRT LPSTSSSGSK RHKSGSMEED VDTSPGGDYY
TSPNSPTSSS RNWTEDIEGG ISSPVKKTEM DKSPFNSPSP QDSPRLSSFT QHHRPVIAVH
SGIARSPHPT SALHFPATPI LPQTASTYFP HTAIRYPPHL NPQDPLKDLV SLACDPATQQ
PGPPALRPTR PLQTVPLWD
