GenomeNet

Database: UniProt
Entry: Q8BX65
LinkDB: Q8BX65
Original site: Q8BX65 
ID   MDFIC_MOUSE             Reviewed;         247 AA.
AC   Q8BX65; Q3T9H3; Q6NXM1; Q8BJS3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   13-FEB-2019, entry version 120.
DE   RecName: Full=MyoD family inhibitor domain-containing protein;
DE   AltName: Full=I-mfa domain-containing protein;
DE   AltName: Full=Kidney cell line-derived transcript 1;
GN   Name=Mdfic {ECO:0000312|MGI:MGI:104611};
GN   Synonyms=Kdt1 {ECO:0000312|MGI:MGI:104611};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Aorta, Cerebellum, Eye, Spleen, and Vein;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAH67006.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH67006.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH67006.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, INTERACTION WITH ZIC2, AND SUBCELLULAR LOCATION.
RX   PubMed=15207726; DOI=10.1016/j.bbrc.2004.05.158;
RA   Mizugishi K., Hatayama M., Tohmonda T., Ogawa M., Inoue T.,
RA   Mikoshiba K., Aruga J.;
RT   "Myogenic repressor I-mfa interferes with the function of Zic family
RT   proteins.";
RL   Biochem. Biophys. Res. Commun. 320:233-240(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH ZIC2, AND SUBCELLULAR LOCATION.
RX   PubMed=15465018; DOI=10.1016/j.bbrc.2004.09.052;
RA   Ishiguro A., Inoue T., Mikoshiba K., Aruga J.;
RT   "Molecular properties of Zic4 and Zic5 proteins: functional diversity
RT   within Zic family.";
RL   Biochem. Biophys. Res. Commun. 324:302-307(2004).
RN   [5]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH HAND1.
RX   PubMed=17891141; DOI=10.1038/ncb1633;
RA   Martindill D.M.J., Risebro C.A., Smart N., Franco-Viseras Mdel M.,
RA   Rosario C.O., Swallow C.J., Dennis J.W., Riley P.R.;
RT   "Nucleolar release of Hand1 acts as a molecular switch to determine
RT   cell fate.";
RL   Nat. Cell Biol. 9:1131-1141(2007).
CC   -!- FUNCTION: Acts as a transcriptional activator or repressor.
CC       Inhibits the transcriptional activation of Zic family proteins
CC       ZIC1, ZIC2 and ZIC3. Retains nuclear Zic proteins ZIC1, ZIC2 and
CC       ZIC3 in the cytoplasm. Modulates the expression from cellular
CC       promoters. Binds to the axin complex, resulting in an increase in
CC       the level of free beta-catenin. Affects axin-regulation of the WNT
CC       and JNK signaling pathways. {ECO:0000269|PubMed:15207726,
CC       ECO:0000269|PubMed:15465018}.
CC   -!- SUBUNIT: Interacts with HAND1; leading to sequester HAND1 into the
CC       nucleolus and prevent its activity (PubMed:17891141). Interacts
CC       with ZIC2 (PubMed:15207726, PubMed:15465018). The C-terminus
CC       interacts with AXIN1, the histidine-rich region of CCNT1/cyclin-T
CC       and weakly with LEF1. Interacts with CCNT2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9P1T7, ECO:0000269|PubMed:15207726,
CC       ECO:0000269|PubMed:15465018, ECO:0000269|PubMed:17891141}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, nucleolus
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC         IsoId=Q8BX65-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:16141072};
CC         IsoId=Q8BX65-2; Sequence=VSP_052336, VSP_052337;
CC         Note=No experimental confirmation available. {ECO:0000305};
CC   -!- DOMAIN: The cysteine-rich C-terminus is involved in its granular
CC       distribution in the cytoplasm (By similarity). The C2H2-type 3, 4
CC       and 5 zinc finger domains are necessary for transcription
CC       activation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MDFI family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH67006.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=BAC37840.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=BAE43047.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AK048821; BAC33469.1; -; mRNA.
DR   EMBL; AK080178; BAC37840.1; ALT_INIT; mRNA.
DR   EMBL; AK165016; BAE38001.1; -; mRNA.
DR   EMBL; AK172522; BAE43047.1; ALT_INIT; mRNA.
DR   EMBL; BC067006; AAH67006.1; ALT_INIT; mRNA.
DR   CCDS; CCDS19919.1; -. [Q8BX65-1]
DR   RefSeq; NP_780297.3; NM_175088.5. [Q8BX65-1]
DR   UniGene; Mm.1314; -.
DR   ProteinModelPortal; Q8BX65; -.
DR   SMR; Q8BX65; -.
DR   IntAct; Q8BX65; 1.
DR   STRING; 10090.ENSMUSP00000099186; -.
DR   iPTMnet; Q8BX65; -.
DR   PhosphoSitePlus; Q8BX65; -.
DR   SwissPalm; Q8BX65; -.
DR   jPOST; Q8BX65; -.
DR   PaxDb; Q8BX65; -.
DR   PRIDE; Q8BX65; -.
DR   DNASU; 16543; -.
DR   Ensembl; ENSMUST00000101663; ENSMUSP00000099186; ENSMUSG00000041390. [Q8BX65-1]
DR   Ensembl; ENSMUST00000120512; ENSMUSP00000113050; ENSMUSG00000041390. [Q8BX65-1]
DR   Ensembl; ENSMUST00000189359; ENSMUSP00000140208; ENSMUSG00000041390. [Q8BX65-1]
DR   GeneID; 16543; -.
DR   KEGG; mmu:16543; -.
DR   UCSC; uc009azc.2; mouse. [Q8BX65-1]
DR   UCSC; uc012eif.1; mouse. [Q8BX65-2]
DR   CTD; 29969; -.
DR   MGI; MGI:104611; Mdfic.
DR   eggNOG; ENOG410IKRS; Eukaryota.
DR   eggNOG; ENOG4111J6Q; LUCA.
DR   GeneTree; ENSGT00940000158685; -.
DR   HOGENOM; HOG000001577; -.
DR   HOVERGEN; HBG068212; -.
DR   InParanoid; Q8BX65; -.
DR   OrthoDB; 1487193at2759; -.
DR   PhylomeDB; Q8BX65; -.
DR   TreeFam; TF332113; -.
DR   PRO; PR:Q8BX65; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000041390; Expressed in 244 organ(s), highest expression level in female gonad.
DR   ExpressionAtlas; Q8BX65; baseline and differential.
DR   Genevisible; Q8BX65; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030332; F:cyclin binding; ISS:UniProtKB.
DR   GO; GO:0030957; F:Tat protein binding; ISS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0007257; P:activation of JUN kinase activity; ISO:MGI.
DR   GO; GO:0042308; P:negative regulation of protein import into nucleus; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0050434; P:positive regulation of viral transcription; ISS:UniProtKB.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; ISO:MGI.
DR   InterPro; IPR026134; MDFI/MDFIC.
DR   PANTHER; PTHR15304; PTHR15304; 1.
DR   Pfam; PF15316; MDFI; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome; Cytoplasm;
KW   Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    247       MyoD family inhibitor domain-containing
FT                                protein.
FT                                /FTId=PRO_0000280223.
FT   DOMAIN       74    247       MDFI.
FT   COMPBIAS    167    244       Cys-rich. {ECO:0000255}.
FT   MOD_RES     129    129       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1T7}.
FT   MOD_RES     141    141       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1T7}.
FT   VAR_SEQ      32     72       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_052336.
FT   VAR_SEQ      73     73       T -> A (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_052337.
SQ   SEQUENCE   247 AA;  26094 MW;  B4FBA7F07565E3B2 CRC64;
     MSCAGEALAP GPAEQQCPVE AGGGRLGSPA HEACNEDNTE KDKRPATSGH TRCGLMRDQS
     IWPNPSAGEL VRTQPERLPQ LQTSAQEPGK EETGKIKNGG HTRMSNGNGI PHGAKHVSVE
     NHKISAPVSQ KMHRKIQSSL SVNNDISKKS KVNAVFSPKA ASSPEDCCVH CILACLFCEF
     LTLCNIVLGQ ASCGICTSEA CCCCCGDEMG DDCSCPCDMD CGIMDACCES SDCLEICMEC
     CGICFPS
//
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