TAF2_CAEEL
ID TAF2_CAEEL Reviewed; 1086 AA.
AC Q9TYN3;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Transcription initiation factor TFIID subunit 2 {ECO:0000250|UniProtKB:Q6P1X5};
DE AltName: Full=TBP-associated transcription factor 2 {ECO:0000312|WormBase:Y37E11B.4};
GN Name=taf-2 {ECO:0000312|WormBase:Y37E11B.4};
GN ORFNames=Y37E11B.4 {ECO:0000312|WormBase:Y37E11B.4};
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 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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14726532; DOI=10.1074/jbc.m310731200;
RA Walker A.K., Shi Y., Blackwell T.K.;
RT "An extensive requirement for transcription factor IID-specific TAF-1 in
RT Caenorhabditis elegans embryonic transcription.";
RL J. Biol. Chem. 279:15339-15347(2004).
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-2
CC (By similarity). May regulate RNA polymerase II activity and thereby
CC may control transcription initiation by RNA polymerase II
CC (PubMed:14726532). {ECO:0000250|UniProtKB:Q6P1X5,
CC ECO:0000269|PubMed:14726532}.
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). {ECO:0000250|UniProtKB:Q6P1X5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6P1X5}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a severe loss of
CC RNA polymerase II large subunit ama-1 phosphorylation.
CC {ECO:0000269|PubMed:14726532}.
CC -!- SIMILARITY: Belongs to the TAF2 family. {ECO:0000305}.
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DR EMBL; BX284604; CCD61342.1; -; Genomic_DNA.
DR PIR; T33893; T33893.
DR RefSeq; NP_500378.1; NM_067977.3.
DR AlphaFoldDB; Q9TYN3; -.
DR SMR; Q9TYN3; -.
DR IntAct; Q9TYN3; 2.
DR STRING; 6239.Y37E11B.4; -.
DR EPD; Q9TYN3; -.
DR PaxDb; Q9TYN3; -.
DR PeptideAtlas; Q9TYN3; -.
DR EnsemblMetazoa; Y37E11B.4.1; Y37E11B.4.1; WBGene00006383.
DR UCSC; Y37E11B.4; c. elegans.
DR WormBase; Y37E11B.4; CE52319; WBGene00006383; taf-2.
DR eggNOG; KOG1932; Eukaryota.
DR GeneTree; ENSGT00390000000420; -.
DR HOGENOM; CLU_002317_0_0_1; -.
DR InParanoid; Q9TYN3; -.
DR OMA; GQESYEW; -.
DR PhylomeDB; Q9TYN3; -.
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 PRO; PR:Q9TYN3; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006383; Expressed in embryo and 4 other tissues.
DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IMP:WormBase.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR037813; TAF2.
DR PANTHER; PTHR15137; PTHR15137; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1086
FT /note="Transcription initiation factor TFIID subunit 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435003"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1086 AA; 123495 MW; 8D2D6ECF82B9B047 CRC64;
MDFSEASTSG DRVNGFAKPF PPKPREGAPP PAPPLAPGAS TSQAPPPLQP PPVIESAEKF
YVPGVEEKSK FRILSQQVEI SNLNISTRSF NVRTEIVLLP CEKSLYQLDL HIGKCSLLPN
EVPGSASKVT LNGVECEYSR RDFWKDLAQE KSISSLEPVL YEKLAENDYE LQILIPKEVR
KKIKHRKAVR LRVDTVVRDP PRGLQFVDFN EHDCHVFTYH TPHISGAREW TVCLDEPDQL
ALWELTFELE PHLVPVASGE LEEKREVSEN GKIRYKFHQT VPTSACNIGW AIGRFKLEPH
PESPTIYTFS LPGLEPFVNH TTMYLDKMVE FLEEKLSCRF PYPTLKVVFV DQCTEEIQVY
SSLLIVPTAM LYHKKIIDVV QEARQKLIFS IALQFFGCLI SPAQWWHWWI PVSIARFLTS
LYVETKLGTA EARWQLKRAM DDVCDYEHQW GKIVLSPPEP TKKLPLHVDP RHEYTASPLY
VEAMLKKGFL TMRMLQRRIG LEPFMRVLHR VLTVGLDMSE KKTTPAAWRH LLTTTESFFR
SVISVTGKEI PSFLSQFVRT GGHAAFAVKF DFNRKRNIVE IEIKQDDTEG NGRTQYTGPL
SVVVQEVDGA FTHTIQIDGA VSHAEISCHS KGRKQRKKKV PLLTGEEIEI DLTNMDAESP
ILWLRIDPDY LLIREITISQ PMFHWEYMLR YERDVIAQME ALERIQALPS AHSRSVIVDA
VANEKFFYRI RYRAAFVLTF VQNRKSEALT VGTPVLINMF RESFGSKAAT NIPRSNNFVV
TAQNLQQYFV MQALPQAIAR LRRQSGECHE DVQPFLLDLI KFNDNSTNRY SDDFYRAALY
NSLASSVFPH DALPCHVELP ENLSNDVRVL IKEFTYALNM DTVSPSWGRV VGAAALTGLY
QLQKCGYLPL DSQLLWTFSH PNCCVQMRRC AITLIIDRIV NDPHAADTRM LDLSRILELA
ELEQDPSIRR MIPRLLAQTP PTIFGSENAA NTAETAERLW KLCTNSSIDS CIRSGFLDVY
YSLYALGAPP ALGGPEESVG IHRAYVTVPN AASTFATSQW HNSGYEAARR SPPRRDFGDE
TMNLMQ
