TAF8_BOVIN
ID TAF8_BOVIN Reviewed; 310 AA.
AC A7MAZ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Transcription initiation factor TFIID subunit 8;
DE AltName: Full=TBP-associated factor 8;
GN Name=TAF8;
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].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC role in the initiation of RNA polymerase II (Pol II)-dependent
CC transcription. TFIID recognizes and binds promoters with or without a
CC TATA box via its subunit TBP, a TATA-box-binding protein, and promotes
CC assembly of the pre-initiation complex (PIC). The TFIID complex
CC consists of TBP and TBP-associated factors (TAFs), including TAF1,
CC TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and
CC TAF13. The TFIID complex structure can be divided into 3 modules TFIID-
CC A, TFIID-B, and TFIID-C. TAF8 is involved in forming the TFIID-B
CC module, together with TAF5. Mediates both basal and activator-dependent
CC transcription. Plays a role in the differentiation of preadipocyte
CC fibroblasts to adipocytes, however, does not seem to play a role in
CC differentiation of myoblasts. Required for the integration of TAF10 in
CC the TAF complex (By similarity). May be important for survival of cells
CC of the inner cell mass which constitute the pluripotent cell population
CC of the early embryo (By similarity). {ECO:0000250|UniProtKB:Q7Z7C8,
CC ECO:0000250|UniProtKB:Q9EQH4}.
CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC composed of TATA-box-binding protein TBP, and a number of TBP-
CC associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5,
CC TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Interacts with
CC TBP, TAF1, TAF6, TAF10, TAF11 and TAF13. Component also of a small TAF
CC complex (SMAT) containing TAF8, TAF10 and SUPT7L. Forms a heterodimer
CC with TAF10. Interaction with TAF10 is mediated mainly via its histone
CC fold domain while interaction with SUPT7L is via its C-terminal region.
CC {ECO:0000250|UniProtKB:Q7Z7C8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Localized in the cytoplasm and transported from the cytoplasm to
CC the nucleus in some cells, possibly depending on the functional or
CC developmental state of the cell. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TAF8 family. {ECO:0000305}.
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DR EMBL; BC151255; AAI51256.1; -; mRNA.
DR RefSeq; NP_001094670.1; NM_001101200.2.
DR AlphaFoldDB; A7MAZ4; -.
DR SMR; A7MAZ4; -.
DR STRING; 9913.ENSBTAP00000035931; -.
DR PaxDb; A7MAZ4; -.
DR Ensembl; ENSBTAT00000036067; ENSBTAP00000035931; ENSBTAG00000011339.
DR GeneID; 539938; -.
DR KEGG; bta:539938; -.
DR CTD; 129685; -.
DR VEuPathDB; HostDB:ENSBTAG00000011339; -.
DR VGNC; VGNC:35581; TAF8.
DR eggNOG; KOG4336; Eukaryota.
DR GeneTree; ENSGT00390000017567; -.
DR HOGENOM; CLU_070829_0_0_1; -.
DR InParanoid; A7MAZ4; -.
DR OMA; SAHNYCE; -.
DR OrthoDB; 1290064at2759; -.
DR TreeFam; TF316311; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000011339; Expressed in abomasum and 106 other tissues.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001112; P:DNA-templated transcription open complex formation; IEA:Ensembl.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IEA:Ensembl.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd08049; TAF8; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037818; TAF8.
DR InterPro; IPR019473; TFIID_su8_C.
DR PANTHER; PTHR46469; PTHR46469; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF10406; TAF8_C; 1.
DR SMART; SM00576; BTP; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Developmental protein; Differentiation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7C8"
FT CHAIN 2..310
FT /note="Transcription initiation factor TFIID subunit 8"
FT /id="PRO_0000315397"
FT DOMAIN 35..102
FT /note="Histone-fold"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 294..307
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7C8"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7C8"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7C8"
SQ SEQUENCE 310 AA; 34227 MW; 834FF443A8089D28 CRC64;
MADAAATAGA AGSGTRSGSK QSTNPADNYH LARRRTLQVV VSSLLTEAGF ESAEKASVET
LTEMLQSYIS EIGRSAKSYC EHTARTQPTL SDIVVTLVEM GFNVDTLPAY AKRSQRMVIT
APPVTNQPVT PKALTAGQNR PHPPHIPSHF PEFPDPHTYI KTPTYREPVS DYQVLREKAA
SQRRDVERAL TRFMAKTGET QSLFKDDVST FPLIAARPFT IPYLTALLPS ELEMQQMEET
DSSEQDEQTD TENLPLHISP DDSGAEKENT SVLQQNPSLS GSRNGEESII DNPYLRPVKK
PKIRRKKSLS
