ARI3A_MOUSE
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 03-AUG-2022, entry version 159.
DE RecName: Full=AT-rich interactive domain-containing protein 3A;
DE Short=ARID domain-containing protein 3A;
DE AltName: Full=B-cell regulator of IgH transcription;
DE Short=Bright;
DE AltName: Full=Dead ringer-like protein 1;
GN Name=Arid3a; Synonyms=Dri1, Dril1;
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], AND FUNCTION.
RX PubMed=8543152; DOI=10.1101/gad.9.24.3067;
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 by
RT Bright: a B cell-specific trans-activator that describes a new DNA-binding
RT 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., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 project:
RT 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., Dou S.;
RT "Expression of bright at two distinct stages of B lymphocyte development.";
RL J. Immunol. 160:4747-4754(1998).
RN [5]
RP INTERACTION WITH BTK.
RX PubMed=11120822; DOI=10.4049/jimmunol.165.12.6956;
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 kinase,
RT 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., Tucker P.W.;
RT "Transcriptional activation by a matrix associating region-binding protein.
RT 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 PRO-268;
RP 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 Bright act
RT as dominant negative proteins and interfere with immunoglobulin
RT 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 function as
RT 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., 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; DOI=10.4049/jimmunol.178.5.2996;
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 that
RT overexpress the transcription factor Bright.";
RL J. Immunol. 178:2996-3006(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-89; SER-127 AND
RP SER-358, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, 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: Transcription factor involved in B-cell differentiation.
CC Binds a VH promoter proximal site necessary for induced mu-heavy-chain
CC transcription. Binds the minor groove of a restricted ATC sequence that
CC is sufficient for nuclear matrix association. This sequence motif is
CC present in matrix-associating regions (MARS) proximal to the promoter
CC and flanking E mu. Activates E mu-driven transcription by binding these
CC sites. May be involved in the control of cell cycle progression by the
CC RB1/E2F1 pathway. {ECO:0000269|PubMed:11294836,
CC ECO:0000269|PubMed:17312145, ECO:0000269|PubMed:8543152}.
CC -!- SUBUNIT: Homodimer. Heterodimer with ARID3B. Interacts with E2F1 (By
CC similarity). Interacts with GTF2I and BTK. {ECO:0000250,
CC ECO:0000269|PubMed:11120822, ECO:0000269|PubMed:15456761,
CC ECO:0000269|PubMed:16738337}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between nucleus
CC and cytoplasm.
CC -!- TISSUE SPECIFICITY: B-cell specific in the adult. Expressed in B-cell
CC progenitors, down-regulated in the immature B-cell stage, and is up-
CC regulated again at later stages of B-lymphocyte differentiation.
CC {ECO:0000269|PubMed:9590220}.
CC -!- DEVELOPMENTAL STAGE: Expressed in lymphocytes from fetal liver.
CC Expressed in fetal thymus and brain. {ECO:0000269|PubMed:9590220}.
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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 CCDS; CCDS23999.1; -.
DR RefSeq; NP_001275554.1; NM_001288625.1.
DR RefSeq; NP_001275555.1; NM_001288626.1.
DR RefSeq; NP_031906.1; NM_007880.4.
DR RefSeq; XP_006513264.1; XM_006513201.3.
DR RefSeq; XP_006513265.1; XM_006513202.3.
DR AlphaFoldDB; Q62431; -.
DR SMR; Q62431; -.
DR BioGRID; 199312; 3.
DR STRING; 10090.ENSMUSP00000019708; -.
DR iPTMnet; Q62431; -.
DR PhosphoSitePlus; Q62431; -.
DR EPD; Q62431; -.
DR MaxQB; Q62431; -.
DR PaxDb; Q62431; -.
DR PeptideAtlas; Q62431; -.
DR PRIDE; Q62431; -.
DR ProteomicsDB; 282018; -.
DR Antibodypedia; 1435; 285 antibodies from 33 providers.
DR DNASU; 13496; -.
DR Ensembl; ENSMUST00000019708; ENSMUSP00000019708; ENSMUSG00000019564.
DR Ensembl; ENSMUST00000105376; ENSMUSP00000101015; ENSMUSG00000019564.
DR GeneID; 13496; -.
DR KEGG; mmu:13496; -.
DR UCSC; uc007gap.2; mouse.
DR CTD; 1820; -.
DR MGI; MGI:1328360; Arid3a.
DR VEuPathDB; HostDB:ENSMUSG00000019564; -.
DR eggNOG; KOG2744; Eukaryota.
DR GeneTree; ENSGT00940000160899; -.
DR HOGENOM; CLU_026952_3_0_1; -.
DR InParanoid; Q62431; -.
DR OMA; MKPKWEE; -.
DR OrthoDB; 1347369at2759; -.
DR PhylomeDB; Q62431; -.
DR TreeFam; TF320364; -.
DR BioGRID-ORCS; 13496; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Arid3a; mouse.
DR PRO; PR:Q62431; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q62431; protein.
DR Bgee; ENSMUSG00000019564; Expressed in granulocyte and 153 other tissues.
DR ExpressionAtlas; Q62431; baseline and differential.
DR Genevisible; Q62431; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR045147; ARI3A/B/C.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR023334; REKLES_domain.
DR PANTHER; PTHR15348; PTHR15348; 1.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51486; REKLES; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..601
FT /note="AT-rich interactive domain-containing protein 3A"
FT /id="PRO_0000200579"
FT DOMAIN 243..335
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 449..546
FT /note="REKLES"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00819"
FT REGION 1..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..165
FT /note="Acidic"
FT REGION 450..493
FT /note="Important for nuclear localization"
FT REGION 495..518
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 542..562
FT /note="Important for cytoplasmic localization"
FT REGION 545..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99856"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99856"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99856"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99856"
FT CROSSLNK 403
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99856"
FT CROSSLNK 404
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99856"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99856"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99856"
FT MUTAGEN 268
FT /note="P->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:15456761"
FT MUTAGEN 299
FT /note="W->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:15456761"
FT MUTAGEN 317
FT /note="F->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:15456761"
FT MUTAGEN 330
FT /note="Y->A: Impairs DNA-binding."
FT /evidence="ECO:0000269|PubMed:15456761"
FT MUTAGEN 457
FT /note="K->A: No effect on cellular location."
FT /evidence="ECO:0000269|PubMed:16507996"
FT MUTAGEN 463
FT /note="P->A: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:16507996"
FT MUTAGEN 466
FT /note="K->A: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:16507996"
FT MUTAGEN 467
FT /note="K->A: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:16507996"
FT MUTAGEN 532
FT /note="G->A: Abolishes cytosolic localization."
FT /evidence="ECO:0000269|PubMed:16507996"
FT MUTAGEN 535
FT /note="Y->A: Abolishes cytosolic localization."
FT /evidence="ECO:0000269|PubMed:16507996"
FT MUTAGEN 535
FT /note="Y->F: No effect on cellular location."
FT /evidence="ECO:0000269|PubMed:16507996"
FT MUTAGEN 537
FT /note="G->A: Abolishes cytosolic localization."
FT /evidence="ECO:0000269|PubMed:16507996"
FT MUTAGEN 539
FT /note="L->A: Abolishes cytosolic localization."
FT /evidence="ECO:0000269|PubMed:16507996"
FT CONFLICT 405..406
FT /note="Missing (in Ref. 3; AAH50925)"
FT /evidence="ECO:0000305"
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
