SPT3_SCHPO
ID SPT3_SCHPO Reviewed; 307 AA.
AC O14311;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 2.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=SAGA complex subunit spt3;
GN Name=spt3; ORFNames=SPCC61.02;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9559549;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<409::aid-yea237>3.0.co;2-x;
RA Madison J.M., Winston F.;
RT "Identification and analysis of homologues of Saccharomyces cerevisiae Spt3
RT suggest conserved functional domains.";
RL Yeast 14:409-417(1998).
RN [2]
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 [3]
RP IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19056896; DOI=10.1101/gad.1719908;
RA Helmlinger D., Marguerat S., Villen J., Gygi S.P., Bahler J., Winston F.;
RT "The S. pombe SAGA complex controls the switch from proliferation to sexual
RT differentiation through the opposing roles of its subunits Gcn5 and Spt8.";
RL Genes Dev. 22:3184-3195(2008).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complex SAGA. SAGA is involved in RNA
CC polymerase II-dependent transcriptional regulation. At the promoters,
CC SAGA is required for recruitment of the basal transcription machinery.
CC It influences RNA polymerase II transcriptional activity through
CC different activities such as TBP interaction (spt3, spt8 and spt20) and
CC promoter selectivity, interaction with transcription activators (gcn5,
CC ada2, ada3 and tra1), and chromatin modification through histone
CC acetylation (gcn5) and deubiquitination (ubp8). SAGA acetylates
CC nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac
CC and H3K23ac). SAGA interacts with DNA via upstream activating sequences
CC (UASs). Spt3 is required for recruitment of TATA-binding protein (TBP)
CC to SAGA-dependent promoters. During SAGA-mediated transcriptional
CC inhibition, spt3 and spt8 prevent binding of TBP to the TATA box (By
CC similarity). SPT factors 3, 7 and 8 are required for the initiation of
CC Ty transcription from the delta promoter. Spt3 regulates Ty1 as well as
CC the mating factor genes. {ECO:0000250, ECO:0000269|PubMed:9559549}.
CC -!- SUBUNIT: Component of the SAGA complex. {ECO:0000269|PubMed:19056896}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9559549}.
CC -!- SIMILARITY: Belongs to the SPT3 family. {ECO:0000305}.
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DR EMBL; AF005931; AAC49995.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA22271.1; -; Genomic_DNA.
DR PIR; T41462; T41462.
DR RefSeq; NP_588193.1; NM_001023183.2.
DR AlphaFoldDB; O14311; -.
DR SMR; O14311; -.
DR BioGRID; 276130; 6.
DR IntAct; O14311; 2.
DR MINT; O14311; -.
DR STRING; 4896.SPCC61.02.1; -.
DR MaxQB; O14311; -.
DR PaxDb; O14311; -.
DR EnsemblFungi; SPCC61.02.1; SPCC61.02.1:pep; SPCC61.02.
DR GeneID; 2539570; -.
DR KEGG; spo:SPCC61.02; -.
DR PomBase; SPCC61.02; spt3.
DR VEuPathDB; FungiDB:SPCC61.02; -.
DR eggNOG; KOG3902; Eukaryota.
DR HOGENOM; CLU_038706_1_1_1; -.
DR InParanoid; O14311; -.
DR OMA; QFMFNEQ; -.
DR PhylomeDB; O14311; -.
DR PRO; PR:O14311; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; NAS:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:PomBase.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd07978; TAF13; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003195; TFIID_TAF13.
DR PANTHER; PTHR11380; PTHR11380; 1.
DR Pfam; PF02269; TFIID-18kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..307
FT /note="SAGA complex subunit spt3"
FT /id="PRO_0000072165"
FT CONFLICT 102
FT /note="A -> R (in Ref. 1; AAC49995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 35633 MW; AB868458D651CC04 CRC64;
MTETGRTSKY RVEIQQMMFI LGEVQDPLPE TTQLVEELIR GQVMEMLIQA NELALRRGSR
SITVEDLFFL IRHDRAKVNR LKTYLSWKEV RKKAKEQDAN PADTKDLFEE VDSKTRSMNA
VAMPWEVKNM FTEPVPETEE FEEDNDTMEM AYATRQRLKM ADERTKKMTR EEYVHWSECR
QASFTYRKGK RFREWCGMSI LTDTRPDNDI VDILGFLTFE IVATLTEEAL AVKDRMDRIQ
NSSGSGGSHA AHHPKNCSLF DGLTEGRTPL QVSHVLEAFR RLQIPDKTHT AMRSFHGGLV
KSRVYLI
