BATF3_MOUSE
ID BATF3_MOUSE Reviewed; 118 AA.
AC Q9D275;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Basic leucine zipper transcriptional factor ATF-like 3;
DE Short=B-ATF-3;
GN Name=Batf3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19008445; DOI=10.1126/science.1164206;
RA Hildner K., Edelson B.T., Purtha W.E., Diamond M., Matsushita H.,
RA Kohyama M., Calderon B., Schraml B.U., Unanue E.R., Diamond M.S.,
RA Schreiber R.D., Murphy T.L., Murphy K.M.;
RT "Batf3 deficiency reveals a critical role for CD8alpha+ dendritic cells in
RT cytotoxic T cell immunity.";
RL Science 322:1097-1100(2008).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20351058; DOI=10.1084/jem.20091627;
RA Edelson B.T., Kc W., Juang R., Kohyama M., Benoit L.A., Klekotka P.A.,
RA Moon C., Albring J.C., Ise W., Michael D.G., Bhattacharya D.,
RA Stappenbeck T.S., Holtzman M.J., Sung S.S., Murphy T.L., Hildner K.,
RA Murphy K.M.;
RT "Peripheral CD103+ dendritic cells form a unified subset developmentally
RT related to CD8alpha+ conventional dendritic cells.";
RL J. Exp. Med. 207:823-836(2010).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=21867927; DOI=10.1016/j.immuni.2011.06.012;
RA Edelson B.T., Bradstreet T.R., Hildner K., Carrero J.A., Frederick K.E.,
RA Kc W., Belizaire R., Aoshi T., Schreiber R.D., Miller M.J., Murphy T.L.,
RA Unanue E.R., Murphy K.M.;
RT "CD8alpha(+) dendritic cells are an obligate cellular entry point for
RT productive infection by Listeria monocytogenes.";
RL Immunity 35:236-248(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21867928; DOI=10.1016/j.immuni.2011.08.008;
RA Mashayekhi M., Sandau M.M., Dunay I.R., Frickel E.M., Khan A.,
RA Goldszmid R.S., Sher A., Ploegh H.L., Murphy T.L., Sibley L.D.,
RA Murphy K.M.;
RT "CD8alpha(+) dendritic cells are the critical source of interleukin-12 that
RT controls acute infection by Toxoplasma gondii tachyzoites.";
RL Immunity 35:249-259(2011).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=22992524; DOI=10.1038/nature11531;
RA Tussiwand R., Lee W.L., Murphy T.L., Mashayekhi M., Kc W., Albring J.C.,
RA Satpathy A.T., Rotondo J.A., Edelson B.T., Kretzer N.M., Wu X., Weiss L.A.,
RA Glasmacher E., Li P., Liao W., Behnke M., Lam S.S., Aurthur C.T.,
RA Leonard W.J., Singh H., Stallings C.L., Sibley L.D., Schreiber R.D.,
RA Murphy K.M.;
RT "Compensatory dendritic cell development mediated by BATF-IRF
RT interactions.";
RL Nature 490:502-507(2012).
CC -!- FUNCTION: AP-1 family transcription factor that controls the
CC differentiation of CD8(+) thymic conventional dendritic cells in the
CC immune system. Acts via the formation of a heterodimer with JUN family
CC proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and
CC regulates expression of target genes. Required for development of CD8-
CC alpha(+) classical dendritic cells (cDCs) and related CD103(+)
CC dendritic cells that cross-present antigens to CD8 T-cells and produce
CC interleukin-12 (IL12) in response to pathogens.
CC {ECO:0000269|PubMed:19008445, ECO:0000269|PubMed:20351058,
CC ECO:0000269|PubMed:21867928}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with JUN family proteins.
CC Interacts with JUN.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- TISSUE SPECIFICITY: Highly expressed in CD8-alpha(+) classical
CC dendritic cells (cDCs), with low to absent expression in other immune
CC cells and non-immune tissues. {ECO:0000269|PubMed:19008445}.
CC -!- DISRUPTION PHENOTYPE: Selective loss of CD8-alpha(+) classical
CC dendritic cells (cDCs) and CD103(+) dendritic cells, without
CC abnormalities in other hematopoietic cell types or architecture.
CC Dendritic cells are defective in cross-presentation, and mice lack
CC virus-specific CD8(+) T-cell responses to West Nile virus. Mice also
CC show reduced priming of CD8 T-cells after pulmonary Sendai virus
CC infection, with increased pulmonary inflammation. Mice are extremely
CC susceptible to T.gondii infection, with decreased production of
CC interleukin-12 (IL12) and interferon-gamma. In contrast, mice are more
CC resistant to L.monocytogenes infection. {ECO:0000269|PubMed:19008445,
CC ECO:0000269|PubMed:20351058, ECO:0000269|PubMed:21867927,
CC ECO:0000269|PubMed:21867928, ECO:0000269|PubMed:22992524}.
CC -!- MISCELLANEOUS: The increased protection toward L.monocytogenes
CC infection in mice lacking Batf3 suggests that CD8-alpha(+) classical
CC dendritic cells (cDCs) and CD103(+) dendritic cells are an entry point
CC for infection by L.monocytogenes. {ECO:0000305|PubMed:21867927}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AK020278; BAB32053.1; -; mRNA.
DR EMBL; BC117083; AAI17084.1; -; mRNA.
DR EMBL; BC117085; AAI17086.1; -; mRNA.
DR CCDS; CCDS15615.1; -.
DR RefSeq; NP_084336.1; NM_030060.2.
DR AlphaFoldDB; Q9D275; -.
DR SMR; Q9D275; -.
DR BioGRID; 237877; 13.
DR IntAct; Q9D275; 13.
DR STRING; 10090.ENSMUSP00000027943; -.
DR iPTMnet; Q9D275; -.
DR PhosphoSitePlus; Q9D275; -.
DR EPD; Q9D275; -.
DR MaxQB; Q9D275; -.
DR PaxDb; Q9D275; -.
DR PRIDE; Q9D275; -.
DR ProteomicsDB; 273729; -.
DR Antibodypedia; 34609; 150 antibodies from 22 providers.
DR DNASU; 381319; -.
DR Ensembl; ENSMUST00000027943; ENSMUSP00000027943; ENSMUSG00000026630.
DR GeneID; 381319; -.
DR KEGG; mmu:381319; -.
DR UCSC; uc007ecd.1; mouse.
DR CTD; 55509; -.
DR MGI; MGI:1925491; Batf3.
DR VEuPathDB; HostDB:ENSMUSG00000026630; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000161120; -.
DR HOGENOM; CLU_088612_1_1_1; -.
DR InParanoid; Q9D275; -.
DR OMA; TMNFVTI; -.
DR OrthoDB; 1440552at2759; -.
DR PhylomeDB; Q9D275; -.
DR TreeFam; TF332340; -.
DR BioGRID-ORCS; 381319; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Batf3; mouse.
DR PRO; PR:Q9D275; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D275; protein.
DR Bgee; ENSMUSG00000026630; Expressed in placenta labyrinth and 119 other tissues.
DR Genevisible; Q9D275; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; 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:0097028; P:dendritic cell differentiation; IMP:UniProtKB.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029818; p21SNFT.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF13; PTHR23351:SF13; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 2: Evidence at transcript level;
KW Activator; Differentiation; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..118
FT /note="Basic leucine zipper transcriptional factor ATF-like
FT 3"
FT /id="PRO_0000326107"
FT DOMAIN 28..91
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..55
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 56..84
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR55"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR55"
SQ SEQUENCE 118 AA; 13657 MW; 67EA973561ECCFA1 CRC64;
MSQGPPAVSV LQRSVDAPGN QPQSPKDDDR KVRRREKNRV AAQRSRKKQT QKADKLHEEH
ESLEQENSVL RREISKLKEE LRHLSEVLKE HEKMCPLLLC PMNFVQLRSD PVASCLPR
