BRF2_DANRE
ID BRF2_DANRE Reviewed; 423 AA.
AC A8KBY2; Q6DC40;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Transcription factor IIIB 50 kDa subunit;
DE AltName: Full=B-related factor 2;
DE Short=BRF-2;
GN Name=brf2; ORFNames=zgc:100856;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) 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. Interacts with TBP and forms a
CC ternary complex with TBp and target DNA sequences.
CC {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; BC078247; AAH78247.1; -; mRNA.
DR EMBL; BC154287; AAI54288.1; -; mRNA.
DR RefSeq; NP_001003536.1; NM_001003536.1.
DR AlphaFoldDB; A8KBY2; -.
DR SMR; A8KBY2; -.
DR STRING; 7955.ENSDARP00000006590; -.
DR PaxDb; A8KBY2; -.
DR GeneID; 445142; -.
DR KEGG; dre:445142; -.
DR CTD; 55290; -.
DR ZFIN; ZDB-GENE-040801-43; brf2.
DR eggNOG; KOG1598; Eukaryota.
DR InParanoid; A8KBY2; -.
DR OrthoDB; 1518547at2759; -.
DR PhylomeDB; A8KBY2; -.
DR Reactome; R-DRE-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR PRO; PR:A8KBY2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; ISS:UniProtKB.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
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:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
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; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 2: Evidence at transcript level;
KW Activator; Metal-binding; Nucleus; Oxidation; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..423
FT /note="Transcription factor IIIB 50 kDa subunit"
FT /id="PRO_0000337191"
FT REPEAT 171..245
FT /note="2"
FT ZN_FING 1..34
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT REGION 325..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT MOD_RES 373
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT CONFLICT 312
FT /note="L -> M (in Ref. 1; AAH78247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48439 MW; B646E7B231C6BA0F CRC64;
MSKNCPECGS SRVVEDDLYS QKQWVCEDCG SVVSEGLLTT TLSEESHSRA VPFFTSTAAF
KKPCRNLVSG FSRLRALCRI FRLSSSMEDA SANLFERAYN HPNFLHISLS KKQILAGCCM
FHICRQNSWP VFMGTIGYLL DADNYQMGTI YQELTKSLNL QTTQVCITRM LESFCYDFKL
APDEVEEVFS VAQQRLVDQT SALLELAADT WILTGRRPFP LFLAAVYVAW QSLNPLARMK
YSLMKFCKIA KAPEQLWCKS KDTINKRLNE LLEVLCKLGR ELPWVRPTDI QMNTVTTLVE
DILKHRKALL ILAVKHYEKQ LEETQTSQYS ESELSDSKSS VQTQCKSPPD EEDEGCELPP
DHWGKRHLFL PPCVRTQKRQ KINEAPLEVT GDEDISDSEI ESYIRSEEEI KLFAKARKKI
CKY
