Reviewed, UniProtKB/Swiss-Prot P33441 (MFT1_YEAST)

Names and origin

Protein names

Recommended name:
    THO complex subunit MFT1
Alternative name(s):
    Mitochondrial fusion target protein 1

Gene names

Name:	MFT1
Ordered Locus Names:	YML062C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA. Ref.4 Ref.6 Ref.7 Ref.10
Subunit structure	Component of the THO complex, which is composed of HPR1, MFT1, THO2 and THP2. Together with SUB2, TEX1 and YRA1, THO forms the transcription/export (TREX) complex. THO associates with DNA and RNA in vitro.
Subcellular location	Nucleus.
Miscellaneous	Present with 5910 molecules/cell in log phase SD medium. Ref.9
Caution	Was originally (Ref.1) thought to be involved in mitochondrial protein import.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA recombination Ref.3 Inferred from mutant phenotype. Source: SGD RNA elongation from RNA polymerase II promoter Ref.4 Inferred from mutant phenotype. Source: SGD mRNA export from nucleus Ref.5 Inferred from mutant phenotype. Source: SGD regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	THO complex part of transcription export complex Ref.5 Inferred from mutant phenotype. Source: SGD nucleoplasmic THO complex Ref.3 Inferred from mutant phenotype. Source: SGD
Molecular function	nucleic acid binding Ref.4 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 392	392	THO complex subunit MFT1		PRO_0000096463
Amino acid modifications
	Modified residue	47	1	Phosphoserine Ref.13
	Modified residue	115	1	Phosphoserine Ref.13
	Modified residue	266	1	Phosphoserine Ref.13 Ref.11 Ref.12
	Modified residue	368	1	Phosphoserine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	P33441-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 45A775F8C1DA3E29	FASTA	392	44,996
	10 20 30 40 50 60 MPLSQKQIDQ VRTKVHYSEV DTPFNKYLDI LGKVTKLTGS IINGTLSNDD SKIEKLTEQN 70 80 90 100 110 120 ISQLKESAHL RFLDLQSSID TKKVADENWE TCQQETLAKL ENLKDKLPDI KSIHSKLLLR 130 140 150 160 170 180 IGKLQGLYDS VQVINREVEG LSEGRTSLVV TRAEWEKELG TDLVKFLIEK NYLKLVDPGL 190 200 210 220 230 240 KKDSSEERYR IYDDFSKGPK ELESINASMK SDIENVRQEV SSYKEKWLRD AEIFGKITSI 250 260 270 280 290 300 FKEELLKRDG LLNEAEGDNI DEDYESDEDE ERKERFKRQR SMVEVNTIEN VDEKEESDHE 310 320 330 340 350 360 YDDQEDEENE EEDDMEVDVE DIKEDNEVDG ESSQQEDNSR QGNNEETDKE TGVIEEPDAV 370 380 390 NDAEEADSDH SSRKLGGTTS DFSASSSVEE VK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Precise mapping and molecular characterization of the MFT1 gene involved in import of a fusion protein into mitochondria in Saccharomyces cerevisiae." Ito M., Yasui A., Komamine A. FEBS Lett. 320:125-129(1993) [PubMed: 8458428] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae." Chavez S., Beilharz T., Rondon A.G., Erdjument-Bromage H., Tempst P., Svejstrup J.Q., Lithgow T., Aguilera A. EMBO J. 19:5824-5834(2000) [PubMed: 11060033] [Abstract] Cited for: IDENTIFICATION IN THO COMPLEX, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[4]	"The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability." Jimeno S., Rondon A.G., Luna R., Aguilera A. EMBO J. 21:3526-3535(2002) [PubMed: 12093753] [Abstract] Cited for: FUNCTION.
[5]	"TREX is a conserved complex coupling transcription with messenger RNA export." Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M., Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R., Hurt E. Nature 417:304-308(2002) [PubMed: 11979277] [Abstract] Cited for: IDENTIFICATION IN TREX COMPLEX, MASS SPECTROMETRY.
[6]	"Molecular evidence that the eukaryotic THO/TREX complex is required for efficient transcription elongation." Rondon A.G., Jimeno S., Garcia-Rubio M., Aguilera A. J. Biol. Chem. 278:39037-39043(2003) [PubMed: 12871933] [Abstract] Cited for: FUNCTION.
[7]	"Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination." Huertas P., Aguilera A. Mol. Cell 12:711-721(2003) [PubMed: 14527416] [Abstract] Cited for: FUNCTION.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes." Abruzzi K.C., Lacadie S., Rosbash M. EMBO J. 23:2620-2631(2004) [PubMed: 15192704] [Abstract] Cited for: FUNCTION.
[11]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, MASS SPECTROMETRY.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266 AND SER-368, MASS SPECTROMETRY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-115 AND SER-266, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S57517 Genomic DNA. Translation: AAB26005.1. Z38114 Genomic DNA. Translation: CAA86259.1.
PIR	S32405.
RefSeq	NP_013649.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4537N.
IntAct	P33441. 43 interactions.
STRING	P33441.
Proteomic databases
PRIDE	P33441.
Genome annotation databases
Ensembl	YML062C; YML062C; YML062C; Saccharomyces cerevisiae. [Genome view]
GeneID	854940.
KEGG	sce:YML062C.
NMPDR	fig|4932.3.peg.4686.
Organism-specific databases
CYGD	YML062c.
SGD	S000004527. MFT1.
Phylogenomic databases
HOGENOM	P33441.
OMA	DDFSKGP
OrthoDB	EOG9DFR4V
Gene expression databases
ArrayExpress	P33441.
Genevestigator	P33441.
GermOnline	YML062C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008501. THOC7/Mft1p. [Graphical view]
Pfam	PF05615. THOC7. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	977989.

Entry information

Entry name

MFT1_YEAST

Accession

Primary (citable) accession number: P33441

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 24, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)