MTEF3_HUMAN
ID MTEF3_HUMAN Reviewed; 417 AA.
AC Q96E29; B3KMG6; G3V130; Q9Y301;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transcription termination factor 3, mitochondrial;
DE AltName: Full=Mitochondrial transcription termination factor 3;
DE Short=mTERF3;
DE AltName: Full=mTERF domain-containing protein 1, mitochondrial;
DE Flags: Precursor;
GN Name=MTERF3; Synonyms=MTERFD1; ORFNames=CGI-12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Ovarian cancer;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [6]
RP FUNCTION, PARTIAL PROTEIN SEQUENCE, DNA-BINDING, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=17662942; DOI=10.1016/j.cell.2007.05.046;
RA Park C.B., Asin-Cayuela J., Camara Y., Shi Y., Pellegrini M., Gaspari M.,
RA Wibom R., Hultenby K., Erdjument-Bromage H., Tempst P., Falkenberg M.,
RA Gustafsson C.M., Larsson N.G.;
RT "MTERF3 is a negative regulator of mammalian mtDNA transcription.";
RL Cell 130:273-285(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 148-417, DOMAIN, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20430012; DOI=10.1016/j.bbrc.2010.04.130;
RA Spaahr H., Samuelsson T., Haellberg B.M., Gustafsson C.M.;
RT "Structure of mitochondrial transcription termination factor 3 reveals a
RT novel nucleic acid-binding domain.";
RL Biochem. Biophys. Res. Commun. 397:386-390(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=23300484; DOI=10.1371/journal.pgen.1003178;
RA Wredenberg A., Lagouge M., Bratic A., Metodiev M.D., Spaahr H., Mourier A.,
RA Freyer C., Ruzzenente B., Tain L., Groenke S., Baggio F., Kukat C.,
RA Kremmer E., Wibom R., Polosa P.L., Habermann B., Partridge L., Park C.B.,
RA Larsson N.G.;
RT "MTERF3 regulates mitochondrial ribosome biogenesis in invertebrates and
RT mammals.";
RL PLoS Genet. 9:E1003178-E1003178(2013).
CC -!- FUNCTION: Binds promoter DNA and regulates initiation of transcription
CC (PubMed:17662942). Required for normal mitochondrial transcription and
CC translation, and for normal assembly of mitochondrial respiratory
CC complexes. Required for normal mitochondrial function (By similarity).
CC Maintains 16S rRNA levels and functions in mitochondrial ribosome
CC assembly by regulating the biogenesis of the 39S ribosomal subunit (By
CC similarity). {ECO:0000250|UniProtKB:Q8R3J4,
CC ECO:0000269|PubMed:17662942}.
CC -!- INTERACTION:
CC Q96E29; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-7825321, EBI-11277970;
CC Q96E29; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-7825321, EBI-741181;
CC Q96E29; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-7825321, EBI-11522760;
CC Q96E29; P02654: APOC1; NbExp=3; IntAct=EBI-7825321, EBI-1220105;
CC Q96E29; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-7825321, EBI-714543;
CC Q96E29; Q9UGQ2: CACFD1; NbExp=3; IntAct=EBI-7825321, EBI-8652492;
CC Q96E29; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-7825321, EBI-2548702;
CC Q96E29; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-7825321, EBI-11522780;
CC Q96E29; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-7825321, EBI-711490;
CC Q96E29; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-7825321, EBI-3943864;
CC Q96E29; Q8IVP5: FUNDC1; NbExp=3; IntAct=EBI-7825321, EBI-3059266;
CC Q96E29; Q9NPR9: GPR108; NbExp=3; IntAct=EBI-7825321, EBI-11343451;
CC Q96E29; A8MV81: HIGD1C; NbExp=3; IntAct=EBI-7825321, EBI-12809676;
CC Q96E29; Q969L2: MAL2; NbExp=3; IntAct=EBI-7825321, EBI-944295;
CC Q96E29; Q96AL5: PBX3; NbExp=3; IntAct=EBI-7825321, EBI-741171;
CC Q96E29; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-7825321, EBI-17589229;
CC Q96E29; O15126: SCAMP1; NbExp=3; IntAct=EBI-7825321, EBI-954338;
CC Q96E29; Q9BYT1: SLC17A9; NbExp=3; IntAct=EBI-7825321, EBI-3940816;
CC Q96E29; P22732: SLC2A5; NbExp=3; IntAct=EBI-7825321, EBI-2825135;
CC Q96E29; Q9BRV3: SLC50A1; NbExp=3; IntAct=EBI-7825321, EBI-8634123;
CC Q96E29; Q9UNK0: STX8; NbExp=3; IntAct=EBI-7825321, EBI-727240;
CC Q96E29; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-7825321, EBI-12187159;
CC Q96E29; P08247: SYP; NbExp=3; IntAct=EBI-7825321, EBI-9071725;
CC Q96E29; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-7825321, EBI-2339195;
CC Q96E29; O95070: YIF1A; NbExp=3; IntAct=EBI-7825321, EBI-2799703;
CC Q96E29; Q8IVQ6: ZDHHC21; NbExp=3; IntAct=EBI-7825321, EBI-2849773;
CC Q96E29; O95159: ZFPL1; NbExp=3; IntAct=EBI-7825321, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17662942,
CC ECO:0000269|PubMed:23300484}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96E29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96E29-2; Sequence=VSP_021292;
CC Name=3;
CC IsoId=Q96E29-3; Sequence=VSP_053985;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, liver, kidney and
CC testis. Detected at lower levels in brain, spleen and lung.
CC {ECO:0000269|PubMed:17662942}.
CC -!- DOMAIN: Contains seven structural repeats of about 35 residues, where
CC each repeat contains three helices. The repeats form a superhelical
CC structure with a solenoid shape. {ECO:0000269|PubMed:20430012}.
CC -!- SIMILARITY: Belongs to the mTERF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27721.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF132946; AAD27721.1; ALT_FRAME; mRNA.
DR EMBL; AK001801; BAG50978.1; -; mRNA.
DR EMBL; AP003465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91752.1; -; Genomic_DNA.
DR EMBL; BC012995; AAH12995.2; -; mRNA.
DR CCDS; CCDS6270.1; -. [Q96E29-1]
DR RefSeq; NP_057026.3; NM_015942.4. [Q96E29-1]
DR PDB; 3M66; X-ray; 1.60 A; A=148-417.
DR PDBsum; 3M66; -.
DR AlphaFoldDB; Q96E29; -.
DR SMR; Q96E29; -.
DR BioGRID; 119209; 358.
DR IntAct; Q96E29; 52.
DR MINT; Q96E29; -.
DR STRING; 9606.ENSP00000287025; -.
DR GlyGen; Q96E29; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96E29; -.
DR PhosphoSitePlus; Q96E29; -.
DR BioMuta; MTERF3; -.
DR DMDM; 74731522; -.
DR EPD; Q96E29; -.
DR jPOST; Q96E29; -.
DR MassIVE; Q96E29; -.
DR MaxQB; Q96E29; -.
DR PaxDb; Q96E29; -.
DR PeptideAtlas; Q96E29; -.
DR PRIDE; Q96E29; -.
DR ProteomicsDB; 32240; -.
DR ProteomicsDB; 76367; -. [Q96E29-1]
DR ProteomicsDB; 76368; -. [Q96E29-2]
DR Antibodypedia; 1268; 63 antibodies from 21 providers.
DR DNASU; 51001; -.
DR Ensembl; ENST00000287025.4; ENSP00000287025.3; ENSG00000156469.9. [Q96E29-1]
DR Ensembl; ENST00000522822.5; ENSP00000430138.1; ENSG00000156469.9. [Q96E29-3]
DR GeneID; 51001; -.
DR KEGG; hsa:51001; -.
DR MANE-Select; ENST00000287025.4; ENSP00000287025.3; NM_015942.5; NP_057026.3.
DR UCSC; uc003yhr.3; human. [Q96E29-1]
DR CTD; 51001; -.
DR GeneCards; MTERF3; -.
DR HGNC; HGNC:24258; MTERF3.
DR HPA; ENSG00000156469; Low tissue specificity.
DR MIM; 616930; gene.
DR neXtProt; NX_Q96E29; -.
DR OpenTargets; ENSG00000156469; -.
DR PharmGKB; PA142671309; -.
DR VEuPathDB; HostDB:ENSG00000156469; -.
DR eggNOG; KOG1267; Eukaryota.
DR GeneTree; ENSGT00390000005801; -.
DR HOGENOM; CLU_042536_0_0_1; -.
DR InParanoid; Q96E29; -.
DR OMA; PRLMMIP; -.
DR OrthoDB; 1294087at2759; -.
DR PhylomeDB; Q96E29; -.
DR TreeFam; TF317943; -.
DR PathwayCommons; Q96E29; -.
DR Reactome; R-HSA-5205685; PINK1-PRKN Mediated Mitophagy.
DR SignaLink; Q96E29; -.
DR BioGRID-ORCS; 51001; 128 hits in 1083 CRISPR screens.
DR EvolutionaryTrace; Q96E29; -.
DR GenomeRNAi; 51001; -.
DR Pharos; Q96E29; Tdark.
DR PRO; PR:Q96E29; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96E29; protein.
DR Bgee; ENSG00000156469; Expressed in oocyte and 201 other tissues.
DR ExpressionAtlas; Q96E29; baseline and differential.
DR Genevisible; Q96E29; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0061668; P:mitochondrial ribosome assembly; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
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; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Mitochondrion; Reference proteome; Ribosome biogenesis; Transcription;
KW Transcription regulation; Transit peptide.
FT TRANSIT 1..68
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:17662942"
FT CHAIN 69..417
FT /note="Transcription termination factor 3, mitochondrial"
FT /id="PRO_0000255457"
FT REGION 69..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053985"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_021292"
FT VARIANT 396
FT /note="E -> G (in dbSNP:rs7461970)"
FT /id="VAR_053786"
FT CONFLICT 153
FT /note="S -> P (in Ref. 2; BAG50978)"
FT /evidence="ECO:0000305"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 255..269
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 327..338
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:3M66"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 387..392
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:3M66"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:3M66"
SQ 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
