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Transcription termination factor 3, mitochondrial (Mitochondrial transcription termination factor 3) (mTERF3) (mTERF domain-containing protein 1, mitochondrial)

 MTEF3_HUMAN             Reviewed;         417 AA.
Q96E29; B3KMG6; G3V130; Q9Y301;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
23-MAY-2018, entry version 128.
RecName: Full=Transcription termination factor 3, mitochondrial;
AltName: Full=Mitochondrial transcription termination factor 3;
Short=mTERF3;
AltName: Full=mTERF domain-containing protein 1, mitochondrial;
Flags: Precursor;
Name=MTERF3; Synonyms=MTERFD1; ORFNames=CGI-12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Ovarian cancer;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, PARTIAL PROTEIN SEQUENCE, DNA-BINDING, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=17662942; DOI=10.1016/j.cell.2007.05.046;
Park C.B., Asin-Cayuela J., Camara Y., Shi Y., Pellegrini M.,
Gaspari M., Wibom R., Hultenby K., Erdjument-Bromage H., Tempst P.,
Falkenberg M., Gustafsson C.M., Larsson N.G.;
"MTERF3 is a negative regulator of mammalian mtDNA transcription.";
Cell 130:273-285(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 148-417, DOMAIN, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20430012; DOI=10.1016/j.bbrc.2010.04.130;
Spaahr H., Samuelsson T., Haellberg B.M., Gustafsson C.M.;
"Structure of mitochondrial transcription termination factor 3 reveals
a novel nucleic acid-binding domain.";
Biochem. Biophys. Res. Commun. 397:386-390(2010).
[9]
SUBCELLULAR LOCATION.
PubMed=23300484; DOI=10.1371/journal.pgen.1003178;
Wredenberg A., Lagouge M., Bratic A., Metodiev M.D., Spaahr H.,
Mourier A., Freyer C., Ruzzenente B., Tain L., Groenke S., Baggio F.,
Kukat C., Kremmer E., Wibom R., Polosa P.L., Habermann B.,
Partridge L., Park C.B., Larsson N.G.;
"MTERF3 regulates mitochondrial ribosome biogenesis in invertebrates
and mammals.";
PLoS Genet. 9:E1003178-E1003178(2013).
-!- FUNCTION: Binds promoter DNA and regulates initiation of
transcription (PubMed:17662942). Required for normal mitochondrial
transcription and translation, and for normal assembly of
mitochondrial respiratory complexes. Required for normal
mitochondrial function (By similarity). Maintains 16S rRNA levels
and functions in mitochondrial ribosome assembly by regulating the
biogenesis of the 39S ribosomal subunit (By similarity).
{ECO:0000250|UniProtKB:Q8R3J4, ECO:0000269|PubMed:17662942}.
-!- INTERACTION:
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-7825321, EBI-741181;
Q15041:ARL6IP1; NbExp=3; IntAct=EBI-7825321, EBI-714543;
Q96DZ9:CMTM5; NbExp=3; IntAct=EBI-7825321, EBI-2548702;
Q8IVP5:FUNDC1; NbExp=3; IntAct=EBI-7825321, EBI-3059266;
P08247:SYP; NbExp=4; IntAct=EBI-7825321, EBI-9071725;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17662942,
ECO:0000269|PubMed:23300484}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96E29-1; Sequence=Displayed;
Name=2;
IsoId=Q96E29-2; Sequence=VSP_021292;
Name=3;
IsoId=Q96E29-3; Sequence=VSP_053985;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in heart, liver, kidney and
testis. Detected at lower levels in brain, spleen and lung.
{ECO:0000269|PubMed:17662942}.
-!- DOMAIN: Contains seven structural repeats of about 35 residues,
where each repeat contains three helices. The repeats form a
superhelical structure with a solenoid shape.
{ECO:0000269|PubMed:20430012}.
-!- SIMILARITY: Belongs to the mTERF family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD27721.1; Type=Frameshift; Positions=261, 262; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF132946; AAD27721.1; ALT_FRAME; mRNA.
EMBL; AK001801; BAG50978.1; -; mRNA.
EMBL; AP003465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471060; EAW91752.1; -; Genomic_DNA.
EMBL; BC012995; AAH12995.2; -; mRNA.
CCDS; CCDS6270.1; -. [Q96E29-1]
RefSeq; NP_057026.3; NM_015942.4. [Q96E29-1]
UniGene; Hs.308613; -.
PDB; 3M66; X-ray; 1.60 A; A=148-417.
PDBsum; 3M66; -.
ProteinModelPortal; Q96E29; -.
SMR; Q96E29; -.
BioGrid; 119209; 41.
IntAct; Q96E29; 17.
MINT; Q96E29; -.
STRING; 9606.ENSP00000287025; -.
iPTMnet; Q96E29; -.
PhosphoSitePlus; Q96E29; -.
BioMuta; MTERFD1; -.
DMDM; 74731522; -.
EPD; Q96E29; -.
MaxQB; Q96E29; -.
PaxDb; Q96E29; -.
PeptideAtlas; Q96E29; -.
PRIDE; Q96E29; -.
DNASU; 51001; -.
Ensembl; ENST00000287025; ENSP00000287025; ENSG00000156469. [Q96E29-1]
Ensembl; ENST00000522822; ENSP00000430138; ENSG00000156469. [Q96E29-3]
GeneID; 51001; -.
KEGG; hsa:51001; -.
UCSC; uc003yhr.3; human. [Q96E29-1]
CTD; 51001; -.
EuPathDB; HostDB:ENSG00000156469.8; -.
GeneCards; MTERF3; -.
HGNC; HGNC:24258; MTERF3.
HPA; HPA002966; -.
MIM; 616930; gene.
neXtProt; NX_Q96E29; -.
OpenTargets; ENSG00000156469; -.
PharmGKB; PA142671309; -.
eggNOG; KOG1267; Eukaryota.
eggNOG; ENOG410XT49; LUCA.
GeneTree; ENSGT00390000005801; -.
HOGENOM; HOG000044443; -.
HOVERGEN; HBG062577; -.
InParanoid; Q96E29; -.
KO; K15032; -.
OMA; NNFYFVR; -.
OrthoDB; EOG091G0AZ7; -.
PhylomeDB; Q96E29; -.
TreeFam; TF317943; -.
Reactome; R-HSA-5205685; Pink/Parkin Mediated Mitophagy.
EvolutionaryTrace; Q96E29; -.
GenomeRNAi; 51001; -.
PRO; PR:Q96E29; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000156469; -.
CleanEx; HS_MTERFD1; -.
ExpressionAtlas; Q96E29; baseline and differential.
Genevisible; Q96E29; HS.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro.
GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0032502; P:developmental process; IBA:GO_Central.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0042255; P:ribosome assembly; IBA:GO_Central.
GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.25.70.10; -; 1.
InterPro; IPR003690; MTERF.
InterPro; IPR038538; MTERF_sf.
Pfam; PF02536; mTERF; 1.
SMART; SM00733; Mterf; 6.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; DNA-binding; Mitochondrion; Polymorphism;
Reference proteome; Ribosome biogenesis; Transcription;
Transcription regulation; Transit peptide.
TRANSIT 1 68 Mitochondrion.
{ECO:0000269|PubMed:17662942}.
CHAIN 69 417 Transcription termination factor 3,
mitochondrial.
/FTId=PRO_0000255457.
VAR_SEQ 1 121 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053985.
VAR_SEQ 1 90 Missing (in isoform 2).
{ECO:0000303|PubMed:10810093}.
/FTId=VSP_021292.
VARIANT 396 396 E -> G (in dbSNP:rs7461970).
/FTId=VAR_053786.
CONFLICT 153 153 S -> P (in Ref. 2; BAG50978).
{ECO:0000305}.
HELIX 149 161 {ECO:0000244|PDB:3M66}.
HELIX 166 169 {ECO:0000244|PDB:3M66}.
HELIX 173 180 {ECO:0000244|PDB:3M66}.
HELIX 184 187 {ECO:0000244|PDB:3M66}.
HELIX 189 198 {ECO:0000244|PDB:3M66}.
HELIX 202 204 {ECO:0000244|PDB:3M66}.
HELIX 205 211 {ECO:0000244|PDB:3M66}.
HELIX 215 217 {ECO:0000244|PDB:3M66}.
HELIX 220 232 {ECO:0000244|PDB:3M66}.
HELIX 237 246 {ECO:0000244|PDB:3M66}.
HELIX 250 252 {ECO:0000244|PDB:3M66}.
HELIX 255 269 {ECO:0000244|PDB:3M66}.
HELIX 273 282 {ECO:0000244|PDB:3M66}.
HELIX 284 287 {ECO:0000244|PDB:3M66}.
HELIX 292 303 {ECO:0000244|PDB:3M66}.
HELIX 309 318 {ECO:0000244|PDB:3M66}.
HELIX 320 323 {ECO:0000244|PDB:3M66}.
HELIX 327 338 {ECO:0000244|PDB:3M66}.
HELIX 345 350 {ECO:0000244|PDB:3M66}.
HELIX 352 356 {ECO:0000244|PDB:3M66}.
HELIX 359 371 {ECO:0000244|PDB:3M66}.
STRAND 381 383 {ECO:0000244|PDB:3M66}.
HELIX 387 392 {ECO:0000244|PDB:3M66}.
HELIX 395 401 {ECO:0000244|PDB:3M66}.
HELIX 407 414 {ECO:0000244|PDB:3M66}.
SEQUENCE 417 AA; 47971 MW; 2062EFE902584696 CRC64;
MALSAQQIPR WFNSVKLRSL INAAQLTKRF TRPARTLLHG FSAQPQISSD NCFLQWGFKT
YRTSSLWNSS QSTSSSSQEN NSAQSSLLPS MNEQSQKTQN ISSFDSELFL EELDELPPLS
PMQPISEEEA IQIIADPPLP PASFTLRDYV DHSETLQKLV LLGVDLSKIE KHPEAANLLL
RLDFEKDIKQ MLLFLKDVGI EDNQLGAFLT KNHAIFSEDL ENLKTRVAYL HSKNFSKADV
AQMVRKAPFL LNFSVERLDN RLGFFQKELE LSVKKTRDLV VRLPRLLTGS LEPVKENMKV
YRLELGFKHN EIQHMITRIP KMLTANKMKL TETFDFVHNV MSIPHHIIVK FPQVFNTRLF
KVKERHLFLT YLGRAQYDPA KPNYISLDKL VSIPDEIFCE EIAKASVQDF EKFLKTL


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