MFT1_SCHPO
ID MFT1_SCHPO Reviewed; 202 AA.
AC Q9P7J4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=THO complex subunit mft1;
GN Name=mft1; ORFNames=SPCC24B10.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB76220.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the THO and TREX complexes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAB76220.1; -; Genomic_DNA.
DR PIR; T50418; T50418.
DR RefSeq; NP_588014.1; NM_001023005.2.
DR AlphaFoldDB; Q9P7J4; -.
DR SMR; Q9P7J4; -.
DR BioGRID; 275579; 5.
DR STRING; 4896.SPCC24B10.11c.1; -.
DR MaxQB; Q9P7J4; -.
DR PaxDb; Q9P7J4; -.
DR PRIDE; Q9P7J4; -.
DR EnsemblFungi; SPCC24B10.11c.1; SPCC24B10.11c.1:pep; SPCC24B10.11c.
DR GeneID; 2539006; -.
DR KEGG; spo:SPCC24B10.11c; -.
DR PomBase; SPCC24B10.11c; mft1.
DR VEuPathDB; FungiDB:SPCC24B10.11c; -.
DR eggNOG; ENOG502S942; Eukaryota.
DR HOGENOM; CLU_1422179_0_0_1; -.
DR InParanoid; Q9P7J4; -.
DR OMA; QMQLDTH; -.
DR PhylomeDB; Q9P7J4; -.
DR Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SPO-72187; mRNA 3'-end processing.
DR PRO; PR:Q9P7J4; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000445; C:THO complex part of transcription export complex; ISS:PomBase.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:PomBase.
DR InterPro; IPR008501; THOC7/Mft1.
DR Pfam; PF05615; THOC7; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..202
FT /note="THO complex subunit mft1"
FT /id="PRO_0000361067"
FT REGION 166..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..151
FT /evidence="ECO:0000255"
SQ SEQUENCE 202 AA; 23282 MW; C7C7700DFA5AB04E CRC64;
MEETAIRSRL TVEERPLKRL ISRCLGFAAQ NVDEANLRDL EIEFSALSAF WLRLQMQLDM
NAKEVDVYEG ELKKTQTFCE AEKTEISQLE QDLLVAQEEL RKREQYDELA KPIMSKGLRS
RTEQQESIGK LQDAIRELEE ENANYVKAWN LRKDIFDETL KQMNHLQSIL HPPSNPESDS
EEGIASEGEN PSSSSSTQYK AK
