MTEF1_HUMAN
ID MTEF1_HUMAN Reviewed; 399 AA.
AC Q99551; A4D1E3; Q32NF8; Q53H51; Q9BVR7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Transcription termination factor 1, mitochondrial;
DE AltName: Full=Mitochondrial transcription termination factor 1;
DE Short=mTERF;
DE Short=mTERF1;
DE Flags: Precursor;
GN Name=MTERF1; Synonyms=MTERF;
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 [MRNA], PROTEIN SEQUENCE OF 91-108; 118-141; 148-181
RP AND 254-260, AND MUTAGENESIS.
RX PubMed=9118945; DOI=10.1093/emboj/16.5.1066;
RA Fernandez-Silva P., Martinez-Azorin F., Micol V., Attardi G.;
RT "The human mitochondrial transcription termination factor (mTERF) is a
RT multizipper protein but binds to DNA as a monomer, with evidence pointing
RT to intramolecular leucine zipper interactions.";
RL EMBO J. 16:1066-1079(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-294.
RC TISSUE=Colon;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-231.
RC TISSUE=Brain, Placenta, and Uterus;
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 [7]
RP PHOSPHORYLATION.
RX PubMed=15087485; DOI=10.1093/nar/gkh528;
RA Prieto-Martin A., Montoya J., Martinez-Azorin F.;
RT "Phosphorylation of rat mitochondrial transcription termination factor
RT (mTERF) is required for transcription termination but not for binding to
RT DNA.";
RL Nucleic Acids Res. 32:2059-2068(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 57-396 IN COMPLEX WITH
RP DOUBLE-STRANDED DNA, DOMAIN, SUBUNIT, FUNCTION, AND MUTAGENESIS OF ARG-162;
RP ARG-169; ARG-202; PHE-243; ARG-251; TYR-288; ARG-350 AND ARG-387.
RX PubMed=20550934; DOI=10.1016/j.cell.2010.05.018;
RA Yakubovskaya E., Mejia E., Byrnes J., Hambardjieva E., Garcia-Diaz M.;
RT "Helix unwinding and base flipping enable human MTERF1 to terminate
RT mitochondrial transcription.";
RL Cell 141:982-993(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 56-399 IN COMPLEX WITH
RP DOUBLE-STRANDED DNA, DOMAIN, AND SUBUNIT.
RX PubMed=20543826; DOI=10.1038/nsmb.1859;
RA Jimenez-Menendez N., Fernandez-Millan P., Rubio-Cosials A., Arnan C.,
RA Montoya J., Jacobs H.T., Bernado P., Coll M., Uson I., Sola M.;
RT "Human mitochondrial mTERF wraps around DNA through a left-handed
RT superhelical tandem repeat.";
RL Nat. Struct. Mol. Biol. 17:891-893(2010).
CC -!- FUNCTION: Transcription termination factor. Binds to a 28 bp region
CC within the tRNA(Leu(uur)) gene at a position immediately adjacent to
CC and downstream of the 16S rRNA gene; this region comprises a tridecamer
CC sequence critical for directing accurate termination. Binds DNA along
CC the major grove and promotes DNA bending and partial unwinding.
CC Promotes base flipping. Transcription termination activity appears to
CC be polarized with highest specificity for transcripts initiated on the
CC light strand. {ECO:0000269|PubMed:20550934}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20543826,
CC ECO:0000269|PubMed:20550934}.
CC -!- INTERACTION:
CC Q99551; Q5F1R6: DNAJC21; NbExp=2; IntAct=EBI-2690033, EBI-2654581;
CC Q99551; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-2690033, EBI-10694905;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- DOMAIN: Contains nine structural repeats of about 35 residues, where
CC each repeat contains three helices. The repeats form a left-handed
CC superhelical assembly with a solenoid structure that wraps itself
CC around DNA. {ECO:0000269|PubMed:20543826, ECO:0000269|PubMed:20550934}.
CC -!- PTM: Phosphoprotein with mostly four phosphate groups. While the DNA-
CC binding activity is unaffected by the phosphorylation state, only the
CC phosphorylated form of the protein is active for termination activity.
CC Functioning seems to be regulated by phosphorylation.
CC {ECO:0000269|PubMed:15087485}.
CC -!- SIMILARITY: Belongs to the mTERF family. {ECO:0000305}.
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DR EMBL; Y09615; CAA70830.1; -; mRNA.
DR EMBL; AK222730; BAD96450.1; -; mRNA.
DR EMBL; AC003086; AAB83941.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24159.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76869.1; -; Genomic_DNA.
DR EMBL; BC000965; AAH00965.1; -; mRNA.
DR EMBL; BC108648; AAI08649.1; -; mRNA.
DR EMBL; BC130389; AAI30390.1; -; mRNA.
DR EMBL; BC130391; AAI30392.1; -; mRNA.
DR CCDS; CCDS5621.1; -.
DR RefSeq; NP_001288063.1; NM_001301134.1.
DR RefSeq; NP_001288064.1; NM_001301135.1.
DR RefSeq; NP_008911.1; NM_006980.4.
DR RefSeq; XP_005250650.1; XM_005250593.3.
DR RefSeq; XP_006716189.1; XM_006716126.3.
DR PDB; 3MVA; X-ray; 2.20 A; O=57-396.
DR PDB; 3MVB; X-ray; 2.79 A; O=57-396.
DR PDB; 3N6S; X-ray; 3.10 A; A=56-399.
DR PDB; 3N7Q; X-ray; 2.40 A; A=99-399.
DR PDB; 5CKY; X-ray; 2.62 A; O=73-396.
DR PDB; 5CO0; X-ray; 2.65 A; O=73-396.
DR PDB; 5CRJ; X-ray; 2.59 A; O=73-396.
DR PDB; 5CRK; X-ray; 2.48 A; O=73-396.
DR PDBsum; 3MVA; -.
DR PDBsum; 3MVB; -.
DR PDBsum; 3N6S; -.
DR PDBsum; 3N7Q; -.
DR PDBsum; 5CKY; -.
DR PDBsum; 5CO0; -.
DR PDBsum; 5CRJ; -.
DR PDBsum; 5CRK; -.
DR AlphaFoldDB; Q99551; -.
DR SMR; Q99551; -.
DR BioGRID; 113691; 14.
DR IntAct; Q99551; 16.
DR MINT; Q99551; -.
DR STRING; 9606.ENSP00000248643; -.
DR iPTMnet; Q99551; -.
DR PhosphoSitePlus; Q99551; -.
DR BioMuta; MTERF1; -.
DR DMDM; 12644536; -.
DR EPD; Q99551; -.
DR jPOST; Q99551; -.
DR MassIVE; Q99551; -.
DR MaxQB; Q99551; -.
DR PaxDb; Q99551; -.
DR PeptideAtlas; Q99551; -.
DR PRIDE; Q99551; -.
DR ProteomicsDB; 78325; -.
DR Antibodypedia; 29914; 200 antibodies from 26 providers.
DR DNASU; 7978; -.
DR Ensembl; ENST00000351870.8; ENSP00000248643.3; ENSG00000127989.14.
DR GeneID; 7978; -.
DR KEGG; hsa:7978; -.
DR MANE-Select; ENST00000351870.8; ENSP00000248643.3; NM_006980.5; NP_008911.1.
DR UCSC; uc003ulc.2; human.
DR CTD; 7978; -.
DR DisGeNET; 7978; -.
DR GeneCards; MTERF1; -.
DR HGNC; HGNC:21463; MTERF1.
DR HPA; ENSG00000127989; Low tissue specificity.
DR MIM; 602318; gene.
DR neXtProt; NX_Q99551; -.
DR OpenTargets; ENSG00000127989; -.
DR PharmGKB; PA142671308; -.
DR VEuPathDB; HostDB:ENSG00000127989; -.
DR eggNOG; KOG1267; Eukaryota.
DR GeneTree; ENSGT00530000063817; -.
DR InParanoid; Q99551; -.
DR OMA; LDYSTQN; -.
DR OrthoDB; 713769at2759; -.
DR PhylomeDB; Q99551; -.
DR TreeFam; TF330821; -.
DR PathwayCommons; Q99551; -.
DR Reactome; R-HSA-163316; Mitochondrial transcription termination.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR SignaLink; Q99551; -.
DR BioGRID-ORCS; 7978; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; MTERF1; human.
DR EvolutionaryTrace; Q99551; -.
DR GeneWiki; MTERF; -.
DR GenomeRNAi; 7978; -.
DR Pharos; Q99551; Tbio.
DR PRO; PR:Q99551; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q99551; protein.
DR Bgee; ENSG00000127989; Expressed in corpus callosum and 107 other tissues.
DR ExpressionAtlas; Q99551; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032392; P:DNA geometric change; IDA:UniProtKB.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006393; P:termination of mitochondrial transcription; IDA:UniProtKB.
DR Gene3D; 1.25.70.10; -; 2.
DR InterPro; IPR003690; MTERF.
DR InterPro; IPR038538; MTERF_sf.
DR PANTHER; PTHR15437; PTHR15437; 1.
DR Pfam; PF02536; mTERF; 1.
DR SMART; SM00733; Mterf; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Mitochondrion;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transcription termination; Transit peptide.
FT TRANSIT 1..57
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 58..399
FT /note="Transcription termination factor 1, mitochondrial"
FT /id="PRO_0000021779"
FT REGION 169..170
FT /note="Interaction with DNA"
FT REGION 247..251
FT /note="Interaction with DNA"
FT REGION 324..331
FT /note="Interaction with DNA"
FT REGION 355..358
FT /note="Interaction with DNA"
FT REGION 384..391
FT /note="Interaction with DNA"
FT SITE 162
FT /note="Interaction with DNA"
FT SITE 202
FT /note="Interaction with DNA"
FT SITE 243
FT /note="Interaction with DNA"
FT SITE 288
FT /note="Interaction with DNA"
FT SITE 350
FT /note="Interaction with DNA"
FT VARIANT 231
FT /note="A -> T (in dbSNP:rs17856025)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_053785"
FT VARIANT 294
FT /note="A -> T (in dbSNP:rs10266424)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_024237"
FT MUTAGEN 162
FT /note="R->A: Reduces affinity for cognate DNA; when
FT associated with A-243 and A-288."
FT /evidence="ECO:0000269|PubMed:20550934"
FT MUTAGEN 169
FT /note="R->A: Strongly reduces affinity for DNA. Strongly
FT reduces transcription termination."
FT /evidence="ECO:0000269|PubMed:20550934"
FT MUTAGEN 202
FT /note="R->A: Strongly reduces affinity for DNA. Strongly
FT reduces transcription termination."
FT /evidence="ECO:0000269|PubMed:20550934"
FT MUTAGEN 243
FT /note="F->A: Reduces affinity for cognate DNA; when
FT associated with A-162 and A-288."
FT /evidence="ECO:0000269|PubMed:20550934"
FT MUTAGEN 251
FT /note="R->A: Strongly reduces transcription termination."
FT /evidence="ECO:0000269|PubMed:20550934"
FT MUTAGEN 288
FT /note="Y->A: Reduces affinity for cognate DNA; when
FT associated with A-162 and A-243."
FT /evidence="ECO:0000269|PubMed:20550934"
FT MUTAGEN 350
FT /note="R->A: Reduces transcription termination."
FT /evidence="ECO:0000269|PubMed:20550934"
FT MUTAGEN 387
FT /note="R->A: Strongly reduces affinity for cognate DNA.
FT Strongly reduces transcription termination."
FT /evidence="ECO:0000269|PubMed:20550934"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:3MVA"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 208..224
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:3MVA"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:3MVA"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:3MVA"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 342..347
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:3MVA"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:3MVA"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 378..382
FT /evidence="ECO:0007829|PDB:3MVA"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:3MVA"
SQ SEQUENCE 399 AA; 45778 MW; A0C6CE4A8498526E CRC64;
MQSLSLGQTS ISKGLNYLTI MAPGNLWHMR NNFLFGSRCW MTRFSAENIF KSVSFRLFGV
KCHNTDSEPL KNEDLLKNLL TMGVDIDMAR KRQPGVFHRM ITNEQDLKMF LLSKGASKEV
IASIISRYPR AITRTPENLS KRWDLWRKIV TSDLEIVNIL ERSPESFFRS NNNLNLENNI
KFLYSVGLTR KCLCRLLTNA PRTFSNSLDL NKQMVEFLQA AGLSLGHNDP ADFVRKIIFK
NPFILIQSTK RVKANIEFLR STFNLNSEEL LVLICGPGAE ILDLSNDYAR RSYANIKEKL
FSLGCTEEEV QKFVLSYPDV IFLAEKKFND KIDCLMEENI SISQIIENPR VLDSSISTLK
SRIKELVNAG CNLSTLNITL LSWSKKRYEA KLKKLSRFA
