ID TAF3_CHICK Reviewed; 930 AA.
AC Q5F489;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 08-NOV-2023, entry version 100.
DE RecName: Full=Transcription initiation factor TFIID subunit 3;
DE AltName: Full=TBP-associated factor 3;
GN Name=TAF3; ORFNames=RCJMB04_2c9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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. TAF3 forms the TFIID-A module together with
CC TAF5 and TBP. Required in complex with TBPL2 for the differentiation of
CC myoblasts into myocytes. The TAF3-TBPL2 complex replaces TFIID at
CC specific promoters at an early stage in the differentiation process.
CC {ECO:0000250|UniProtKB:Q5VWG9}.
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 TAF10 via the histone fold. Interacts with TAF13, TBP, SAP130 and
CC GCN5L2. Interacts with TBPL2. {ECO:0000250|UniProtKB:Q5VWG9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TAF3 family. {ECO:0000305}.
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DR EMBL; AJ851411; CAH65045.1; -; mRNA.
DR RefSeq; NP_001026012.1; NM_001030841.2.
DR AlphaFoldDB; Q5F489; -.
DR SMR; Q5F489; -.
DR STRING; 9031.ENSGALP00000010875; -.
DR PaxDb; 9031-ENSGALP00000010875; -.
DR GeneID; 419107; -.
DR KEGG; gga:419107; -.
DR CTD; 83860; -.
DR VEuPathDB; HostDB:geneid_419107; -.
DR eggNOG; KOG1973; Eukaryota.
DR eggNOG; KOG2389; Eukaryota.
DR InParanoid; Q5F489; -.
DR PhylomeDB; Q5F489; -.
DR PRO; PR:Q5F489; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15522; PHD_TAF3; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46452; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 3; 1.
DR PANTHER; PTHR46452:SF1; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 3; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00576; BTP; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..930
FT /note="Transcription initiation factor TFIID subunit 3"
FT /id="PRO_0000245530"
FT ZN_FING 866..916
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 128..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..820
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 103181 MW; C60B08BFE8643256 CRC64;
MCETYSRWLL RVSVAQICQA LGWDSVQVSA CDLLTDVLQR YLQGLGRGCH RYCELYGRTD
PILDDVGDAF KLMGVNLHEL EDYIHNIEPV TFAHQIPSFP VSKNNVLQFP QPGSKDAEER
KEYIPDYMPP IVSSQEEEEE EQVPTDGGTS AEAMQVPLEE EGDMEEDEAI NDENYLSKRP
LESPDAEEFP PMKRPKLSVS KGDALDGALE PREPLSSINT QKVPPMLSPV HVQDSTDLAP
PSPEPPMLAP IAKSQVPTPK TLESKPPAPK TKSKTSSPGQ KTKSPKTTPS PVVAGSPIRS
PKTGSKEKKS PGRAKSPKSP KSPKAPVHVP PPPVKPETPS RTPLAALSDK IGKENIQVKQ
GQTPPEPVTK PNIENQTKKL PVVDKTIDDS IDAVIARACA EREPDPFEFS SGSESEGEIF
TSPKRLSVSE TTATTPKPSV STNCSNKAGA TPVPPSGGTS SSDISWTMDD SIDEVIRKAN
MGTPSNPPAN FTYFSSPSAS PPTPEPLLKV YEEKTKLASS VEVKKKLKKE LKTKMKKKEK
QKEKDKEKSK EKNKEKEKNK EKDKDKEGNK EAKFQWKELL KDDEHDPYKF KLKDFEDADT
KVKLKDGNTK KEKEKHKDKK KEKEKGKKDK DKKDKEKVKD KSKEDKIKPP SAPLVLPPKE
MSLPLFSTPT AMRLPSMLPS LSPMLPEKLF EDKEKPKEKK KDKKEKKKKK EREKDKEKEK
KDKEKERKER EKKEKEKEKH KHEKIKVEPV VPAPSPVIPR LTLRVGAGQD KIVISKVVPA
PEAKPATPVS RPKTPPPVPS PVPAPVHVTP PPAPVPAPPQ PTVSPALLPP ASPAVSAAGG
SKAPVRSVVT ETVSTYVIRD EWGNQIWFCP GCNKPDDGSP MIGCDDCDDW YHWPCVGITA
APPEEMQWFC SKCANKKKDK KHKKRKHRAH
//
