ID ARI3A_MOUSE Reviewed; 601 AA. AC Q62431; Q3U338; Q80YP8; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 10-JUL-2007, entry version 51. DE AT-rich interactive domain-containing protein 3A (ARID domain- DE containing protein 3A) (Dead ringer-like protein 1) (Bright) (B-cell DE regulator of IgH transcription). GN Name=Arid3a; Synonyms=Dri1, Dril1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX MEDLINE=96127903; PubMed=8543152; RA Herrscher R.F., Kaplan M.H., Lelsz D.L., Das C., Scheuermann R., RA Tucker P.W.; RT "The immunoglobulin heavy-chain matrix-associating regions are bound RT by Bright: a B cell-specific trans-activator that describes a new DNA- RT binding protein family."; RL Genes Dev. 9:3067-3082(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; 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 [4] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=9590220; RA Webb C.F., Smith E.A., Medina K.L., Buchanan K.L., Smithson G., RA Dou S.; RT "Expression of bright at two distinct stages of B lymphocyte RT development."; RL J. Immunol. 160:4747-4754(1998). RN [5] RP INTERACTION WITH BTK. RX PubMed=11120822; RA Webb C.F., Yamashita Y., Ayers N., Evetts S., Paulin Y., Conley M.E., RA Smith E.A.; RT "The transcription factor Bright associates with Bruton's tyrosine RT kinase, the defective protein in immunodeficiency disease."; RL J. Immunol. 165:6956-6965(2000). RN [6] RP FUNCTION. RX PubMed=11294836; DOI=10.1074/jbc.M100836200; RA Kaplan M.H., Zong R.-T., Herrscher R.F., Scheuermann R.H., RA Tucker P.W.; RT "Transcriptional activation by a matrix associating region-binding RT protein. contextual requirements for the function of bright."; RL J. Biol. Chem. 276:21325-21330(2001). RN [7] RP DNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP PRO-268; TRP-299; PHE-317 AND TYR-330. RX PubMed=15456761; DOI=10.1074/jbc.M403028200; RA Nixon J.C., Rajaiya J., Webb C.F.; RT "Mutations in the DNA-binding domain of the transcription factor RT Bright act as dominant negative proteins and interfere with RT immunoglobulin transactivation."; RL J. Biol. Chem. 279:52465-52472(2004). RN [8] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-457; PRO-463; LYS-466; RP LYS-467; GLY-532; TYR-535; GLY-537 AND LEU-539. RX PubMed=16507996; DOI=10.1128/MCB.26.6.2187-2201.2006; RA Kim D., Tucker P.W.; RT "A regulated nucleocytoplasmic shuttle contributes to Bright's RT function as a transcriptional activator of immunoglobulin genes."; RL Mol. Cell. Biol. 26:2187-2201(2006). RN [9] RP INTERACTION WITH GTF2I AND BTK. RX PubMed=16738337; DOI=10.1128/MCB.02009-05; RA Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L., RA Webb C.F.; RT "Induction of immunoglobulin heavy-chain transcription through the RT transcription factor Bright requires TFII-I."; RL Mol. Cell. Biol. 26:4758-4768(2006). RN [10] RP FUNCTION. RX PubMed=17312145; RA Shankar M., Nixon J.C., Maier S., Workman J., Farris A.D., Webb C.F.; RT "Anti-nuclear antibody production and autoimmunity in transgenic mice RT that overexpress the transcription factor Bright."; RL J. Immunol. 178:2996-3006(2007). CC -!- FUNCTION: Transcription factor involved in B-cell differentiation. CC Binds a VH promoter proximal site necessary for induced mu-heavy- CC chain transcription. Binds the minor groove of a restricted ATC CC sequence that is sufficient for nuclear matrix association. This CC sequence motif is present in matrix-associating regions (MARS) CC proximal to the promoter and flanking E mu. Activates E mu-driven CC transcription by binding these sites. May be involved in the CC control of cell cycle progression by the RB1/E2F1 pathway. CC -!- SUBUNIT: Homodimer. Heterodimer with ARID3B. Interacts with E2F1 CC (By similarity). Interacts with GTF2I and BTK. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between CC nucleus and cytoplasm. CC -!- TISSUE SPECIFICITY: B-cell specific in the adult. Expressed in B- CC cell progenitors, down-regulated in the immature B-cell stage, and CC is up-regulated again at later stages of B-lymphocyte CC differentiation. CC -!- DEVELOPMENTAL STAGE: Expressed in lymphocytes from fetal liver. CC Expressed in fetal thymus and brain. CC -!- SIMILARITY: Contains 1 ARID domain. CC -!- SIMILARITY: Contains 1 NAP (nucleosome assembly protein) domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U60335; AAB03416.1; -; mRNA. DR EMBL; AK141283; BAE24635.1; -; mRNA. DR EMBL; AK154956; BAE32951.1; -; mRNA. DR EMBL; BC050925; AAH50925.1; -; mRNA. DR UniGene; Mm.301282; -. DR HSSP; Q24573; 1C20. DR SMR; Q62431; 228-354. DR Ensembl; ENSMUSG00000019564; Mus musculus. DR KEGG; mmu:13496; -. DR MGI; MGI:1328360; Arid3a. DR ArrayExpress; Q62431; -. DR GermOnline; ENSMUSG00000019564; Mus musculus. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0042803; F:protein homodimerization activity; IPI:MGI. DR GO; GO:0003700; F:transcription factor activity; IDA:MGI. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA:MGI. DR InterPro; IPR001606; ARID. DR Pfam; PF01388; ARID; 1. DR SMART; SM00501; BRIGHT; 1. DR PROSITE; PS51011; ARID; 1. KW Activator; DNA-binding; Nucleus; Phosphorylation; Transcription; KW Transcription regulation. FT CHAIN 1 601 AT-rich interactive domain-containing FT protein 3A. FT /FTId=PRO_0000200579. FT DOMAIN 131 165 NAP. FT DOMAIN 243 335 ARID. FT REGION 450 493 Important for nuclear localization. FT REGION 495 518 Homodimerization (By similarity). FT REGION 542 562 Important for cytoplasmic localization. FT COMPBIAS 27 34 Poly-Pro. FT COMPBIAS 68 71 Poly-Ala. FT COMPBIAS 128 131 Poly-Asp. FT COMPBIAS 146 154 Poly-Glu. FT COMPBIAS 158 165 Poly-Glu. FT COMPBIAS 437 446 Poly-Ala. FT COMPBIAS 543 546 Poly-Pro. FT MOD_RES 78 78 Phosphoserine (By similarity). FT MOD_RES 82 82 Phosphoserine (By similarity). FT MOD_RES 89 89 Phosphoserine (By similarity). FT MUTAGEN 268 268 P->A: Impairs DNA-binding. FT MUTAGEN 299 299 W->A: Impairs DNA-binding. FT MUTAGEN 317 317 F->A: Impairs DNA-binding. FT MUTAGEN 330 330 Y->A: Impairs DNA-binding. FT MUTAGEN 457 457 K->A: No effect on cellular location. FT MUTAGEN 463 463 P->A: Abolishes nuclear localization. FT MUTAGEN 466 466 K->A: Abolishes nuclear localization. FT MUTAGEN 467 467 K->A: Abolishes nuclear localization. FT MUTAGEN 532 532 G->A: Abolishes cytosolic localization. FT MUTAGEN 535 535 Y->A: Abolishes cytosolic localization. FT MUTAGEN 535 535 Y->F: No effect on cellular location. FT MUTAGEN 537 537 G->A: Abolishes cytosolic localization. FT MUTAGEN 539 539 L->A: Abolishes cytosolic localization. FT CONFLICT 405 406 Missing (in Ref. 3; AAH50925). SQ SEQUENCE 601 AA; 64173 MW; 66994C01E1FB68CD CRC64; MKLQAVMETL IQRQQRARQE LEARQAPPPP PPEPTGVRAR TTMTDEDREP ENARMHRTQM AALAAMRAAA AGLGHPSSPG GSEDGPPISG DEDTAREGTL SSPALHGSVL EGAGHAEGDR HLMDVGSDDD DTKSKWEEQE LEELGEEEEE EEEEDDFEEE EEEEEGLGPP ESASLGTAGL FTRKAPPAQA FRGDGGPRML SGPERLGPGP AHPSHMASQM PPPDHGDWTF EEQFKQLYEL DADPKRKEFL DDLFSFMQKR GTPVNRIPIM AKQVLDLFML YVLVTEKGGL VEVINKKLWR EITKGLNLPT SITSAAFTLR TQYMKYLYPY ECERRGLSSP NELQAAIDSN RREGRRQSFG GSLFAYSPSG AHSMLPSPKL PVTPLGLAAS TNGSSITPAP KIKKEEDSAI PITVPGRLPV SLAGHPVVAA QAAAVQAAAA QAAVAAQAAA LEQLREKLES TEPPEKKMAL VADEQQRLMQ RAVQQSFLAM TAQLPMNIRI NSQASESRQD SAVSLTSANG SNSISMSVEM NGIVYTGVLF AQPPPPTAPS APGKGGVSSI GTNTTTGSRT GASGSTVSGG QVGLPGVSTP TMSSTSNNSL P //