SWT1_YEAST
ID SWT1_YEAST Reviewed; 458 AA.
AC Q12104; D6W2M4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Transcriptional protein SWT1;
DE AltName: Full=Synthetically lethal with TREX protein 1;
GN Name=SWT1; OrderedLocusNames=YOR166C; ORFNames=O3595;
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].
RC STRAIN=S288c / FY1678;
RX PubMed=8972579;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1563::aid-yea44>3.0.co;2-m;
RA Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.;
RT "Analysis of a 22,956 bp region on the right arm of Saccharomyces
RT cerevisiae chromosome XV.";
RL Yeast 12:1563-1573(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 FUNCTION, INTERACTION WITH THE TREX COMPLEX AND RNA POLYMERASE II,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF 1-MET--LYS-115 AND 260-LEU--THR-458,
RP AND DELETION MUTANT.
RX PubMed=17030511; DOI=10.1074/jbc.m607510200;
RA Roether S., Clausing E., Kieser A., Straesser K.;
RT "Swt1, a novel yeast protein, functions in transcription.";
RL J. Biol. Chem. 281:36518-36525(2006).
RN [5]
RP FUNCTION.
RX PubMed=16464826; DOI=10.1093/nar/gkj493;
RA Titz B., Thomas S., Rajagopala S.V., Chiba T., Ito T., Uetz P.;
RT "Transcriptional activators in yeast.";
RL Nucleic Acids Res. 34:955-967(2006).
CC -!- FUNCTION: Involved in transcription. Probably functions as a
CC transcriptional activator. {ECO:0000269|PubMed:16464826,
CC ECO:0000269|PubMed:17030511}.
CC -!- SUBUNIT: Interacts with the TREX complex and RNA polymerase II.
CC {ECO:0000269|PubMed:17030511}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17030511}.
CC Note=Mainly nuclear, but might shuttle between the nucleus and the
CC cytoplasm.
CC -!- MISCELLANEOUS: Deletion causes a slow growth phenotype on synthetic
CC medium at 37 degrees Celsius and leads to decreased transcription.
CC Deletion has no effect on ribosome biogenesis or frequency of
CC recombination. Deletion is synthetically lethal with a deletion of each
CC of the THO complex subunits HPR1, MFT1, THO2, and THP2.
CC -!- SIMILARITY: Belongs to the SWT1 family. {ECO:0000305}.
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DR EMBL; U55021; AAB47413.1; -; Genomic_DNA.
DR EMBL; Z75074; CAA99372.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10940.1; -; Genomic_DNA.
DR PIR; S67054; S67054.
DR RefSeq; NP_014809.3; NM_001183585.3.
DR PDB; 4PQZ; X-ray; 2.30 A; A=312-458.
DR PDBsum; 4PQZ; -.
DR AlphaFoldDB; Q12104; -.
DR SMR; Q12104; -.
DR BioGRID; 34562; 63.
DR STRING; 4932.YOR166C; -.
DR iPTMnet; Q12104; -.
DR MaxQB; Q12104; -.
DR PaxDb; Q12104; -.
DR PRIDE; Q12104; -.
DR EnsemblFungi; YOR166C_mRNA; YOR166C; YOR166C.
DR GeneID; 854337; -.
DR KEGG; sce:YOR166C; -.
DR SGD; S000005692; SWT1.
DR VEuPathDB; FungiDB:YOR166C; -.
DR eggNOG; KOG4689; Eukaryota.
DR GeneTree; ENSGT00390000001254; -.
DR HOGENOM; CLU_048317_0_0_1; -.
DR InParanoid; Q12104; -.
DR OMA; WANDWIY; -.
DR BioCyc; YEAST:G3O-33682-MON; -.
DR PRO; PR:Q12104; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12104; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:SGD.
DR GO; GO:0071032; P:nuclear mRNA surveillance of mRNP export; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR Pfam; PF13638; PIN_4; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..458
FT /note="Transcriptional protein SWT1"
FT /id="PRO_0000237661"
FT DOMAIN 130..262
FT /note="PINc"
FT MUTAGEN 1..115
FT /note="Missing: Fully functional; when associated with
FT deletion of 260-L--T-458."
FT /evidence="ECO:0000269|PubMed:17030511"
FT MUTAGEN 260..458
FT /note="Missing: Fully functional; when associated with
FT deletion of 1-M--K-115."
FT /evidence="ECO:0000269|PubMed:17030511"
FT HELIX 326..353
FT /evidence="ECO:0007829|PDB:4PQZ"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:4PQZ"
FT TURN 358..361
FT /evidence="ECO:0007829|PDB:4PQZ"
FT HELIX 370..379
FT /evidence="ECO:0007829|PDB:4PQZ"
FT TURN 380..384
FT /evidence="ECO:0007829|PDB:4PQZ"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:4PQZ"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:4PQZ"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:4PQZ"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:4PQZ"
FT HELIX 413..430
FT /evidence="ECO:0007829|PDB:4PQZ"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:4PQZ"
FT HELIX 436..454
FT /evidence="ECO:0007829|PDB:4PQZ"
SQ SEQUENCE 458 AA; 52374 MW; 20E358D9568543EC CRC64;
MTDEKRAFPK GNNHIRSETF NGSVSHKISE SIKDIASLRP HGKYTVQDID NIIASTSSHE
NRGQSGDSNG CINHDEEGDI PMCDLNDESD VEMISEYLSS QREMEAQSVA NYMPKINDDL
PLLNPPTLKT AFVVDTNFII SHLNTLEKLR SLSSTYHHLI IVPTTVIQEL DGLKKSPDIA
RDNDDTTNQE HDRTIGTLAR WGNDWIYKNL ANLDSGLIGQ KLKQSLNPGS LKDDSILDCC
LYFKEILNCF VILLSNDKNL CTKALTEDIL TVSFRKNMDA KIIAMRAYEE NQLRFANLRD
STVNNFDQNV TSYAHIPGIE TPPLQFDKVS QNVFEQVKET IFFAIDHTLR KEYGEDIGFI
DYNPDKLTTI ENASNYIYLF WVSVFSELFT CSKIKKNEWK SLPTVLKSKP TNLNDLRTFE
QFWETVLHFL FSKFTNEEKQ SLEKQIHEWK TSINAIST
