TFAM_PIG
ID TFAM_PIG Reviewed; 246 AA.
AC Q5D144;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kunej T., Wu X.-L., Milosevic Berlic T., Michal J.J., Jiang Z., Dovc P.;
RT "The porcine mitochondrial transcription factor A (TFAM) gene: sequencing,
RT mapping and genetic diversity among 12 pig breeds.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}. Mitochondrion
CC matrix, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY923074; AAX18878.1; -; mRNA.
DR RefSeq; NP_001123683.1; NM_001130211.1.
DR RefSeq; XP_013845911.1; XM_013990457.1.
DR AlphaFoldDB; Q5D144; -.
DR SMR; Q5D144; -.
DR STRING; 9823.ENSSSCP00000019961; -.
DR PaxDb; Q5D144; -.
DR PeptideAtlas; Q5D144; -.
DR PRIDE; Q5D144; -.
DR Ensembl; ENSSSCT00000046982; ENSSSCP00000042490; ENSSSCG00000040185.
DR Ensembl; ENSSSCT00025095928; ENSSSCP00025042122; ENSSSCG00025069797.
DR Ensembl; ENSSSCT00030040451; ENSSSCP00030018521; ENSSSCG00030028998.
DR Ensembl; ENSSSCT00035065029; ENSSSCP00035026320; ENSSSCG00035048817.
DR Ensembl; ENSSSCT00040084039; ENSSSCP00040036627; ENSSSCG00040061715.
DR Ensembl; ENSSSCT00045022675; ENSSSCP00045015636; ENSSSCG00045013293.
DR Ensembl; ENSSSCT00050075064; ENSSSCP00050032387; ENSSSCG00050055011.
DR Ensembl; ENSSSCT00055023143; ENSSSCP00055018304; ENSSSCG00055011815.
DR Ensembl; ENSSSCT00060028401; ENSSSCP00060012166; ENSSSCG00060020953.
DR Ensembl; ENSSSCT00065008738; ENSSSCP00065003689; ENSSSCG00065006459.
DR Ensembl; ENSSSCT00070045780; ENSSSCP00070038583; ENSSSCG00070023001.
DR GeneID; 397279; -.
DR KEGG; ssc:397279; -.
DR CTD; 7019; -.
DR VGNC; VGNC:109416; TFAM.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00440000039001; -.
DR HOGENOM; CLU_2800755_0_0_1; -.
DR InParanoid; Q5D144; -.
DR OMA; ISVQAKM; -.
DR OrthoDB; 1641977at2759; -.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Bgee; ENSSSCG00000040185; Expressed in testis and 44 other tissues.
DR ExpressionAtlas; Q5D144; baseline.
DR Genevisible; Q5D144; SS.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; IBA:GO_Central.
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:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
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; Reference proteome; Repeat; Transcription;
KW Transcription regulation; 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_0000270512"
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 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; 28726 MW; D83F0FAC0EBAAAD1 CRC64;
MALLRGVWGV LSALGKSGAD LCAVCGSRLR SPFSFAYVPR WFSSTLSGFP KKPMTSYVRF
SKEQLPIFKA QNPDAKNSEL IKKIAELWRE LPDSEKKIYE DAYRADWQVY KEEVNRIQEQ
LTPSQMVSLE KEIMQKRLKK KALIKKRELT MLGKPKRPRS AYNIFIAERF QEAKDGPSQV
KLKTINENWK NLSSSQKQVY IQLAEDDKVR YYNEMKSWEE QMVEVGRNDL IRRSMKHSAK
KDTEEC
