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   04-NOV-2026, entry version 188.
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; DOI=10.1038/387s090;
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=5; 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   PDB; 7V2W; EM; 3.20 A; I=1-392.
DR   PDB; 7V2Y; EM; 3.40 A; D=1-392.
DR   AlphaFoldDB; P33441; -.
DR   EMDB; EMD-11859; -.
DR   EMDB; EMD-11871; -.
DR   EMDB; EMD-16841; -.
DR   EMDB; EMD-23527; -.
DR   EMDB; EMD-31669; -.
DR   EMDB; EMD-31670; -.
DR   SMR; P33441; -.
DR   BioGRID; 35104; 271.
DR   ComplexPortal; CPX-1792; THO complex.
DR   ComplexPortal; CPX-1793; TREX complex.
DR   DIP; DIP-4537N; -.
DR   FunCoup; P33441; 106.
DR   IntAct; P33441; 44.
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   PaxDb; 4932-YML062C; -.
DR   PeptideAtlas; P33441; -.
DR   EnsemblFungi; YML062C_mRNA; YML062C; YML062C.
DR   GeneID; 854940; -.
DR   KEGG; sce:YML062C; -.
DR   AGR; SGD:S000004527; -.
DR   SGD; S000004527; MFT1.
DR   VEuPathDB; FungiDB:YML062C; -.
DR   eggNOG; ENOG502S0NG; Eukaryota.
DR   HOGENOM; CLU_054999_1_0_1; -.
DR   InParanoid; P33441; -.
DR   OMA; AKWSHNA; -.
DR   OrthoDB; 4035165at2759; -.
DR   BioCyc; YEAST:G3O-32657-MONOMER; -.
DR   BioGRID-ORCS; 854940; 0 hits in 10 CRISPR screens.
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:0000347; C:THO complex; IPI:ComplexPortal.
DR   GO; GO:0000445; C:THO complex part of transcription export complex; IMP: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:0006368; P:transcription elongation by RNA polymerase II; 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        258..271
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..330
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..367
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..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..16
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   HELIX           22..41
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   TURN            42..44
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   HELIX           61..77
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   HELIX           80..97
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   TURN            98..102
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:7APX"
FT   HELIX           108..141
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   STRAND          146..150
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   HELIX           152..155
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   HELIX           161..167
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   TURN            168..171
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   HELIX           199..234
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   TURN            235..237
FT                   /evidence="ECO:0007829|PDB:7V2W"
FT   HELIX           238..246
FT                   /evidence="ECO:0007829|PDB:7V2W"
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
//