BATF_RAT
ID BATF_RAT Reviewed; 125 AA.
AC D4A7E1;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Basic leucine zipper transcriptional factor ATF-like;
DE AltName: Full=B-cell-activating transcription factor;
DE Short=B-ATF;
GN Name=Batf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: AP-1 family transcription factor that controls the
CC differentiation of lineage-specific cells in the immune system:
CC specifically mediates the differentiation of T-helper 17 cells (Th17),
CC follicular T-helper cells (TfH), CD8(+) dendritic cells and class-
CC switch recombination (CSR) in B-cells. Acts via the formation of a
CC heterodimer with JUNB that recognizes and binds DNA sequence 5'-
CC TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4
CC (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-
CC TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by
CC cooperative binding of BATF and IRF4 (or IRF8) and activation of genes.
CC Controls differentiation of T-helper cells producing interleukin-17
CC (Th17 cells) by binding to Th17-associated gene promoters: regulates
CC expression of the transcription factor RORC itself and RORC target
CC genes such as IL17 (IL17A or IL17B). Also involved in differentiation
CC of follicular T-helper cells (TfH) by directing expression of BCL6 and
CC MAF. In B-cells, involved in class-switch recombination (CSR) by
CC controlling the expression of both AICDA and of germline transcripts of
CC the intervening heavy-chain region and constant heavy-chain region
CC (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic
CC cell differentiation via interaction with IRF4 and IRF8 to mediate
CC cooperative gene activation. Regulates effector CD8(+) T-cell
CC differentiation by regulating expression of SIRT1. Following DNA
CC damage, part of a differentiation checkpoint that limits self-renewal
CC of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to
CC differentiation of HSCs, thereby restricting self-renewal of HSCs (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; mainly heterodimerizes with JUNB. The BATF-JUNB
CC heterodimer interacts with IRF4 and IRF8. Interacts (via bZIP domain)
CC with IRF4 and IRF8; the interaction is direct. Also forms heterodimers
CC with JUN and JUND. Interacts with IFI35 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC Cytoplasm {ECO:0000250}. Note=Present in the nucleus and cytoplasm, but
CC shows increased nuclear translocation after activation of T-cells.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine and threonine residues and at least one
CC tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding
CC activity and transforms it as a negative regulator of AP-1 mediated
CC transcription (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; CH473982; EDL81581.1; -; Genomic_DNA.
DR RefSeq; NP_001100218.1; NM_001106748.1.
DR RefSeq; XP_008762980.1; XM_008764758.2.
DR AlphaFoldDB; D4A7E1; -.
DR SMR; D4A7E1; -.
DR STRING; 10116.ENSRNOP00000011563; -.
DR PaxDb; D4A7E1; -.
DR Ensembl; ENSRNOT00000011563; ENSRNOP00000011563; ENSRNOG00000008588.
DR GeneID; 299206; -.
DR KEGG; rno:299206; -.
DR UCSC; RGD:1304923; rat.
DR CTD; 10538; -.
DR RGD; 1304923; Batf.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000159745; -.
DR HOGENOM; CLU_088612_4_0_1; -.
DR InParanoid; D4A7E1; -.
DR OMA; CTGLTPQ; -.
DR OrthoDB; 1544557at2759; -.
DR PhylomeDB; D4A7E1; -.
DR TreeFam; TF332340; -.
DR PRO; PR:D4A7E1; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000008588; Expressed in thymus and 13 other tissues.
DR Genevisible; D4A7E1; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0042832; P:defense response to protozoan; ISS:UniProtKB.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0045190; P:isotype switching; ISS:UniProtKB.
DR GO; GO:0002320; P:lymphoid progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072539; P:T-helper 17 cell differentiation; ISS:UniProtKB.
DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; ISS:UniProtKB.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR029820; BATF.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF14; PTHR23351:SF14; 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 3: Inferred from homology;
KW Activator; Cytoplasm; Differentiation; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..125
FT /note="Basic leucine zipper transcriptional factor ATF-
FT like"
FT /id="PRO_0000420464"
FT DOMAIN 26..89
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..50
FT /note="Basic motif"
FT REGION 54..75
FT /note="Leucine-zipper"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35284"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35284"
SQ SEQUENCE 125 AA; 14065 MW; A23B00D6E0827938 CRC64;
MPHSSDSSDS SFSRSPPPGK QDSSDDVRKV QRREKNRIAA QKSRQRQTQK ADTLHLESED
LEKQNAALRK EIKQLTEELK YFTSVLSSHE PLCSVLASGT PSPPEVVYSA HAFHQPHISS
PRFQP
