Detail Information for IndEnz0002012814
IED ID IndEnz0002012814
Enzyme Type ID protease012814
Protein Name Transcription factor A, mitochondrial
mtTFA
Testis-specific high mobility group protein
TS-HMG
Gene Name Tfam Hmgts
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MALFRGMWSVLKALGRTGVEMCAGCGGRIPSSISLVCIPKCFSSMGSYPKKPMSSYLRFSTEQLPKFKAKHPDAKLSELVRKIAALWRELPEAEKKVYEADFKAEWKAYKEAVSKYKEQLTPSQLMGMEKEARQRRLKKKALVKRRELILLGKPKRPRSAYNIYVSESFQEAKDDSAQGKLKLVNEAWKNLSPEEKQAYIQLAKDDRIRYDNEMKSWEEQMAEVGRSDLIRRSVKRSGDISEH
Enzyme Length 243
Uniprot Accession Number P40630
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 49..117; /note=HMG box 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00267; DNA_BIND 154..218; /note=HMG box 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00267
EC Number
Enzyme Function FUNCTION: [Isoform Mitochondrial]: Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation (By similarity). Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA (By similarity). In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (By similarity). Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase (By similarity). Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites (By similarity). Is able to unwind DNA (By similarity). Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes (By similarity). Required for maintenance of normal levels of mitochondrial DNA (PubMed:9500544). May play a role in organizing and compacting mitochondrial DNA (PubMed:17581862). {ECO:0000250|UniProtKB:Q00059, ECO:0000269|PubMed:17581862, ECO:0000269|PubMed:9500544}.; FUNCTION: [Isoform Nuclear]: May also function as a transcriptional activator or may have a structural role in the compaction of nuclear DNA during spermatogenesis. {ECO:0000269|PubMed:8673128}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Chain (1); DNA binding (2); Erroneous initiation (1); Frameshift (1); Modified residue (7); Sequence conflict (1); Site (2); Transit peptide (1)
Keywords Activator;Alternative splicing;DNA-binding;Mitochondrion;Mitochondrion nucleoid;Nucleus;Phosphoprotein;Reference proteome;Repeat;Transcription;Transcription regulation;Transit peptide
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:Q00059}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q00059}.; SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus {ECO:0000269|PubMed:8673128}.
Modified Residue MOD_RES 54; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:Q00059; MOD_RES 55; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:Q00059; MOD_RES 60; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:Q00059; MOD_RES 66; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 121; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q00059; MOD_RES 159; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:Q00059; MOD_RES 192; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q00059
Post Translational Modification PTM: Phosphorylation by PKA within the HMG box 1 impairs DNA binding and promotes degradation by the AAA+ Lon protease. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10341094; 10737799; 11062475; 11171100; 11217851; 11259653; 11588181; 11668394; 11940593; 12070272; 12206900; 12417746; 12466851; 12904583; 14610273; 14651853; 14978272; 15016765; 15545607; 15618518; 15757973; 15895466; 16043643; 16296893; 16325481; 16615898; 16996481; 17003040; 17227870; 17609113; 17827403; 18245781; 18614015; 18614564; 18790059; 18945718; 19805233; 20002202; 20022934; 20059953; 20071537; 20130269; 2035027; 20412781; 20421486; 20566479; 20656029; 20686481; 20932939; 21135502; 21212186; 21233488; 21267068; 21677750; 21752989; 21768369; 21780252; 22056359; 22110743; 22251459; 22474357; 22482729; 22904065; 22904094; 22961549; 22988253; 22988430; 23168219; 23321074; 23349485; 23386745; 23393161; 23473319; 23499423; 23690562; 23977020; 24150248; 24486705; 24703694; 24952961; 25005176; 25171792; 25371971; 25642965; 25752644; 25918232; 25944881; 26086365; 2628167; 26299452; 26305956; 26359992; 26374844; 26407721; 26545237; 27003179; 27053209; 27068470; 27124299; 27166947; 27659966; 27703142; 27760051; 28111078; 28122051; 28375739; 28376279; 28461218; 28466093; 28474670; 28504706; 28504707; 28595911; 28768180; 28846746; 28867657; 28962857; 29021295; 29132502; 29514069; 29615705; 29684311; 29844370; 29925003; 30226866; 30318339; 30333037; 30440089; 30553768; 30659235; 30853890; 30914652; 30933310; 30949583; 31042480; 31105007; 31226324; 31269437; 31505196; 31835787; 31890743; 32005765; 32057291; 32192190; 32244769; 32439659; 32525278; 32564285; 32579581; 32923630; 32971400; 33246070; 33264655; 33358867; 33760663; 34312668; 34320035; 34378772; 34462320; 9060414; 9570966; 9653653; 9916807;
Motif
Gene Encoded By
Mass 27,988
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda