TFAM_RAT
ID TFAM_RAT Reviewed; 244 AA.
AC Q91ZW1; Q9WTM7;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Transcription factor A, mitochondrial {ECO:0000305};
DE Short=mtTFA;
DE Flags: Precursor;
GN Name=Tfam {ECO:0000312|RGD:620682};
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], AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10902920; DOI=10.3109/10425170009033980;
RA Inagaki H., Hayashi T., Matsushima Y., Lin K.H., Maeda S., Ichihara S.,
RA Hitagawa Y., Saito T.;
RT "Isolation of rat mitochondrial transcription factor A (r-Tfam) cDNA.";
RL DNA Seq. 11:131-135(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=11943465; DOI=10.1016/s0378-1119(01)00811-3;
RA Mezzina M., Reyes A., D'Errico I., Gadaleta G.;
RT "Characterization of the mtTFA gene and identification of a processed
RT pseudogene in rat.";
RL Gene 286:105-112(2002).
RN [3]
RP RETRACTED PAPER.
RC STRAIN=ACI;
RX PubMed=12198131; DOI=10.1074/jbc.m206958200;
RA Dong X., Ghoshal K., Majumder S., Yadav S.P., Jacob S.T.;
RT "Mitochondrial transcription factor A and its downstream targets are up-
RT regulated in a rat hepatoma.";
RL J. Biol. Chem. 277:43309-43318(2002).
RN [4]
RP RETRACTION NOTICE OF PUBMED:12198131.
RX PubMed=30120151; DOI=10.1074/jbc.w118.004969;
RA Dong X., Ghoshal K., Majumder S., Yadav S.P., Jacob S.T.;
RL J. Biol. Chem. 293:12947-12947(2018).
RN [5]
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: [Isoform Mitochondrial]: Binds to the mitochondrial light
CC strand promoter and functions in mitochondrial transcription
CC regulation. Component of the mitochondrial transcription initiation
CC complex, composed at least of TFB2M, TFAM and POLRMT that is required
CC for basal transcription of mitochondrial DNA. In this complex, TFAM
CC recruits POLRMT to a specific promoter whereas TFB2M induces structural
CC changes in POLRMT to enable promoter opening and trapping of the DNA
CC non-template strand. Required for accurate and efficient promoter
CC recognition by the mitochondrial RNA polymerase. Promotes transcription
CC initiation from the HSP1 and the light strand promoter by binding
CC immediately upstream of transcriptional start sites. Is able to unwind
CC DNA. Bends the mitochondrial light strand promoter DNA into a U-turn
CC shape via its HMG boxes. Required for maintenance of normal levels of
CC mitochondrial DNA. May play a role in organizing and compacting
CC mitochondrial DNA (By similarity). {ECO:0000250|UniProtKB:Q00059}.
CC -!- FUNCTION: [Isoform Nuclear]: May also function as a transcriptional
CC activator or may have a structural role in the compaction of nuclear
CC DNA during spermatogenesis. {ECO:0000250|UniProtKB:P40630}.
CC -!- SUBUNIT: Monomer; binds DNA as a monomer. Homodimer. Component of the
CC mitochondrial transcription initiation complex, composed at least of
CC TFB2M, TFAM and POLRMT. In this complex TFAM recruits POLRMT to the
CC promoter whereas TFB2M induces structural changes in POLRMT to enable
CC promoter opening and trapping of the DNA non-template strand. Upon
CC metabolic stress, forms a complex composed of FOXO3, SIRT3, TFAM and
CC POLRMT. Interacts with TFB1M and TFB2M. Interacts with CLPX; this
CC enhances DNA-binding. {ECO:0000250|UniProtKB:Q00059}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion
CC {ECO:0000250|UniProtKB:Q00059}. Mitochondrion matrix, mitochondrion
CC nucleoid {ECO:0000250|UniProtKB:Q00059}.
CC -!- SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=Q91ZW1-1; Sequence=Displayed;
CC Name=Nuclear;
CC IsoId=Q91ZW1-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: The mitochondrial isoform is widely expressed while
CC the nuclear isoform is testis-specific.
CC -!- DOMAIN: Binds DNA via its HMG boxes. When bound to the mitochondrial
CC light strand promoter, bends DNA into a U-turn shape, each HMG box
CC bending the DNA by 90 degrees (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation by PKA within the HMG box 1 impairs DNA binding
CC and promotes degradation by the AAA+ Lon protease. {ECO:0000250}.
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DR EMBL; AB014089; BAA77755.1; -; mRNA.
DR EMBL; AJ312746; CAC84763.1; -; mRNA.
DR EMBL; AF377866; AAL12892.1; -; mRNA.
DR EMBL; BC062022; AAH62022.1; -; mRNA.
DR RefSeq; NP_112616.1; NM_031326.1. [Q91ZW1-1]
DR AlphaFoldDB; Q91ZW1; -.
DR SMR; Q91ZW1; -.
DR STRING; 10116.ENSRNOP00000000753; -.
DR jPOST; Q91ZW1; -.
DR PaxDb; Q91ZW1; -.
DR PRIDE; Q91ZW1; -.
DR Ensembl; ENSRNOT00000000753; ENSRNOP00000000753; ENSRNOG00000000613. [Q91ZW1-1]
DR GeneID; 83474; -.
DR KEGG; rno:83474; -.
DR UCSC; RGD:620682; rat. [Q91ZW1-1]
DR CTD; 7019; -.
DR RGD; 620682; Tfam.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00440000039001; -.
DR HOGENOM; CLU_083132_0_0_1; -.
DR InParanoid; Q91ZW1; -.
DR OMA; ISVQAKM; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; Q91ZW1; -.
DR TreeFam; TF318343; -.
DR Reactome; R-RNO-163282; Mitochondrial transcription initiation.
DR PRO; PR:Q91ZW1; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000613; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; Q91ZW1; RN.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
DR GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0034246; F:mitochondrial transcription factor activity; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:RGD.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; ISO:RGD.
DR GO; GO:0006390; P:mitochondrial transcription; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; ISS:UniProtKB.
DR Gene3D; 1.10.30.10; -; 2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09011; HMG_box_2; 1.
DR SMART; SM00398; HMG; 2.
DR SUPFAM; SSF47095; SSF47095; 2.
DR PROSITE; PS50118; HMG_BOX_2; 2.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA-binding; Mitochondrion;
KW Mitochondrion nucleoid; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..244
FT /note="Transcription factor A, mitochondrial"
FT /id="PRO_0000013472"
FT DNA_BIND 49..117
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 154..218
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 221..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57
FT /note="Intercalates between bases and promotes DNA bending"
FT /evidence="ECO:0000250"
FT SITE 181
FT /note="Intercalates between bases and promotes DNA bending"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 55
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 60
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 66
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40630"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 159
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT CONFLICT 171
FT /note="E -> G (in Ref. 1; BAA77755)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="A -> P (in Ref. 1; BAA77755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 28187 MW; 8725027A6331D62E CRC64;
MALFRGMWGV LRTLGRTGVE MCAGCGGRIP SPVSLICIPK CFSSLGNYPK KPMSSYLRFS
TEQLPKFKAK HPDAKVSELI RKIAAMWREL PEAEKKVYEA DFKAEWKVYK EAVSKYKEQL
TPSQLMGLEK EARQKRLKKK AQIKRRELIL LGKPKRPRSA YNIYVSESFQ EAKDESAQGK
LKLVNQAWKN LSHDEKQAYI QLAKDDRIRY DNEMKSWEEQ MAEVGRSDLI RRSVKRPPGD
ISEN
