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TAF3_CHICK
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   03-AUG-2022, entry version 96.
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; Q5F489; -.
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   OrthoDB; 320730at2759; -.
DR   PhylomeDB; Q5F489; -.
DR   PRO; PR:Q5F489; -.
DR   Proteomes; UP000000539; Unplaced.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   Gene3D; 1.10.20.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 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   Pfam; PF07524; Bromo_TP; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00576; BTP; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; SSF57903; 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
 
 
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