BRF2_BOVIN
ID BRF2_BOVIN Reviewed; 421 AA.
AC Q29S07; Q5E9M2; Q5E9P4; Q5EAB8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Transcription factor IIIB 50 kDa subunit;
DE AltName: Full=B-related factor 2;
DE Short=BRF-2;
GN Name=BRF2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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, Cys-363 is reversibly oxidized to
CC cysteine sulfenic acid. Oxidation of Cys-363 impairs formation of a
CC ternary complex with TBP and DNA and down-regulates expression of
CC target genes in response to oxidative stress.
CC {ECO:0000250|UniProtKB:Q9HAW0}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
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DR EMBL; BT020651; AAX08668.1; -; mRNA.
DR EMBL; BT020781; AAX08798.1; -; mRNA.
DR EMBL; BT020876; AAX08893.1; -; mRNA.
DR EMBL; BT020884; AAX08901.1; -; mRNA.
DR EMBL; BT020898; AAX08915.1; -; mRNA.
DR EMBL; BC113270; AAI13271.1; -; mRNA.
DR RefSeq; NP_001015582.1; NM_001015582.1.
DR AlphaFoldDB; Q29S07; -.
DR SMR; Q29S07; -.
DR STRING; 9913.ENSBTAP00000039624; -.
DR PaxDb; Q29S07; -.
DR PRIDE; Q29S07; -.
DR Ensembl; ENSBTAT00000039838; ENSBTAP00000039624; ENSBTAG00000027665.
DR GeneID; 512789; -.
DR KEGG; bta:512789; -.
DR CTD; 55290; -.
DR VEuPathDB; HostDB:ENSBTAG00000027665; -.
DR VGNC; VGNC:26563; BRF2.
DR eggNOG; KOG1598; Eukaryota.
DR GeneTree; ENSGT00390000002288; -.
DR HOGENOM; CLU_039947_0_0_1; -.
DR InParanoid; Q29S07; -.
DR OMA; LARFCKM; -.
DR OrthoDB; 1518547at2759; -.
DR TreeFam; TF331596; -.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000027665; Expressed in uterine horn and 106 other tissues.
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 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; Oxidation; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..421
FT /note="Transcription factor IIIB 50 kDa subunit"
FT /id="PRO_0000337186"
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 325..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..365
FT /note="Required for the formation of a ternary complex with
FT DNA and TBP; not required for interaction with TBP in the
FT absence of DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT REGION 367..421
FT /note="Required for interaction with TBP and formation of a
FT ternary complex with DNA and TBP"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
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"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT MOD_RES 363
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:Q9HAW0"
FT CONFLICT 238
FT /note="R -> Q (in Ref. 1; AAX08668/AAX08915)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="G -> A (in Ref. 1; AAX08668/AAX08798/AAX08893/
FT AAX08901/AAX08915)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="P -> A (in Ref. 1; AAX08915)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="V -> G (in Ref. 1; AAX08915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 46591 MW; F81ACF38B8FB1667 CRC64;
MPGRGRCPDC GSAELVEDSH YSQNQLVCSD CGCVVTEGVL TTTFSDEGNL REVTYSRSTG
ENEQVSRSQQ RGLRRVRDLC RVLQLPPTFE DTAVAYYQQA HQLAGIRTAR LQKKEVLAGC
CVLITCRQRN WPLTMGTICT LLYADLDVFS GTYMQIVKLL GLDVPSLCLV DLVKTYCSSF
KLFEASPSVP AKYVEDKEKM LSRTLQLVEL ADETWLVTGR HPLPVITAAT FLAWQSLRPS
DRLTCSLARF CKLANVDLPY PASSRLQELL AVLLRMAEQL AWLQVLKLDK RSVVKHIGDL
LQHRHMLVRK AFRDGTAEMD AGEKELQGQG QGQGLGDEDV GSSSLELPAG KRPSSPALLL
PPCMLKPPKR VCPAPPVSMV TGDEDISDSE IEQYLRTPQE VRDFQKAQAA RQAAQGTPNP
P
