TFAM_TRACR
ID TFAM_TRACR Reviewed; 246 AA.
AC Q4H0T5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Transcription factor A, mitochondrial {ECO:0000250|UniProtKB:Q00059};
DE Short=mtTFA;
DE Flags: Precursor;
GN Name=TFAM {ECO:0000250|UniProtKB:Q00059};
OS Trachypithecus cristatus (Silvered leaf-monkey) (Presbytis cristata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Trachypithecus.
OX NCBI_TaxID=122765;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15978747; DOI=10.1016/j.gene.2005.03.044;
RA D'Errico I., Reyes A., Dinardo M., Gadaleta G.;
RT "Study of mitochondrial transcription factor A (Tfam) gene in the primate
RT Presbytis cristata.";
RL Gene 354:117-124(2005).
CC -!- FUNCTION: Binds to the mitochondrial light strand promoter and
CC functions in mitochondrial transcription regulation. Component of the
CC mitochondrial transcription initiation complex, composed at least of
CC TFB2M, TFAM and POLRMT that is required for basal transcription of
CC mitochondrial DNA. In this complex, TFAM recruits POLRMT to a specific
CC promoter whereas TFB2M induces structural changes in POLRMT to enable
CC promoter opening and trapping of the DNA non-template strand. Required
CC for accurate and efficient promoter recognition by the mitochondrial
CC RNA polymerase. Promotes transcription initiation from the HSP1 and the
CC light strand promoter by binding immediately upstream of
CC transcriptional start sites. Is able to unwind DNA. Bends the
CC mitochondrial light strand promoter DNA into a U-turn shape via its HMG
CC boxes. Required for maintenance of normal levels of mitochondrial DNA.
CC May play a role in organizing and compacting mitochondrial DNA.
CC {ECO:0000250|UniProtKB:Q00059}.
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: Mitochondrion. Mitochondrion matrix,
CC mitochondrion nucleoid {ECO:0000250}.
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; AJ830015; CAH25649.1; -; mRNA.
DR AlphaFoldDB; Q4H0T5; -.
DR SMR; Q4H0T5; -.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0034246; F:mitochondrial transcription factor activity; ISS:UniProtKB.
DR GO; GO:0006390; P:mitochondrial transcription; ISS:UniProtKB.
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; DNA-binding; Mitochondrion; Mitochondrion nucleoid;
KW Phosphoprotein; Repeat; Transcription; Transcription regulation;
KW Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..246
FT /note="Transcription factor A, mitochondrial"
FT /id="PRO_0000269182"
FT DNA_BIND 50..118
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 155..219
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT SITE 58
FT /note="Intercalates between bases and promotes DNA bending"
FT /evidence="ECO:0000250"
FT SITE 182
FT /note="Intercalates between bases and promotes DNA bending"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 56
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 61
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 160
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00059"
SQ SEQUENCE 246 AA; 28898 MW; B78FDCA6BAC2B167 CRC64;
MAFLRSMWGV LSALGRSGAA VCIGCGSRLR SPFSFVYLPK CFSSVLASCP KKPVSSYLRF
SKEQLPIFKA ENPDAKPTEL IRRIAKLWRE LPDSKKKIYQ DAYRADWQVY KEKISRFKEQ
LTPSQITSLE KEIMDKHLKR KAMTKRKELT QLGKPKRPRS AYNVYVAEKF QEAKGDSPQE
KLKTVKENWK NLSDSEKELY IRLAKEDEIR YHNEMKSWEE QMIEAGRKDL LRRTIKQRQK
YGAEEY
