Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription termination factor 1a, mitochondrial

Gene

Mterf1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Transcription termination factor. Binds to a 28 bp region within the tRNA(Leu(uur)) gene at a position immediately adjacent to and downstream of the 16S rRNA gene; this region comprises a tridecamer sequence critical for directing accurate termination. Binds DNA along the major grove and promotes DNA bending and partial unwinding. Promotes base flipping. Transcription termination activity appears to be polarized with highest specificity for transcripts initiated on the light strand.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Transcription termination

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-163316. Mitochondrial transcription termination.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription termination factor 1a, mitochondrial
Alternative name(s):
Mitochondrial transcription termination factor 1a
Short name:
mTERF1a
Gene namesi
Name:Mterf1a
Synonyms:Mterf, Mterf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1918240. Mterf1a.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: GO_Central
  • mitochondrial nucleoid Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Double knockout of Mterf1a and Mterf1b results in viable animals with no gross phenotype, and normal oxidative phosphorylation capacity. Steady-state mitochondrial DNA levels are normal. There are subtle effects on levels of mitochondrial transcripts: transcripts initiated at the light strand promoter and also downstream of the MTERF binding site are increased, levels of 7S RNA are reduced, while levels of other mitochondrial transcripts are normal.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionSequence analysisAdd
BLAST
Chaini38 – 379342Transcription termination factor 1a, mitochondrialPRO_0000021780Add
BLAST

Post-translational modificationi

Phosphoprotein with mostly four phosphate groups. While the DNA-binding activity is unaffected by the phosphorylation state, only the phosphorylated form of the protein is active for termination activity. Functioning seems to be regulated by phosphorylation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8CHZ9.
PaxDbiQ8CHZ9.
PeptideAtlasiQ8CHZ9.
PRIDEiQ8CHZ9.

PTM databases

iPTMnetiQ8CHZ9.
PhosphoSiteiQ8CHZ9.

Expressioni

Tissue specificityi

Predominantly expressed in heart and liver, with extremely low levels in other tissues (PubMed:15582606). Expressed strongly in the heart and at lower levels in brain, liver and kidney (PubMed:23562081).2 Publications

Gene expression databases

BgeeiQ8CHZ9.
CleanExiMM_MTERF.
GenevisibleiQ8CHZ9. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei144 – 1441Interaction with DNABy similarity
Sitei184 – 1841Interaction with DNABy similarity
Sitei332 – 3321Interaction with DNABy similarity

Protein-protein interaction databases

IntActiQ8CHZ9. 1 interaction.
STRINGi10090.ENSMUSP00000046017.

Structurei

3D structure databases

ProteinModelPortaliQ8CHZ9.
SMRiQ8CHZ9. Positions 55-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 1522Interaction with DNABy similarity
Regioni229 – 2335Interaction with DNABy similarity
Regioni306 – 3138Interaction with DNABy similarity
Regioni337 – 3404Interaction with DNABy similarity
Regioni366 – 3738Interaction with DNABy similarity

Domaini

Contains nine structural repeats of about 35 residues, where each repeat contains three helices. The repeats form a left-handed superhelical assembly with a solenoid structure that wraps itself around DNA (By similarity).By similarity

Sequence similaritiesi

Belongs to the mTERF family.Curated

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG1267. Eukaryota.
ENOG410XT49. LUCA.
GeneTreeiENSGT00530000063817.
HOGENOMiHOG000252957.
HOVERGENiHBG052524.
InParanoidiQ8CHZ9.
KOiK15031.
OMAiISQITAC.
OrthoDBiEOG74FF1K.
PhylomeDBiQ8CHZ9.
TreeFamiTF330821.

Family and domain databases

InterProiIPR003690. MTERF.
[Graphical view]
PfamiPF02536. mTERF. 1 hit.
[Graphical view]
SMARTiSM00733. Mterf. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8CHZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRNIWCVR RNFLFDLRDW MLQYSAEVFL KSISFRPFSA ECDSKDKESL
60 70 80 90 100
EEEREDLLSN LVTMGVDIDM ARRRQPGVFN KAVTNEQELK LFLLSKGASD
110 120 130 140 150
KVIGSIISRY PRAITRTPES LSKRWDLWRK IMASDLEIVN ILERSPESFF
160 170 180 190 200
RSNNNLNLEN NIKFLCSVGL THKCLCRLLT NAPRTFSNSL NLNKQMVEFL
210 220 230 240 250
QETGMSLGHN DPRDFVRKII SKNPSILIQS TKRVKTNIEF LQSTFNLNKR
260 270 280 290 300
DLLLLICGPG ARILDLSNDC TKKNYTNIRE RLLSLGCSEE EVQRFVLSYL
310 320 330 340 350
NMVFLSEKKF NDKIDCLIEE KISASQIIEN PRILDSSINT LKTRIRELSH
360 370
AGYDLSTSSI ALLSWSQRRY EAKLKRLCG
Length:379
Mass (Da):43,815
Last modified:March 1, 2003 - v1
Checksum:i735133D605A04054
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191D → G in AAH82778 (PubMed:15489334).Curated
Sequence conflicti19 – 191D → G in AAH94442 (PubMed:15489334).Curated
Sequence conflicti40 – 401A → V in AAH82778 (PubMed:15489334).Curated
Sequence conflicti40 – 401A → V in AAH94442 (PubMed:15489334).Curated
Sequence conflicti91 – 911L → I in AAH82778 (PubMed:15489334).Curated
Sequence conflicti91 – 911L → I in AAH94442 (PubMed:15489334).Curated
Sequence conflicti126 – 1261D → H in AAH82778 (PubMed:15489334).Curated
Sequence conflicti126 – 1261D → H in AAH94442 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY726770 mRNA. Translation: AAU26065.1.
AC027653 Genomic DNA. No translation available.
BC038058 mRNA. Translation: AAH38058.1.
BC051251 mRNA. Translation: AAH51251.1.
BC082778 mRNA. Translation: AAH82778.1.
BC094442 mRNA. Translation: AAH94442.1.
AK049308 mRNA. Translation: BAC33673.1.
CCDSiCCDS39003.1.
RefSeqiNP_001013041.2. NM_001013023.2.
NP_742147.1. NM_172135.2.
UniGeneiMm.489094.
Mm.99593.

Genome annotation databases

EnsembliENSMUST00000044746; ENSMUSP00000046017; ENSMUSG00000040429.
ENSMUST00000117463; ENSMUSP00000113306; ENSMUSG00000040429.
GeneIDi545725.
KEGGimmu:545725.
UCSCiuc008why.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY726770 mRNA. Translation: AAU26065.1.
AC027653 Genomic DNA. No translation available.
BC038058 mRNA. Translation: AAH38058.1.
BC051251 mRNA. Translation: AAH51251.1.
BC082778 mRNA. Translation: AAH82778.1.
BC094442 mRNA. Translation: AAH94442.1.
AK049308 mRNA. Translation: BAC33673.1.
CCDSiCCDS39003.1.
RefSeqiNP_001013041.2. NM_001013023.2.
NP_742147.1. NM_172135.2.
UniGeneiMm.489094.
Mm.99593.

3D structure databases

ProteinModelPortaliQ8CHZ9.
SMRiQ8CHZ9. Positions 55-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CHZ9. 1 interaction.
STRINGi10090.ENSMUSP00000046017.

PTM databases

iPTMnetiQ8CHZ9.
PhosphoSiteiQ8CHZ9.

Proteomic databases

EPDiQ8CHZ9.
PaxDbiQ8CHZ9.
PeptideAtlasiQ8CHZ9.
PRIDEiQ8CHZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044746; ENSMUSP00000046017; ENSMUSG00000040429.
ENSMUST00000117463; ENSMUSP00000113306; ENSMUSG00000040429.
GeneIDi545725.
KEGGimmu:545725.
UCSCiuc008why.1. mouse.

Organism-specific databases

CTDi545725.
MGIiMGI:1918240. Mterf1a.

Phylogenomic databases

eggNOGiKOG1267. Eukaryota.
ENOG410XT49. LUCA.
GeneTreeiENSGT00530000063817.
HOGENOMiHOG000252957.
HOVERGENiHBG052524.
InParanoidiQ8CHZ9.
KOiK15031.
OMAiISQITAC.
OrthoDBiEOG74FF1K.
PhylomeDBiQ8CHZ9.
TreeFamiTF330821.

Enzyme and pathway databases

ReactomeiR-MMU-163316. Mitochondrial transcription termination.

Miscellaneous databases

PROiQ8CHZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CHZ9.
CleanExiMM_MTERF.
GenevisibleiQ8CHZ9. MM.

Family and domain databases

InterProiIPR003690. MTERF.
[Graphical view]
PfamiPF02536. mTERF. 1 hit.
[Graphical view]
SMARTiSM00733. Mterf. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of mouse mTERF encoding a mitochondrial transcriptional termination factor."
    Li X., Zhang L.S., Guan M.-X.
    Biochem. Biophys. Res. Commun. 326:505-510(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: SWR/J.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II and FVB/N.
    Tissue: Colon, Eye and Mammary tumor.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-271.
    Strain: C57BL/6J.
  5. "MTERF1 binds mtDNA to prevent transcriptional interference at the light-strand promoter but is dispensable for rRNA gene transcription regulation."
    Terzioglu M., Ruzzenente B., Harmel J., Mourier A., Jemt E., Lopez M.D., Kukat C., Stewart J.B., Wibom R., Meharg C., Habermann B., Falkenberg M., Gustafsson C.M., Park C.B., Larsson N.G.
    Cell Metab. 17:618-626(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMTF1A_MOUSE
AccessioniPrimary (citable) accession number: Q8CHZ9
Secondary accession number(s): Q63ZX5, Q8C7T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.