TAF1C_RAT
ID TAF1C_RAT Reviewed; 842 AA.
AC Q6P773;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=TATA box-binding protein-associated factor, RNA polymerase I, subunit C;
DE AltName: Full=TATA box-binding protein-associated factor 1C;
DE Short=TBP-associated factor 1C;
DE AltName: Full=Transcription initiation factor SL1/TIF-IB subunit C;
GN Name=Taf1c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Component of the transcription factor SL1/TIF-IB complex,
CC which is involved in the assembly of the PIC (preinitiation complex)
CC during RNA polymerase I-dependent transcription. The rate of PIC
CC formation probably is primarily dependent on the rate of association of
CC SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in
CC stabilization of nucleolar transcription factor 1/UBTF on rDNA.
CC Formation of SL1/TIF-IB excludes the association of TBP with TFIID
CC subunits. Recruits RNA polymerase I to the rRNA gene promoter via
CC interaction with RRN3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the transcription factor SL1/TIF-IB complex,
CC composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the
CC complex interacts directly with TBP, TAF1A and TAF1B. Interaction of
CC the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the
CC transcription factor IID (TFIID) subunits. Interacts with MYC and RRN3.
CC Interacts with p53/TP53; the interaction prevents the association of
CC SL1/TIF-IB with UBTF and represses RNA polymerase I transcription (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; BC061804; AAH61804.1; -; mRNA.
DR RefSeq; NP_001014177.1; NM_001014155.1.
DR AlphaFoldDB; Q6P773; -.
DR STRING; 10116.ENSRNOP00000020990; -.
DR PaxDb; Q6P773; -.
DR PRIDE; Q6P773; -.
DR Ensembl; ENSRNOT00000020990; ENSRNOP00000020990; ENSRNOG00000015632.
DR GeneID; 361420; -.
DR KEGG; rno:361420; -.
DR UCSC; RGD:1305658; rat.
DR CTD; 9013; -.
DR RGD; 1305658; Taf1c.
DR eggNOG; ENOG502QTCT; Eukaryota.
DR GeneTree; ENSGT00390000010767; -.
DR HOGENOM; CLU_360905_0_0_1; -.
DR InParanoid; Q6P773; -.
DR OMA; CCRRWLK; -.
DR OrthoDB; 372910at2759; -.
DR PhylomeDB; Q6P773; -.
DR TreeFam; TF351959; -.
DR Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR PRO; PR:Q6P773; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000015632; Expressed in thymus and 19 other tissues.
DR Genevisible; Q6P773; RN.
DR GO; GO:0001650; C:fibrillar center; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; ISO:RGD.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; ISO:RGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR038801; TAF1C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15319; PTHR15319; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..842
FT /note="TATA box-binding protein-associated factor, RNA
FT polymerase I, subunit C"
FT /id="PRO_0000118865"
FT REGION 574..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 808
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15572"
SQ SEQUENCE 842 AA; 92371 MW; 4B8AF9F2BFA77097 CRC64;
MDFPSTLRPS LFMAGPLGMT DGPDLSFMCS WRDALTLPGA QPQNCRDQTS SFAKNLLWEP
STPGPLPLVP PGPDPWDPGL AAQDFLFRGG HYYQYQSRVV LDVTEQLSRF LWDHGDIAFA
PLGKLMLENF RLEGNRGYSK KVTIVSVKRL LQDLGGHQPW GCPWASLSRR LRRFSILGGP
VLSRSVSLLM GRLLHEELAT RWEQLLMDEA FTGGALAWLP GRTARAGQLV YPSGGALDKL
YFQEVSVNSG GNPRVLEDPG HIQLRGPVRQ VVTSTVQGET LLAVRSDYHC AVWKIDKQEP
PAPLQVLQVE KGATGISLSP HLSGELAICS RSGTVCLWTP QDGLQTIYKD PETLAFRDPS
PWRWADFTAH PRVLTVGDRT GVKMVDIQGP PGCGLLLFCA GAEAACQKGE RVLLAQYLGQ
PGPASTSLHL ICTQFSIYLM DERLPLVPML KWDHGLPSAP LLARLLPPAS PGYPRPLLLG
GQGGQVQLLH IAGEGTSIPQ LAGPPQSLPS ITDSLSAFPL LEPKRQQQLQ ERLEAPVIGL
AAAPPCASAP GLLLFQLSAA GDVFYQHLRI QQTSSLREPD HPAPERPASR AAAPPVDQGS
TPSWTSRASA RCSRWLEALM ELSPTNPVWA APTFSHRRFL GHMERQKSQE TLAQKLQAAM
AKGQLLRPGD LGTLPKAEPP PAPQCSQQDE LTERLTKAWE GQAAAWWKRH QDQTSGSQRQ
SKRPKRRTQL SSTFSSFTSY MDSPDASSAP HSQDLSNSEA CPQPPRTPPS QELTQELWAQ
GVQHERRQTL RDYMAKLPLQ DNPGPVATPP SQTSSRQTRS FRQQTPVLSG SHPPRKKPRM
GF
