TF3A_XENLA
ID TF3A_XENLA Reviewed; 366 AA.
AC P03001; Q91856;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transcription factor IIIA;
DE Short=TFIIIA;
DE AltName: Full=S-TFIIIA/O-TFIIIA;
GN Name=gtf3a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-366.
RX PubMed=6210149; DOI=10.1016/0092-8674(84)90455-0;
RA Ginsberg A.M., King B.O., Roeder R.G.;
RT "Xenopus 5S gene transcription factor, TFIIIA: characterization of a cDNA
RT clone and measurement of RNA levels throughout development.";
RL Cell 39:479-489(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-366.
RX PubMed=3754326; DOI=10.1093/nar/14.5.2187;
RA Yun Tso J., van den Berg J., Korn L.J.;
RT "Structure of the gene for Xenopus transcription factor TFIIIA.";
RL Nucleic Acids Res. 14:2187-2201(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 112-137.
RX PubMed=3755818; DOI=10.1093/nar/14.15.6185;
RA Taylor W., Jackson I.J., Siegel N., Kumar A., Brown D.D.;
RT "The developmental expression of the gene for TFIIIA in Xenopus laevis.";
RL Nucleic Acids Res. 14:6185-6195(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
RX PubMed=2744458; DOI=10.1101/gad.3.5.651;
RA Scotto K.W., Kaulen H., Roeder R.G.;
RT "Positive and negative regulation of the gene for transcription factor IIIA
RT in Xenopus laevis oocytes.";
RL Genes Dev. 3:651-662(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-26, AND FUNCTION.
RX PubMed=2253880; DOI=10.1101/gad.4.9.1602;
RA Kim S.H., Darby M.K., Joho K.E., Brown D.D.;
RT "The characterization of the TFIIIA synthesized in somatic cells of Xenopus
RT laevis.";
RL Genes Dev. 4:1602-1610(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-123, AND FUNCTION.
RX PubMed=1538401; DOI=10.1016/0022-2836(92)90248-i;
RA Liao X.B., Clemens K.R., Tennant L., Wright P.E., Gottesfeld J.M.;
RT "Specific interaction of the first three zinc fingers of TFIIIA with the
RT internal control region of the Xenopus 5 S RNA gene.";
RL J. Mol. Biol. 223:857-871(1992).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF CYS-42; HIS-55; GLY-91; LYS-93; CYS-134 AND
RP CYS-186.
RX PubMed=1762917; DOI=10.1093/nar/19.24.6871;
RA Smith J.F., Hawkins J., Leonard R.E., Hanas J.S.;
RT "Structural elements in the N-terminal half of transcription factor IIIA
RT required for factor binding to the 5S RNA gene internal control region.";
RL Nucleic Acids Res. 19:6871-6876(1991).
RN [8]
RP PHOSPHORYLATION AT SER-38 AND SER-336, AND MUTAGENESIS OF SER-38; SER-336
RP AND SER-350.
RX PubMed=11853545; DOI=10.1042/0264-6021:3620375;
RA Westmark C.J., Ghose R., Huber P.W.;
RT "Phosphorylation of Xenopus transcription factor IIIA by an oocyte protein
RT kinase CK2.";
RL Biochem. J. 362:375-382(2002).
RN [9]
RP REPEATS ANALYSIS.
RX PubMed=4040853; DOI=10.1002/j.1460-2075.1985.tb03825.x;
RA Miller J., McLachlan A.D., Klug A.;
RT "Repetitive zinc-binding domains in the protein transcription factor IIIA
RT from Xenopus oocytes.";
RL EMBO J. 4:1609-1614(1985).
RN [10]
RP REPEATS ANALYSIS.
RX PubMed=4007166; DOI=10.1016/0014-5793(85)80723-7;
RA Brown R.S., Sander C., Argos P.;
RT "The primary structure of transcription factor TFIIIA has 12 consecutive
RT repeats.";
RL FEBS Lett. 186:271-274(1985).
RN [11]
RP REPEATS ANALYSIS.
RA Boehm S., Drescher B.;
RT "Multiple internal repeats within the structure of the 5S RNA/DNA binding
RT transcription factor TF-IIIA from Xenopus laevis.";
RL Studia Biophys. 107:237-247(1985).
RN [12]
RP STRUCTURE BY NMR OF 10-101.
RX PubMed=9253405; DOI=10.1038/nsb0897-605;
RA Foster M.P., Wuttke D.S., Radhakrishnan I., Case D.A., Gottesfeld J.M.,
RA Wright P.E.;
RT "Domain packing and dynamics in the DNA complex of the N-terminal zinc
RT fingers of TFIIIA.";
RL Nat. Struct. Biol. 4:605-608(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 32-210.
RX PubMed=9501194; DOI=10.1073/pnas.95.6.2938;
RA Nolte R.T., Conlin R.M., Harrison S.C., Brown R.S.;
RT "Differing roles for zinc fingers in DNA recognition: structure of a six-
RT finger transcription factor IIIA complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2938-2943(1998).
CC -!- FUNCTION: Involved in ribosomal large subunit biogenesis (By
CC similarity). Acts as both a positive transcription factor for 5S RNA
CC genes and a specific RNA binding protein that complexes with 5S RNA in
CC oocytes to form the 7S ribonucleoprotein storage particle. May play an
CC essential role in the developmental change in 5S RNA gene expression.
CC Interacts with the internal control region (ICR) of approximately 50
CC bases within the 5S RNA genes, is required for correct transcription of
CC these genes by RNA polymerase III (PubMed:2253880, PubMed:1538401,
CC PubMed:1762917). Also binds the transcribed 5S RNA's (By similarity).
CC {ECO:0000250|UniProtKB:P17842, ECO:0000250|UniProtKB:Q92664,
CC ECO:0000269|PubMed:1538401, ECO:0000269|PubMed:1762917,
CC ECO:0000269|PubMed:2253880}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Somatic; Synonyms=S-TFIIIA;
CC IsoId=P03001-1; Sequence=Displayed;
CC Name=Oocyte; Synonyms=O-TFIIIA;
CC IsoId=P03001-2; Sequence=VSP_018962;
CC -!- TISSUE SPECIFICITY: Synthesized in oocytes and, in much lower levels,
CC in somatic cells.
CC -!- DEVELOPMENTAL STAGE: The levels follow the transcriptional activity of
CC oocyte type 5S RNA genes during embryogenesis, present in very high
CC levels in maturing oocytes when oocyte type 5S genes are being
CC expressed, and in much lower levels in somatic cells where the oocyte
CC type genes are not expressed.
CC -!- PTM: The N-terminus is blocked.
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DR EMBL; K02938; AAA49967.1; -; mRNA.
DR EMBL; X03681; CAB51745.1; -; Genomic_DNA.
DR EMBL; X03735; CAB51745.1; JOINED; Genomic_DNA.
DR EMBL; X03736; CAB51745.1; JOINED; Genomic_DNA.
DR EMBL; X03737; CAB51745.1; JOINED; Genomic_DNA.
DR EMBL; X03738; CAB51745.1; JOINED; Genomic_DNA.
DR EMBL; X03739; CAB51745.1; JOINED; Genomic_DNA.
DR EMBL; X15785; CAA33786.1; -; Genomic_DNA.
DR PIR; A35916; A35916.
DR PIR; A90857; TWXL3.
DR RefSeq; NP_001081328.1; NM_001087859.1. [P03001-2]
DR PDB; 1TF3; NMR; -; A=32-123.
DR PDB; 1TF6; X-ray; 3.10 A; A/D=23-212.
DR PDB; 1UN6; X-ray; 3.10 A; B/C/D=127-212.
DR PDB; 2HGH; NMR; -; A=127-212.
DR PDB; 2J7J; X-ray; 1.65 A; A=127-210.
DR PDBsum; 1TF3; -.
DR PDBsum; 1TF6; -.
DR PDBsum; 1UN6; -.
DR PDBsum; 2HGH; -.
DR PDBsum; 2J7J; -.
DR AlphaFoldDB; P03001; -.
DR SMR; P03001; -.
DR BioGRID; 99116; 2.
DR iPTMnet; P03001; -.
DR MaxQB; P03001; -.
DR PRIDE; P03001; -.
DR DNASU; 397777; -.
DR GeneID; 397777; -.
DR KEGG; xla:397777; -.
DR CTD; 397777; -.
DR Xenbase; XB-GENE-6252591; gtf3a.L.
DR OrthoDB; 1318335at2759; -.
DR EvolutionaryTrace; P03001; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 397777; Expressed in ovary and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; 6.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Direct protein sequencing;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribosome biogenesis; RNA-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..366
FT /note="Transcription factor IIIA"
FT /id="PRO_0000041632"
FT ZN_FING 35..59
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 65..89
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 95..120
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 127..151
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 157..181
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 184..210
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 214..236
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 243..268
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 274..298
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 299..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:11853545"
FT MOD_RES 336
FT /note="Phosphoserine; by CK2; in vitro"
FT /evidence="ECO:0000269|PubMed:11853545"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform Oocyte)"
FT /evidence="ECO:0000305"
FT /id="VSP_018962"
FT VARIANT 96
FT /note="T -> K"
FT VARIANT 319
FT /note="R -> C"
FT VARIANT 335
FT /note="V -> I"
FT VARIANT 356
FT /note="G -> D"
FT VARIANT 365
FT /note="I -> L"
FT MUTAGEN 38
FT /note="S->E,A: Abolishes phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:11853545"
FT MUTAGEN 42
FT /note="C->S: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:1762917"
FT MUTAGEN 55
FT /note="H->L: Inhibition of specific DNA binding."
FT /evidence="ECO:0000269|PubMed:1762917"
FT MUTAGEN 91
FT /note="G->S: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:1762917"
FT MUTAGEN 93
FT /note="K->E: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:1762917"
FT MUTAGEN 134
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:1762917"
FT MUTAGEN 186
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:1762917"
FT MUTAGEN 336
FT /note="S->E,A: Slightly decreases phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:11853545"
FT MUTAGEN 350
FT /note="S->E,A: No effect on phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:11853545"
FT CONFLICT 4
FT /note="K -> T (in Ref. 4; CAA33786)"
FT /evidence="ECO:0000305"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1TF6"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1TF3"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:1TF6"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1TF3"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1TF3"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:1TF6"
FT TURN 87..91
FT /evidence="ECO:0007829|PDB:1TF6"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1TF6"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1TF6"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:1TF6"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1TF6"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1TF6"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:2J7J"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:2J7J"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1TF6"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1TF6"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:2J7J"
FT HELIX 171..182
FT /evidence="ECO:0007829|PDB:2J7J"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2J7J"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1TF6"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:2J7J"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:2J7J"
SQ SEQUENCE 366 AA; 41911 MW; 29237E710292FA24 CRC64;
MAAKVASTSS EEAEGSLVTE GEMGEKALPV VYKRYICSFA DCGAAYNKNW KLQAHLCKHT
GEKPFPCKEE GCEKGFTSLH HLTRHSLTHT GEKNFTCDSD GCDLRFTTKA NMKKHFNRFH
NIKICVYVCH FENCGKAFKK HNQLKVHQFS HTQQLPYECP HEGCDKRFSL PSRLKRHEKV
HAGYPCKKDD SCSFVGKTWT LYLKHVAECH QDLAVCDVCN RKFRHKDYLR DHQKTHEKER
TVYLCPRDGC DRSYTTAFNL RSHIQSFHEE QRPFVCEHAG CGKCFAMKKS LERHSVVHDP
EKRKLKEKCP RPKRSLASRL TGYIPPKSKE KNASVSGTEK TDSLVKNKPS GTETNGSLVL
DKLTIQ
