TF3A_MOUSE
ID TF3A_MOUSE Reviewed; 364 AA.
AC Q8VHT7; Q8BJ79; Q8K270; Q9CSH8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Transcription factor IIIA;
DE Short=TFIIIA;
GN Name=Gtf3a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-364.
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL69686.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB28476.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF391799; AAL69686.1; ALT_INIT; mRNA.
DR EMBL; AK008247; BAC25209.1; ALT_INIT; mRNA.
DR EMBL; AK012797; BAB28476.2; ALT_INIT; mRNA.
DR EMBL; BC032292; AAH32292.1; -; mRNA.
DR CCDS; CCDS19873.2; -.
DR RefSeq; NP_079928.2; NM_025652.3.
DR AlphaFoldDB; Q8VHT7; -.
DR SMR; Q8VHT7; -.
DR STRING; 10090.ENSMUSP00000119607; -.
DR iPTMnet; Q8VHT7; -.
DR PhosphoSitePlus; Q8VHT7; -.
DR EPD; Q8VHT7; -.
DR MaxQB; Q8VHT7; -.
DR PaxDb; Q8VHT7; -.
DR PRIDE; Q8VHT7; -.
DR ProteomicsDB; 259014; -.
DR Antibodypedia; 5062; 248 antibodies from 25 providers.
DR DNASU; 66596; -.
DR Ensembl; ENSMUST00000146511; ENSMUSP00000119607; ENSMUSG00000016503.
DR GeneID; 66596; -.
DR KEGG; mmu:66596; -.
DR UCSC; uc009ano.3; mouse.
DR CTD; 2971; -.
DR MGI; MGI:1913846; Gtf3a.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155647; -.
DR InParanoid; Q8VHT7; -.
DR OMA; HRKEQHR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8VHT7; -.
DR Reactome; R-MMU-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR BioGRID-ORCS; 66596; 21 hits in 76 CRISPR screens.
DR ChiTaRS; Gtf3a; mouse.
DR PRO; PR:Q8VHT7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VHT7; protein.
DR Bgee; ENSMUSG00000016503; Expressed in otic placode and 267 other tissues.
DR ExpressionAtlas; Q8VHT7; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; ISO:MGI.
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; 6.
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..364
FT /note="Transcription factor IIIA"
FT /id="PRO_0000319866"
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 299..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 75..77
FT /note="CGK -> HAS (in Ref. 3; AAH32292)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="V -> L (in Ref. 1; AAL69686)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..173
FT /note="THQCQHTSEPLFRCTHEGCGKHFAS -> PISASTPASRSSGVPTRDAGSTL
FT PR (in Ref. 2; BAC25209)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="S -> P (in Ref. 2; BAC25209)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="K -> I (in Ref. 2; BAC25209)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="A -> T (in Ref. 3; AAH32292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 41571 MW; FEC01712C5C8D4DA CRC64;
MEPRVSVAEA VSSLTIADAF VGACEGPAPP RPALPSRFIC SFPDCSASYN KAWKLDAHLC
KHTGERPFVC DYEGCGKAFI RDYHLSRHVL IHTGEKPFVC ADDGCNQKFN TKSNLKKHIE
RKHGNPQKQY VCSYEGCKKA FKKHQQLRTH QCQHTSEPLF RCTHEGCGKH FASPSRLKRH
GKVHEGYLCQ KGCSFMGKTW TELLKHMREA HKEDITCNVC QRMFKRRDYL KQHMKTHAPE
RDVYRCPRQG CGRTYTTVFN LQSHILSFHE EKRPFVCEHA GCGKTFAMKQ SLMRHSVVHD
PDKKRMKLKV RAPRERRSLA SRLSGYFPPK RKQEPDYSLP NASAESSSSP EAQLPPPAAL
LTVC
