MTF1A_MOUSE
ID MTF1A_MOUSE Reviewed; 379 AA.
AC Q8CHZ9; Q63ZX5; Q8C7T1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transcription termination factor 1a, mitochondrial;
DE AltName: Full=Mitochondrial transcription termination factor 1a;
DE Short=mTERF1a;
DE Flags: Precursor;
GN Name=Mterf1a; Synonyms=Mterf, Mterf1;
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=SWR/J; TISSUE=Liver;
RX PubMed=15582606; DOI=10.1016/j.bbrc.2004.11.057;
RA Li X., Zhang L.S., Guan M.-X.;
RT "Cloning and characterization of mouse mTERF encoding a mitochondrial
RT transcriptional termination factor.";
RL Biochem. Biophys. Res. Commun. 326:505-510(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, Eye, and 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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-271.
RC STRAIN=C57BL/6J;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23562081; DOI=10.1016/j.cmet.2013.03.006;
RA Terzioglu M., Ruzzenente B., Harmel J., Mourier A., Jemt E., Lopez M.D.,
RA Kukat C., Stewart J.B., Wibom R., Meharg C., Habermann B., Falkenberg M.,
RA Gustafsson C.M., Park C.B., Larsson N.G.;
RT "MTERF1 binds mtDNA to prevent transcriptional interference at the light-
RT strand promoter but is dispensable for rRNA gene transcription
RT regulation.";
RL Cell Metab. 17:618-626(2013).
CC -!- FUNCTION: Transcription termination factor. Binds to a 28 bp region
CC within the tRNA(Leu(uur)) gene at a position immediately adjacent to
CC and downstream of the 16S rRNA gene; this region comprises a tridecamer
CC sequence critical for directing accurate termination. Binds DNA along
CC the major grove and promotes DNA bending and partial unwinding.
CC Promotes base flipping. Transcription termination activity appears to
CC be polarized with highest specificity for transcripts initiated on the
CC light strand. {ECO:0000269|PubMed:23562081}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15582606}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart and liver, with
CC extremely low levels in other tissues (PubMed:15582606). Expressed
CC strongly in the heart and at lower levels in brain, liver and kidney
CC (PubMed:23562081). {ECO:0000269|PubMed:15582606,
CC ECO:0000269|PubMed:23562081}.
CC -!- DOMAIN: Contains nine structural repeats of about 35 residues, where
CC each repeat contains three helices. The repeats form a left-handed
CC superhelical assembly with a solenoid structure that wraps itself
CC around DNA (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphoprotein with mostly four phosphate groups. While the DNA-
CC binding activity is unaffected by the phosphorylation state, only the
CC phosphorylated form of the protein is active for termination activity.
CC Functioning seems to be regulated by phosphorylation (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Double knockout of Mterf1a and Mterf1b results in
CC viable animals with no gross phenotype, and normal oxidative
CC phosphorylation capacity. Steady-state mitochondrial DNA levels are
CC normal. There are subtle effects on levels of mitochondrial
CC transcripts: transcripts initiated at the light strand promoter and
CC also downstream of the MTERF binding site are increased, levels of 7S
CC RNA are reduced, while levels of other mitochondrial transcripts are
CC normal. {ECO:0000269|PubMed:23562081}.
CC -!- SIMILARITY: Belongs to the mTERF family. {ECO:0000305}.
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DR EMBL; AY726770; AAU26065.1; -; mRNA.
DR EMBL; AC027653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038058; AAH38058.1; -; mRNA.
DR EMBL; BC051251; AAH51251.1; -; mRNA.
DR EMBL; BC082778; AAH82778.1; -; mRNA.
DR EMBL; BC094442; AAH94442.1; -; mRNA.
DR EMBL; AK049308; BAC33673.1; -; mRNA.
DR CCDS; CCDS39003.1; -.
DR RefSeq; NP_001013041.2; NM_001013023.2.
DR RefSeq; NP_742147.1; NM_172135.2.
DR AlphaFoldDB; Q8CHZ9; -.
DR SMR; Q8CHZ9; -.
DR IntAct; Q8CHZ9; 1.
DR STRING; 10090.ENSMUSP00000046017; -.
DR iPTMnet; Q8CHZ9; -.
DR PhosphoSitePlus; Q8CHZ9; -.
DR EPD; Q8CHZ9; -.
DR PaxDb; Q8CHZ9; -.
DR PeptideAtlas; Q8CHZ9; -.
DR PRIDE; Q8CHZ9; -.
DR ProteomicsDB; 287631; -.
DR DNASU; 545725; -.
DR Ensembl; ENSMUST00000044746; ENSMUSP00000046017; ENSMUSG00000040429.
DR Ensembl; ENSMUST00000117463; ENSMUSP00000113306; ENSMUSG00000040429.
DR GeneID; 545725; -.
DR KEGG; mmu:545725; -.
DR UCSC; uc008why.1; mouse.
DR CTD; 545725; -.
DR MGI; MGI:1918240; Mterf1a.
DR VEuPathDB; HostDB:ENSMUSG00000040429; -.
DR eggNOG; KOG1267; Eukaryota.
DR GeneTree; ENSGT00530000063817; -.
DR HOGENOM; CLU_058644_0_0_1; -.
DR InParanoid; Q8CHZ9; -.
DR OMA; YLAMEVF; -.
DR PhylomeDB; Q8CHZ9; -.
DR TreeFam; TF330821; -.
DR BioGRID-ORCS; 545725; 9 hits in 40 CRISPR screens.
DR ChiTaRS; Mterf1a; mouse.
DR PRO; PR:Q8CHZ9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CHZ9; protein.
DR Bgee; ENSMUSG00000040429; Expressed in embryonic post-anal tail and 62 other tissues.
DR Genevisible; Q8CHZ9; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:0032392; P:DNA geometric change; ISS:UniProtKB.
DR GO; GO:0006353; P:DNA-templated transcription, termination; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006393; P:termination of mitochondrial transcription; ISS:UniProtKB.
DR Gene3D; 1.25.70.10; -; 2.
DR InterPro; IPR003690; MTERF.
DR InterPro; IPR038538; MTERF_sf.
DR PANTHER; PTHR15437; PTHR15437; 1.
DR Pfam; PF02536; mTERF; 1.
DR SMART; SM00733; Mterf; 6.
PE 2: Evidence at transcript level;
KW DNA-binding; Mitochondrion; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Transcription termination;
KW Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..379
FT /note="Transcription termination factor 1a, mitochondrial"
FT /id="PRO_0000021780"
FT REGION 151..152
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 229..233
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 306..313
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 337..340
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 366..373
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 144
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 184
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 332
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="D -> G (in Ref. 3; AAH82778/AAH94442)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="A -> V (in Ref. 3; AAH82778/AAH94442)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="L -> I (in Ref. 3; AAH82778/AAH94442)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="D -> H (in Ref. 3; AAH82778/AAH94442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 43815 MW; 735133D605A04054 CRC64;
MASRNIWCVR RNFLFDLRDW MLQYSAEVFL KSISFRPFSA ECDSKDKESL EEEREDLLSN
LVTMGVDIDM ARRRQPGVFN KAVTNEQELK LFLLSKGASD KVIGSIISRY PRAITRTPES
LSKRWDLWRK IMASDLEIVN ILERSPESFF RSNNNLNLEN NIKFLCSVGL THKCLCRLLT
NAPRTFSNSL NLNKQMVEFL QETGMSLGHN DPRDFVRKII SKNPSILIQS TKRVKTNIEF
LQSTFNLNKR DLLLLICGPG ARILDLSNDC TKKNYTNIRE RLLSLGCSEE EVQRFVLSYL
NMVFLSEKKF NDKIDCLIEE KISASQIIEN PRILDSSINT LKTRIRELSH AGYDLSTSSI
ALLSWSQRRY EAKLKRLCG
