MTEF3_DROME
ID MTEF3_DROME Reviewed; 354 AA.
AC Q9VPD5; Q06YR8;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Transcription termination factor 3, mitochondrial {ECO:0000305};
DE AltName: Full=Mitochondrial transcription termination factor 3 {ECO:0000303|PubMed:16787637};
DE Short=mTerf3;
DE Flags: Precursor;
GN Name=mTerf3 {ECO:0000303|PubMed:16787637, ECO:0000312|FlyBase:FBgn0037008};
GN ORFNames=CG5047 {ECO:0000312|FlyBase:FBgn0037008};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:ABD75710.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=16787637; DOI=10.1016/j.bbabio.2006.04.026;
RA Roberti M., Bruni F., Loguercio Polosa P., Manzari C., Gadaleta M.N.,
RA Cantatore P.;
RT "MTERF3, the most conserved member of the mTERF-family, is a modular factor
RT involved in mitochondrial protein synthesis.";
RL Biochim. Biophys. Acta 1757:1199-1206(2006).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABD75710.1};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABD75710.1};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAK93168.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93168.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAK93168.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 (By similarity). Regulator of mitochondrial ribosome biogenesis and
CC translation that is essential for development (PubMed:16787637,
CC PubMed:23300484). Required for normal mitochondrial transcription and
CC translation (PubMed:16787637, PubMed:23300484). Required for assembly
CC of mitochondrial respiratory complexes and normal mitochondrial
CC function (PubMed:23300484). Maintains 16S rRNA levels and functions in
CC mitochondrial ribosome assembly by regulating the biogenesis of the 39S
CC ribosomal subunit (PubMed:23300484). {ECO:0000250|UniProtKB:Q96E29,
CC ECO:0000269|PubMed:16787637, ECO:0000269|PubMed:23300484}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23300484}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown is pupal lethal. Larvae
CC display a delay in development and a decrease in body size. Display
CC progressive defects in mitochondrial respiratory chain capacity as well
CC as a decrease in the enzyme activity of all mitochondrial oxidative
CC phosphorylation complexes. Decrease in enzyme activity is particularly
CC severe in complex I and IV which also display a decrease in the levels
CC of their assembled complexes. Progressive reduction in 16S rRNA levels
CC and impaired assembly of the large (39S) mitochondrial ribosomal
CC subunit. Increase in mitochondrial DNA (mtDNA) transcription and
CC impaired mitochondrial translation. {ECO:0000269|PubMed:23300484}.
CC -!- SIMILARITY: Belongs to the mTERF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ414686; ABD75710.1; -; mRNA.
DR EMBL; AE014296; AAF51620.1; -; Genomic_DNA.
DR EMBL; AY051744; AAK93168.1; -; mRNA.
DR RefSeq; NP_649240.1; NM_140983.3.
DR AlphaFoldDB; Q9VPD5; -.
DR SMR; Q9VPD5; -.
DR IntAct; Q9VPD5; 5.
DR STRING; 7227.FBpp0077873; -.
DR PaxDb; Q9VPD5; -.
DR DNASU; 40279; -.
DR EnsemblMetazoa; FBtr0078215; FBpp0077873; FBgn0037008.
DR GeneID; 40279; -.
DR KEGG; dme:Dmel_CG5047; -.
DR UCSC; CG5047-RA; d. melanogaster.
DR CTD; 51001; -.
DR FlyBase; FBgn0037008; mTerf3.
DR VEuPathDB; VectorBase:FBgn0037008; -.
DR eggNOG; KOG1267; Eukaryota.
DR GeneTree; ENSGT00390000005801; -.
DR HOGENOM; CLU_042536_1_0_1; -.
DR InParanoid; Q9VPD5; -.
DR OMA; PRLMMIP; -.
DR OrthoDB; 1294087at2759; -.
DR PhylomeDB; Q9VPD5; -.
DR Reactome; R-DME-5205685; PINK1-PRKN Mediated Mitophagy.
DR SignaLink; Q9VPD5; -.
DR BioGRID-ORCS; 40279; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40279; -.
DR PRO; PR:Q9VPD5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0037008; Expressed in second segment of antenna (Drosophila) and 27 other tissues.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IDA:FlyBase.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IMP:FlyBase.
DR GO; GO:0061668; P:mitochondrial ribosome assembly; IBA:GO_Central.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:FlyBase.
DR GO; GO:1903108; P:regulation of mitochondrial transcription; IMP:FlyBase.
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; 5.
PE 2: Evidence at transcript level;
KW DNA-binding; Mitochondrion; Reference proteome; Ribosome biogenesis;
KW Transcription; Transcription regulation; Transit peptide.
FT TRANSIT 1..89
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 90..354
FT /note="Transcription termination factor 3, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000438919"
FT CONFLICT 42
FT /note="L -> V (in Ref. 1; ABD75710)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="V -> A (in Ref. 1; ABD75710)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="E -> G (in Ref. 1; ABD75710)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="P -> S (in Ref. 1; ABD75710)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="K -> I (in Ref. 1; ABD75710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 41267 MW; 24575D6D3CCE2EAE CRC64;
MFCSALRNIL RNSQNAAKNA TITSQIRNLR GQQSVHHEVE VLTSPGITTK QNDKKTEPAE
CEGSKEVALD FRNREAHVPS FNLAAYVNNS STLQQFLSLG VDLHSIERRK GLGDFVLKLD
FEKNVKPYIT FLVDQGVSPD DFGRMFTKNP LLFKEDLDDL QTRVNYLKSK RFSDEARQRI
LTQNPYWLMF STRRVDRRLG YFQKEFKLSG HDLRLLATRE PNAITYNMEH LRKSVFTLKE
EMGFNAKELS DLVVRKPRLL MIPPDDLVER FSYIHQDMGL PHAQIVQCPE LLASREFRLR
ERHEFLKLLG RAQYDPQKDL YISPKTIVEG NNFYFVRNVA KSDLETFDLF LKTR