TF3A_RAT
ID TF3A_RAT Reviewed; 363 AA.
AC Q8VHT8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Transcription factor IIIA;
DE Short=TFIIIA;
GN Name=Gtf3a;
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 [MRNA] OF 1-134.
RC TISSUE=Spinal ganglion;
RA Fitzpatrick D.;
RT "Amgen rat EST program.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-363.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11814676; DOI=10.1016/s0378-1119(01)00796-x;
RA Hanas J.S., Hocker J.R., Cheng Y.-G., Lerner M.R., Brackett D.J.,
RA Lightfoot S.A., Hanas R.J., Madhusudhan K.T., Moreland R.J.;
RT "cDNA cloning, DNA binding, and evolution of mammalian transcription factor
RT IIIA.";
RL Gene 282:43-52(2002).
CC -!- FUNCTION: Involved in ribosomal large subunit biogenesis. Binds the
CC approximately 50 base pairs internal control region (ICR) of 5S
CC ribosomal RNA genes. It is required for their RNA polymerase III-
CC dependent transcription and may also maintain the transcription of
CC other genes (By similarity). Also binds the transcribed 5S RNA's (By
CC similarity). {ECO:0000250|UniProtKB:P17842,
CC ECO:0000250|UniProtKB:Q92664}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- CAUTION: It is uncertain whether Met-1 is the initiator. Based on the
CC lack of an in-frame AUG codon, mammalian TFIIIA may be translated from
CC this non-AUG initiation site, which has a good Kozak context and which
CC is well conserved among mammals. {ECO:0000305}.
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DR EMBL; CB616240; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF391798; AAL69685.1; -; mRNA.
DR RefSeq; NP_001107042.1; NM_001113570.1.
DR AlphaFoldDB; Q8VHT8; -.
DR SMR; Q8VHT8; -.
DR BioGRID; 251579; 1.
DR STRING; 10116.ENSRNOP00000065623; -.
DR PaxDb; Q8VHT8; -.
DR PRIDE; Q8VHT8; -.
DR GeneID; 246299; -.
DR KEGG; rno:246299; -.
DR CTD; 2971; -.
DR RGD; 619746; Gtf3a.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q8VHT8; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8VHT8; -.
DR Reactome; R-RNO-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR PRO; PR:Q8VHT8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:RGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Ribosome biogenesis; RNA-binding; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..363
FT /note="Transcription factor IIIA"
FT /id="PRO_0000319867"
FT ZN_FING 38..62
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 68..92
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 98..123
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 130..154
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 160..184
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 187..211
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 215..237
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..269
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 275..299
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 301..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 29..32
FT /note="PPRP -> ARAG (in Ref. 1; AAL69685)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="I -> T (in Ref. 1; AAL69685)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="P -> S (in Ref. 1; AAL69685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 41387 MW; AACA8D5B80124563 CRC64;
MEPRVSVAEA VSSLTIADAF VRACVGPAPP RPALPSRFIC SFPDCSASYN KAWKLDAHLC
KHTGERPFVC DYEGCGKAFI RDYHLSRHIL IHTGEKPFVC ADNGCNQKFS TKSNLKKHIE
RKHENPQKQY VCNFEGCKKA FKKHQQLRTH QCQHTNEPLF RCTHEGCGKH FASPSRLKRH
GKVHEGYLCQ KGCSFVGKTW TELLKHTREA HKEEVTCTVC QKMFKRKDHL KQHMKTHAPE
RDVYRCPREG CARTYTTVFN LQSHILSFHE EKRPFVCEHA GCGKTFAMKQ SLMRHSVVHD
PDKKRMKLKV RPPRERRSLA SRLSGYVPPK GKQEPDCSLP NSTESSSSPE ATMLAPAALL
TVH
