TAF4_CAEEL
ID TAF4_CAEEL Reviewed; 523 AA.
AC O61707;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transcription initiation factor TFIID subunit 4 {ECO:0000305};
DE AltName: Full=TBP-associated transcription factor family member taf-4 {ECO:0000312|WormBase:R119.6};
GN Name=taf-4 {ECO:0000312|WormBase:R119.6};
GN Synonyms=taf-5 {ECO:0000303|PubMed:11566890};
GN ORFNames=R119.6 {ECO:0000312|WormBase:R119.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11566890; DOI=10.1093/emboj/20.18.5269;
RA Walker A.K., Rothman J.H., Shi Y., Blackwell T.K.;
RT "Distinct requirements for C.elegans TAF(II)s in early embryonic
RT transcription.";
RL EMBO J. 20:5269-5279(2001).
RN [3]
RP NOMENCLATURE.
RX PubMed=11963920; DOI=10.1101/gad.976402;
RA Tora L.;
RT "A unified nomenclature for TATA box binding protein (TBP)-associated
RT factors (TAFs) involved in RNA polymerase II transcription.";
RL Genes Dev. 16:673-675(2002).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH OMA-1 AND TAF-12, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RX PubMed=18854162; DOI=10.1016/j.cell.2008.07.040;
RA Guven-Ozkan T., Nishi Y., Robertson S.M., Lin R.;
RT "Global transcriptional repression in C. elegans germline precursors by
RT regulated sequestration of TAF-4.";
RL Cell 135:149-160(2008).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24107417; DOI=10.18632/aging.100604;
RA Khan M.H., Ligon M., Hussey L.R., Hufnal B., Farber R. II, Munkacsy E.,
RA Rodriguez A., Dillow A., Kahlig E., Rea S.L.;
RT "TAF-4 is required for the life extension of isp-1, clk-1 and tpk-1 Mit
RT mutants.";
RL Aging (Albany NY) 5:741-758(2013).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30198021; DOI=10.26508/lsa.201800082;
RA Molenaars M., Janssens G.E., Santermans T., Lezzerini M., Jelier R.,
RA MacInnes A.W., Houtkooper R.H.;
RT "Mitochondrial ubiquinone-mediated longevity is marked by reduced
RT cytoplasmic mRNA translation.";
RL Life. Sci Alliance 1:0-0(2018).
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 (By similarity). TFIID recognizes and binds promoters via
CC its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of
CC the pre-initiation complex (PIC) (By similarity). The TFIID complex
CC consists of tbp-1 and TBP-associated factors (TAFs), including taf-4
CC (By similarity). Essential for early embryonic development, probably
CC acting via activating transcription initiation by RNA polymerase II, as
CC part of the TFIID complex (PubMed:18854162, PubMed:11566890). In early
CC embryos, but not oocytes, remains, presumably inactive, in the
CC cytoplasm as a result of binding to oma-1 (PubMed:18854162). Upon
CC degradation of oma-1, taf-4 is released and bound by taf-12, and the
CC taf-4/12 heterodimer translocates to the nucleus and transcriptional
CC repression is relieved (PubMed:18854162). Involved in lifespan
CC extension in a manner dependent upon mitochondrial function
CC (PubMed:24107417). Plays a role in modulating polyribosome formation
CC (PubMed:30198021). {ECO:0000250|UniProtKB:O00268,
CC ECO:0000269|PubMed:11566890, ECO:0000269|PubMed:18854162,
CC ECO:0000269|PubMed:24107417, ECO:0000269|PubMed:30198021}.
CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC composed of TATA-box-binding protein tbp-1, and a number of TBP-
CC associated factors (TAFs) (By similarity). Interacts (via histone-fold
CC domain) with oma-1 (via histone-fold domain) (PubMed:18854162). May
CC also interact with oma-2 (PubMed:18854162). Interacts (via histone-fold
CC domain) with taf-12 (via the histone-fold domain) (PubMed:18854162).
CC {ECO:0000250|UniProtKB:O00268, ECO:0000269|PubMed:18854162}.
CC -!- INTERACTION:
CC O61707; G5EC86: oma-1; NbExp=5; IntAct=EBI-2023840, EBI-327483;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440,
CC ECO:0000269|PubMed:11566890, ECO:0000269|PubMed:18854162}. Cytoplasm
CC {ECO:0000269|PubMed:18854162}. Note=Localization is ubiquitous in one-
CC cell and early two-cell embryos, then enriched in nucleus in all
CC subsequent embryo stages (PubMed:18854162). Localization to the nucleus
CC is prevented by interaction with oma-1 and is sequestered in the
CC cytoplasm, following fertilization, and thus allows for transcriptional
CC suppression in early embryos, but not in oocytes (PubMed:18854162).
CC Localized to the nucleus in a taf-12-dependent manner
CC (PubMed:18854162). {ECO:0000269|PubMed:18854162}.
CC -!- DEVELOPMENTAL STAGE: Expressed in one-, two- and four-cell embryos and
CC through early morphogenesis (at protein level) (PubMed:11566890,
CC PubMed:18854162). Also expressed in oocytes, and until at least 12-cell
CC stage in embryos (PubMed:18854162). {ECO:0000269|PubMed:11566890,
CC ECO:0000269|PubMed:18854162}.
CC -!- DOMAIN: The histone-fold domain mediates hetero-dimer protein-protein
CC interactions. {ECO:0000269|PubMed:18854162}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes arrested
CC development at 90-100 cells and inhibits differentiation
CC (PubMed:11566890). The two E cell daughters (E2 cells), which form the
CC endoderm, divide abnormally early, immediately after the MS2 cells
CC (PubMed:11566890). Phosphorylation of the RNA Pol II large subunit C-
CC terminal domain (CTD) is reduced severely in embryos (PubMed:11566890).
CC Abolishes expression of a range of genes, including let-858, rps-5,
CC hsp16.2, pes-10, cki-2 and sur-5 (PubMed:11566890). RNAi-mediated
CC knockdown in a Rieske iron-sulfur protein isp-1 mutant background
CC abolishes lifespan extension, drastically reduces fertility, and
CC abolishes induction of expression of glutathione S-transferase gst-4
CC (PubMed:24107417). Knockdown also significantly shortens lifespan in
CC either tpk-1 or clk-1 mutant backgrounds (PubMed:24107417). Causes
CC significant up-regulation of expression of the translation initiation
CC factor eif-1, in a clk-1 mutant background (PubMed:30198021).
CC {ECO:0000269|PubMed:11566890, ECO:0000269|PubMed:24107417,
CC ECO:0000269|PubMed:30198021}.
CC -!- SIMILARITY: Belongs to the TAF4 family. {ECO:0000305}.
CC -!- CAUTION: Throughout PMID:11566890, the gene name taf-5 is used instead
CC of taf-4, based on an earlier nomenclature; readers should be aware to
CC avoid confusion. {ECO:0000303|PubMed:11963920,
CC ECO:0000305|PubMed:11566890}.
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DR EMBL; BX284601; CCD73344.1; -; Genomic_DNA.
DR PIR; C87719; C87719.
DR RefSeq; NP_490728.2; NM_058327.5.
DR AlphaFoldDB; O61707; -.
DR SMR; O61707; -.
DR IntAct; O61707; 3.
DR STRING; 6239.R119.6; -.
DR EPD; O61707; -.
DR PaxDb; O61707; -.
DR PeptideAtlas; O61707; -.
DR EnsemblMetazoa; R119.6.1; R119.6.1; WBGene00006385.
DR GeneID; 171630; -.
DR KEGG; cel:CELE_R119.6; -.
DR UCSC; R119.6; c. elegans.
DR CTD; 171630; -.
DR WormBase; R119.6; CE39613; WBGene00006385; taf-4.
DR eggNOG; KOG2341; Eukaryota.
DR GeneTree; ENSGT00390000011620; -.
DR HOGENOM; CLU_520970_0_0_1; -.
DR InParanoid; O61707; -.
DR OMA; RITQCMN; -.
DR OrthoDB; 1272649at2759; -.
DR Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-CEL-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-CEL-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-CEL-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-CEL-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006385; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IMP:WormBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IMP:WormBase.
DR CDD; cd08045; TAF4; 1.
DR Gene3D; 1.20.120.1110; -; 1.
DR InterPro; IPR045144; TAF4.
DR InterPro; IPR007900; TAF4_C.
DR InterPro; IPR037249; TAFH/NHR1_dom_sf.
DR InterPro; IPR003894; TAFH_NHR1.
DR PANTHER; PTHR15138; PTHR15138; 2.
DR Pfam; PF05236; TAF4; 1.
DR Pfam; PF07531; TAFH; 1.
DR SMART; SM00549; TAFH; 1.
DR SUPFAM; SSF158553; SSF158553; 1.
DR PROSITE; PS51119; TAFH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..523
FT /note="Transcription initiation factor TFIID subunit 4"
FT /id="PRO_0000454929"
FT DOMAIN 101..199
FT /note="TAFH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..383
FT /note="Histone-fold"
FT /evidence="ECO:0000303|PubMed:18854162"
FT REGION 333..382
FT /note="Necessary and sufficient for interaction with oma-1"
FT /evidence="ECO:0000269|PubMed:18854162"
FT REGION 407..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 57731 MW; A1AEB0E84AEE3ADA CRC64;
MSLPRFRLVQ GKAIGERSTP GVSTPEPAPP QIKQEVDYQD AHQMAPEPVE APQAQNHQMQ
PPRQPIQQQM QHFQSPSPMA PQGPPGTPQN SAAAAAAASD DKNVTKCVRF LKTLINLSNN
DDPEMPDKAA RVKELIRGVI YLETTAEEFT RNLQQVLKSQ AQPHLLPFLQ NTLPALRNAV
RNGTASVEGV NPPPGYVFNN GRTPGPPQPP PPQQQSQQQP PLEMRQIPNP NQIPPQMVQG
GPHMVSVGAR PMIRPMGPGG PSPMGLQGPV RGPMGHQMVQ MHPPPPPQQI QQQHPAPPVE
MEVEENLQPT AAATATRQYP EGSLKSSILK PDEVLNRITK RMMSSCSVEE EALVAISDAV
ESHLRELITL MAGVAEHRVE SLRIPENYVA IDDVKRQLRF LEDLDRQEEE LRESREKESL
IRMSKNKNSG KETIEKAKEM QRQDAEAKRN RDANAAAIAA LSSNKTVKNK WENTGAATTA
PRPRTVRVTT RDLHLLVNQD SRFTGTFIRE KMSYGGPAVD TTI
