MTEF4_MOUSE
ID MTEF4_MOUSE Reviewed; 346 AA.
AC Q8BVN4; Q99LQ0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transcription termination factor 4, mitochondrial;
DE AltName: Full=Mitochondrial transcription termination factor 4;
DE AltName: Full=mTERF domain-containing protein 2;
DE Flags: Precursor;
GN Name=Mterf4; Synonyms=Mterfd2; OrderedLocusNames=HSPC096;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, 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 [3]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND CONDITIONAL KNOCKOUT.
RX PubMed=21531335; DOI=10.1016/j.cmet.2011.04.002;
RA Camara Y., Asin-Cayuela J., Park C.B., Metodiev M.D., Shi Y.,
RA Ruzzenente B., Kukat C., Habermann B., Wibom R., Hultenby K., Franz T.,
RA Erdjument-Bromage H., Tempst P., Hallberg B.M., Gustafsson C.M.,
RA Larsson N.G.;
RT "MTERF4 regulates translation by targeting the methyltransferase NSUN4 to
RT the mammalian mitochondrial ribosome.";
RL Cell Metab. 13:527-539(2011).
CC -!- FUNCTION: Regulator of mitochondrial ribosome biogenesis and
CC translation. Binds to mitochondrial ribosomal RNAs 16S, 12S and 7S (By
CC similarity). Targets NSUN4 RNA methyltransferase to the mitochondrial
CC large ribosomal subunit. {ECO:0000250, ECO:0000269|PubMed:21531335}.
CC -!- SUBUNIT: Heterodimer with NSUN4; this interaction may be required for
CC NSUN4 recruitment to the mitochondrial large ribosomal subunit.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21531335}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in liver,
CC followed by testis, kidney and brain. {ECO:0000269|PubMed:21531335}.
CC -!- DOMAIN: The MTERF repeats form a half-donut shaped, right-handed
CC superhelix, where the concave side displays a positively charged path
CC for nucleic acid interaction. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Ablation of the gene is not viable. At 8.5 dpc,
CC mutant homozygous embryos exhibit much reduced size, lack of heart and
CC no optic disks. Conditional knockout in heart leads to severe
CC mitochondrial cardiomyopathy. Premature death occurs at about 21 weeks
CC and decreased body weight is observed from 15 weeks until death.
CC {ECO:0000269|PubMed:21531335}.
CC -!- SIMILARITY: Belongs to the mTERF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02280.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH55877.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK077142; BAC36640.1; -; mRNA.
DR EMBL; BC002280; AAH02280.1; ALT_INIT; mRNA.
DR EMBL; BC055877; AAH55877.1; ALT_INIT; mRNA.
DR EMBL; BC064709; AAH64709.1; -; mRNA.
DR CCDS; CCDS35671.1; -.
DR RefSeq; NP_835152.1; NM_178051.4.
DR AlphaFoldDB; Q8BVN4; -.
DR SMR; Q8BVN4; -.
DR BioGRID; 213702; 3.
DR STRING; 10090.ENSMUSP00000027492; -.
DR iPTMnet; Q8BVN4; -.
DR PhosphoSitePlus; Q8BVN4; -.
DR EPD; Q8BVN4; -.
DR MaxQB; Q8BVN4; -.
DR PaxDb; Q8BVN4; -.
DR PeptideAtlas; Q8BVN4; -.
DR PRIDE; Q8BVN4; -.
DR ProteomicsDB; 291430; -.
DR Antibodypedia; 34543; 68 antibodies from 19 providers.
DR DNASU; 69821; -.
DR Ensembl; ENSMUST00000027492; ENSMUSP00000027492; ENSMUSG00000026273.
DR GeneID; 69821; -.
DR KEGG; mmu:69821; -.
DR UCSC; uc007cdo.1; mouse.
DR CTD; 130916; -.
DR MGI; MGI:1918355; Mterf4.
DR VEuPathDB; HostDB:ENSMUSG00000026273; -.
DR eggNOG; ENOG502RXUW; Eukaryota.
DR GeneTree; ENSGT00460000041648; -.
DR HOGENOM; CLU_069384_1_0_1; -.
DR InParanoid; Q8BVN4; -.
DR OMA; TNKNVWK; -.
DR OrthoDB; 1431133at2759; -.
DR PhylomeDB; Q8BVN4; -.
DR TreeFam; TF329452; -.
DR BioGRID-ORCS; 69821; 17 hits in 75 CRISPR screens.
DR ChiTaRS; Mterf4; mouse.
DR PRO; PR:Q8BVN4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BVN4; protein.
DR Bgee; ENSMUSG00000026273; Expressed in animal zygote and 248 other tissues.
DR ExpressionAtlas; Q8BVN4; baseline and differential.
DR Genevisible; Q8BVN4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; ISO:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0006390; P:mitochondrial transcription; IMP:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0042255; P:ribosome assembly; IMP:MGI.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.25.70.10; -; 1.
DR InterPro; IPR003690; MTERF.
DR InterPro; IPR038538; MTERF_sf.
DR PANTHER; PTHR13068; PTHR13068; 1.
DR Pfam; PF02536; mTERF; 1.
DR SMART; SM00733; Mterf; 4.
PE 2: Evidence at transcript level;
KW Mitochondrion; Reference proteome; Repeat; RNA-binding; rRNA processing;
KW Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 43..346
FT /note="Transcription termination factor 4, mitochondrial"
FT /id="PRO_0000255462"
FT REPEAT 142..172
FT /note="MTERF 1"
FT REPEAT 177..204
FT /note="MTERF 2"
FT REPEAT 209..239
FT /note="MTERF 3"
FT REPEAT 245..270
FT /note="MTERF 4"
FT REPEAT 290..318
FT /note="MTERF 5"
FT REGION 310..327
FT /note="Dimerization with NSUN4"
FT /evidence="ECO:0000250"
FT REGION 321..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..346
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 156
FT /note="S -> N (in Ref. 2; AAH02280/AAH55877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 40249 MW; EA34F8129804CC07 CRC64;
MASLGRQVPE WHRLLALSWA CLVRQTPHLR EQKQMSPSLS CKLTTVPGRG SFQEFSSITP
QKYMQEPENR TRLVQCLHEE QKPCVDPESL EPEKVIRSLQ DMGFAEAHIH SLFSIQPSVH
PQQLLGIVSE LLLLGLNPEP VFNALKKNPQ LLKLSSMQMK RRSSYLRKLG LGEGKLKRVL
SVCPEVFTMH QRDIDRVVKV LREKCLFTAQ HITDVLHRCP TVLQEDPNEL EYKFQYAYFR
MGLTHLDIVR TNFLQYSITK IKQRHIYLER LGRYQTPDKK GQTQIPNPSL RNILRVSEAE
FLARTACSSV EEFQVFKKLL DQEEEEESES HASEEEEEEE EEEELL
