BRF2_MACFA
ID BRF2_MACFA Reviewed; 373 AA.
AC Q4R318;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Transcription factor IIIB 50 kDa subunit;
DE AltName: Full=B-related factor 2;
DE Short=BRF-2;
GN Name=BRF2; ORFNames=QtsA-20293;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: General activator of RNA polymerase III transcription. Factor
CC exclusively required for RNA polymerase III transcription of genes with
CC promoter elements upstream of the initiation sites. Contributes to the
CC regulation of gene expression; functions as activator in the absence of
CC oxidative stress. Down-regulates expression of target genes in response
CC to oxidative stress. Overexpression protects cells against apoptosis in
CC response to oxidative stress. {ECO:0000250|UniProtKB:Q9HAW0}.
CC -!- SUBUNIT: Component of TFIIIB complexes. The TFIIIB complex has two
CC activities, alpha and beta. The TFIIIB-alpha activity complex is
CC composed of TBP, BDP1, and a complex containing both BRF2 and at least
CC four stably associated proteins; this complex inhibits the
CC transcription by pol III via its phosphorylation by CK2; YY1
CC facilitates the TFIIIB-alpha complex formation. Interacts with TBP;
CC this interaction promotes recruitment of BRF2 to TATA box-containing
CC promoters. Interacts with TBP and the BURE sequence (GC-rich sequence
CC downstream from the TATA box) to form a strong ternary complex which is
CC joined by BDP1; this ternary complex stimulates pol III transcription.
CC Forms a trimeric complex composed of TBP, BRF2 and mini-SNAPc complex
CC (SNAP43, SNAP50, and the N-terminal third of SNAP190) on the promoter.
CC Assembly of the TBP-BRF2 complex is stimulated by SNAP190. Interacts
CC with MAF1 and SNAPC4. {ECO:0000250|UniProtKB:Q9HAW0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAW0}.
CC -!- PTM: In response to oxidative stress, a Cys-residue is reversibly
CC oxidized to cysteine sulfenic acid. This impairs formation of a ternary
CC complex with TBP and DNA and down-regulates expression of target genes
CC in response to oxidative stress. {ECO:0000250|UniProtKB:Q9HAW0}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
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DR EMBL; AB179450; BAE02501.1; -; mRNA.
DR RefSeq; NP_001271051.1; NM_001284122.1.
DR AlphaFoldDB; Q4R318; -.
DR SMR; Q4R318; -.
DR GeneID; 101867145; -.
DR CTD; 55290; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618; PTHR11618; 2.
DR Pfam; PF08271; TF_Zn_Ribbon; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 2: Evidence at transcript level;
KW Activator; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..373
FT /note="Transcription factor IIIB 50 kDa subunit"
FT /id="PRO_0000337188"
FT REPEAT 72..157
FT /note="1"
FT REPEAT 173..249
FT /note="2"
FT ZN_FING 2..36
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT REGION 108..114
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT REGION 318..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ SEQUENCE 373 AA; 41818 MW; 5EBE818F2E431E2D CRC64;
MPGRGRCPDC GSTELVEDSH YSQSQLVCSD CGCVVTEGVL TTTFSDEGNL REVTYSRSTG
ENEQISRSQQ RGLRRVRDLC RVLQLPPTFE DTAVAYYQQA YRHSGIRAAR LQKKEVLVGC
CVLITCRQHN WPLTMGAICT LLYADLDVFS SIYMQIVKLL GLDMPSLCLA ELVKTYCSSF
KLFQASPSVP AKYVEDKEKM LSRTLQLVEL ANETWLVTGR HPLPVITAAT FLAWQSLQPA
DRLSCSLARF CKLANVDLPY PASSRLQELL AVLLRMAEQL AWLRVLRLDK RSVVKHIGDL
LQHRHSLVRL AFRDGTAEVE TRGKEPPPVS TVTGDENISD SEIEQYLRTP QEVRDFQRAQ
AARQAATSVP NPP
