MFT1_YEAST
ID MFT1_YEAST Reviewed; 392 AA.
AC P33441; D6VZB1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=THO complex subunit MFT1;
DE AltName: Full=Mitochondrial fusion target protein 1;
GN Name=MFT1; OrderedLocusNames=YML062C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8458428; DOI=10.1016/0014-5793(93)80076-7;
RA Ito M., Yasui A., Komamine A.;
RT "Precise mapping and molecular characterization of the MFT1 gene involved
RT in import of a fusion protein into mitochondria in Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 320:125-129(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN THO COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11060033; DOI=10.1093/emboj/19.21.5824;
RA Chavez S., Beilharz T., Rondon A.G., Erdjument-Bromage H., Tempst P.,
RA Svejstrup J.Q., Lithgow T., Aguilera A.;
RT "A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2,
RT connects transcription elongation with mitotic recombination in
RT Saccharomyces cerevisiae.";
RL EMBO J. 19:5824-5834(2000).
RN [5]
RP FUNCTION.
RX PubMed=12093753; DOI=10.1093/emboj/cdf335;
RA Jimeno S., Rondon A.G., Luna R., Aguilera A.;
RT "The yeast THO complex and mRNA export factors link RNA metabolism with
RT transcription and genome instability.";
RL EMBO J. 21:3526-3535(2002).
RN [6]
RP IDENTIFICATION IN TREX COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11979277; DOI=10.1038/nature746;
RA Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M.,
RA Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R.,
RA Hurt E.;
RT "TREX is a conserved complex coupling transcription with messenger RNA
RT export.";
RL Nature 417:304-308(2002).
RN [7]
RP FUNCTION.
RX PubMed=12871933; DOI=10.1074/jbc.m305718200;
RA Rondon A.G., Jimeno S., Garcia-Rubio M., Aguilera A.;
RT "Molecular evidence that the eukaryotic THO/TREX complex is required for
RT efficient transcription elongation.";
RL J. Biol. Chem. 278:39037-39043(2003).
RN [8]
RP FUNCTION.
RX PubMed=14527416; DOI=10.1016/j.molcel.2003.08.010;
RA Huertas P., Aguilera A.;
RT "Cotranscriptionally formed DNA:RNA hybrids mediate transcription
RT elongation impairment and transcription-associated recombination.";
RL Mol. Cell 12:711-721(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP FUNCTION.
RX PubMed=15192704; DOI=10.1038/sj.emboj.7600261;
RA Abruzzi K.C., Lacadie S., Rosbash M.;
RT "Biochemical analysis of TREX complex recruitment to intronless and intron-
RT containing yeast genes.";
RL EMBO J. 23:2620-2631(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component the THO subcomplex of the TREX complex, which
CC operates in coupling transcription elongation to mRNA export. The THO
CC complex is recruited to transcribed genes and moves along the gene with
CC the elongating polymerase during transcription. THO is important for
CC stabilizing nascent RNA in the RNA polymerase II elongation complex by
CC preventing formation of DNA:RNA hybrids behind the elongating
CC polymerase. It functions in cotranscriptional formation of an export-
CC competent messenger ribonucleoprotein particle (mRNP) by facilitating
CC the loading of ATP-dependent RNA helicase SUB2 and the mRNA export
CC factor YRA1 along the nascent mRNA. {ECO:0000269|PubMed:12093753,
CC ECO:0000269|PubMed:12871933, ECO:0000269|PubMed:14527416,
CC ECO:0000269|PubMed:15192704}.
CC -!- SUBUNIT: Component of the THO complex, which is composed of HPR1, MFT1,
CC THO2 and THP2. Together with SUB2, TEX1 and YRA1, THO forms the
CC transcription/export (TREX) complex. THO associates with DNA and RNA in
CC vitro. {ECO:0000269|PubMed:11060033, ECO:0000269|PubMed:11979277}.
CC -!- INTERACTION:
CC P33441; O13539: THP2; NbExp=4; IntAct=EBI-10841, EBI-30898;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11060033,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5910 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- CAUTION: Was originally thought to be involved in mitochondrial protein
CC import. {ECO:0000305|PubMed:8458428}.
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DR EMBL; S57517; AAB26005.1; -; Genomic_DNA.
DR EMBL; Z38114; CAA86259.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09835.1; -; Genomic_DNA.
DR PIR; S32405; S32405.
DR RefSeq; NP_013649.1; NM_001182421.1.
DR PDB; 7APX; EM; 3.40 A; D=1-392.
DR PDB; 7AQO; EM; 4.50 A; D/I=1-392.
DR PDB; 7LUV; EM; 3.70 A; D=1-256.
DR PDBsum; 7APX; -.
DR PDBsum; 7AQO; -.
DR PDBsum; 7LUV; -.
DR AlphaFoldDB; P33441; -.
DR SMR; P33441; -.
DR BioGRID; 35104; 257.
DR ComplexPortal; CPX-1792; THO complex.
DR ComplexPortal; CPX-1793; TREX complex.
DR DIP; DIP-4537N; -.
DR IntAct; P33441; 42.
DR MINT; P33441; -.
DR STRING; 4932.YML062C; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; P33441; -.
DR MaxQB; P33441; -.
DR PaxDb; P33441; -.
DR PRIDE; P33441; -.
DR EnsemblFungi; YML062C_mRNA; YML062C; YML062C.
DR GeneID; 854940; -.
DR KEGG; sce:YML062C; -.
DR SGD; S000004527; MFT1.
DR VEuPathDB; FungiDB:YML062C; -.
DR eggNOG; ENOG502S0NG; Eukaryota.
DR HOGENOM; CLU_054999_1_0_1; -.
DR InParanoid; P33441; -.
DR OMA; YNEQDTA; -.
DR BioCyc; YEAST:G3O-32657-MON; -.
DR PRO; PR:P33441; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P33441; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0000446; C:nucleoplasmic THO complex; IMP:SGD.
DR GO; GO:0000445; C:THO complex part of transcription export complex; IDA:SGD.
DR GO; GO:0000346; C:transcription export complex; IPI:ComplexPortal.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IDA:SGD.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR InterPro; IPR008501; THOC7/Mft1.
DR Pfam; PF05615; THOC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..392
FT /note="THO complex subunit MFT1"
FT /id="PRO_0000096463"
FT REGION 258..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 22..43
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 61..101
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 107..142
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 199..246
FT /evidence="ECO:0007829|PDB:7APX"
SQ SEQUENCE 392 AA; 44996 MW; 45A775F8C1DA3E29 CRC64;
MPLSQKQIDQ VRTKVHYSEV DTPFNKYLDI LGKVTKLTGS IINGTLSNDD SKIEKLTEQN
ISQLKESAHL RFLDLQSSID TKKVADENWE TCQQETLAKL ENLKDKLPDI KSIHSKLLLR
IGKLQGLYDS VQVINREVEG LSEGRTSLVV TRAEWEKELG TDLVKFLIEK NYLKLVDPGL
KKDSSEERYR IYDDFSKGPK ELESINASMK SDIENVRQEV SSYKEKWLRD AEIFGKITSI
FKEELLKRDG LLNEAEGDNI DEDYESDEDE ERKERFKRQR SMVEVNTIEN VDEKEESDHE
YDDQEDEENE EEDDMEVDVE DIKEDNEVDG ESSQQEDNSR QGNNEETDKE TGVIEEPDAV
NDAEEADSDH SSRKLGGTTS DFSASSSVEE VK
