TAF12_CAEEL
ID TAF12_CAEEL Reviewed; 342 AA.
AC Q9U226; C0Z3M2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Transcription initiation factor TFIID subunit 12 {ECO:0000305};
GN Name=taf-12 {ECO:0000312|WormBase:Y56A3A.4a};
GN ORFNames=Y56A3A.4 {ECO:0000312|WormBase:Y56A3A.4a};
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] {ECO:0000305}
RP INTERACTION WITH TAF-4, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
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).
CC -!- FUNCTION: Part of the general transcription factor complex TFIID (By
CC similarity). Plays a role in recruiting taf-4 to the nucleus and
CC thereby activating transcription initiation by RNA polymerase II, as
CC part of the TFIID complex (PubMed:18854162).
CC {ECO:0000250|UniProtKB:Q16514, ECO:0000269|PubMed:18854162}.
CC -!- SUBUNIT: Interacts (via histone-fold domain) with taf-4 (via the
CC histone-fold domain) (PubMed:18854162). Interaction may facilitate the
CC nuclear localization of taf-4 (PubMed:18854162).
CC {ECO:0000269|PubMed:18854162}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18854162}.
CC Note=Localized to nucleus throughout early embryogenesis.
CC {ECO:0000269|PubMed:18854162}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y56A3A.4a};
CC IsoId=Q9U226-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y56A3A.4b};
CC IsoId=Q9U226-2; Sequence=VSP_061417;
CC -!- DOMAIN: The histone-fold domain mediates hetero-dimer protein-protein
CC interactions. {ECO:0000269|PubMed:18854162}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces nuclear
CC localization of taf-4. {ECO:0000269|PubMed:18854162}.
CC -!- SIMILARITY: Belongs to the TAF12 family. {ECO:0000305}.
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DR EMBL; BX284603; CAB60514.2; -; Genomic_DNA.
DR EMBL; BX284603; CAX65090.1; -; Genomic_DNA.
DR RefSeq; NP_001255144.1; NM_001268215.1.
DR RefSeq; NP_001255145.1; NM_001268216.1.
DR AlphaFoldDB; Q9U226; -.
DR SMR; Q9U226; -.
DR DIP; DIP-24869N; -.
DR IntAct; Q9U226; 36.
DR STRING; 6239.Y56A3A.4a; -.
DR PaxDb; Q9U226; -.
DR EnsemblMetazoa; Y56A3A.4a.1; Y56A3A.4a.1; WBGene00006396. [Q9U226-1]
DR EnsemblMetazoa; Y56A3A.4b.1; Y56A3A.4b.1; WBGene00006396. [Q9U226-2]
DR GeneID; 176617; -.
DR KEGG; cel:CELE_Y56A3A.4; -.
DR UCSC; Y56A3A.4; c. elegans. [Q9U226-1]
DR CTD; 176617; -.
DR WormBase; Y56A3A.4a; CE31842; WBGene00006396; taf-12.
DR WormBase; Y56A3A.4b; CE43550; WBGene00006396; taf-12.
DR eggNOG; KOG1142; Eukaryota.
DR GeneTree; ENSGT00390000002144; -.
DR HOGENOM; CLU_797515_0_0_1; -.
DR InParanoid; Q9U226; -.
DR OMA; ACKMIKN; -.
DR OrthoDB; 1569957at2759; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006396; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9U226; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037794; TAF12.
DR InterPro; IPR003228; TFIID_TAF12_dom.
DR PANTHER; PTHR12264; PTHR12264; 1.
DR Pfam; PF03847; TFIID_20kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..342
FT /note="Transcription initiation factor TFIID subunit 12"
FT /id="PRO_0000454932"
FT DOMAIN 230..297
FT /note="Histone-fold"
FT /evidence="ECO:0000303|PubMed:18854162"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..221
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061417"
SQ SEQUENCE 342 AA; 38174 MW; 7F122D0A3DED5633 CRC64;
MKMEEFSPPT SPNNHVIVQA NPQIAAALST NSPMQQGIPP QGHQNPNEQQ QQQQFVGQPP
MGGMGGPMRM QMPQQQIRQM PYPSPQMRAG PPPPQQQQQQ HFQQMGIPQQ QQPQQFTPNG
QSMQMQQRPM QMGMAQGPGP SGHLMGMVGG PPPQHMMQQQ GGGGPPQFVP NSSPMPLPPQ
QIMQVQHQQQ HQQPPPSQQI QQPPIPQPQQ QQAPPPQMIP AAVPYGSIME KSKLDDLMQQ
ISSTTVLEEN VKDVLVEYAD DFVSSLIDKA CKMIKNREVK KIESRDIEFI LKNVYNMPVV
PRAASHNFGS QTEVIDLSKE KFVPTEAHKQ RVALLKKQIK KL
