SPT20_CANAL
ID SPT20_CANAL Reviewed; 751 AA.
AC Q5A2B9; A0A1D8PDK3; Q5A2H1;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Transcription factor SPT20 {ECO:0000305};
GN Name=SPT20; OrderedLocusNames=CAALFM_C105430WA;
GN ORFNames=CaO19.422, CaO19.8052;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION.
RX PubMed=15917516; DOI=10.1128/aac.49.6.2226-2236.2005;
RA Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
RA Rogers P.D.;
RT "Genome-wide expression profiling of the response to azole, polyene,
RT echinocandin, and pyrimidine antifungal agents in Candida albicans.";
RL Antimicrob. Agents Chemother. 49:2226-2236(2005).
RN [5]
RP INDUCTION.
RX PubMed=15796975; DOI=10.1016/j.femsle.2005.02.014;
RA Marchais V., Kempf M., Licznar P., Lefrancois C., Bouchara J.P., Robert R.,
RA Cottin J.;
RT "DNA array analysis of Candida albicans gene expression in response to
RT adherence to polystyrene.";
RL FEMS Microbiol. Lett. 245:25-32(2005).
RN [6]
RP IDENTIFICATION IN THE SAGA COMPLEX.
RX PubMed=19279142; DOI=10.1091/mbc.e08-11-1093;
RA Sellam A., Askew C., Epp E., Lavoie H., Whiteway M., Nantel A.;
RT "Genome-wide mapping of the coactivator Ada2p yields insight into the
RT functional roles of SAGA/ADA complex in Candida albicans.";
RL Mol. Biol. Cell 20:2389-2400(2009).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24732310; DOI=10.1371/journal.pone.0094468;
RA Tan X., Fuchs B.B., Wang Y., Chen W., Yuen G.J., Chen R.B., Jayamani E.,
RA Anastassopoulou C., Pukkila-Worley R., Coleman J.J., Mylonakis E.;
RT "The role of Candida albicans SPT20 in filamentation, biofilm formation and
RT pathogenesis.";
RL PLoS ONE 9:E94468-E94468(2014).
CC -!- FUNCTION: Component of the transcription regulatory histone acetylation
CC (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent
CC transcriptional regulation of approximately 10% of yeast genes. At the
CC promoters, SAGA is required for recruitment of the basal transcription
CC machinery. It influences RNA polymerase II transcriptional activity
CC through different activities such as TBP interaction and promoter
CC selectivity, interaction with transcription activators, and chromatin
CC modification through histone acetylation and deubiquitination. SAGA
CC acetylates nucleosomal histone H3 to some extent (to form H3K9ac,
CC H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream
CC activating sequences (UASs) (By similarity). SPT20 plays a role in
CC nuclear division and regulates hyphal and biofilm formation, which are
CC crucial steps for virulence. {ECO:0000250|UniProtKB:P50875,
CC ECO:0000269|PubMed:24732310, ECO:0000303|PubMed:19279142}.
CC -!- SUBUNIT: Component of the SAGA complex. {ECO:0000250|UniProtKB:P50875,
CC ECO:0000303|PubMed:19279142}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Expression is down-regulated by flucytosine and upon
CC adherence to polystyrene. {ECO:0000269|PubMed:15796975,
CC ECO:0000269|PubMed:15917516}.
CC -!- DISRUPTION PHENOTYPE: Impairs proper nucleus dividing and distribution
CC to the dividing cells. Leads to hypersensitivity to amphotericin B,
CC fluconazole and caspofunginreduced; and to reduced virulence in the
CC C.elegans and the G.mellonella infection models.
CC {ECO:0000269|PubMed:24732310}.
CC -!- SIMILARITY: Belongs to the SPT20 family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26212.1; -; Genomic_DNA.
DR RefSeq; XP_715857.2; XM_710764.2.
DR AlphaFoldDB; Q5A2B9; -.
DR STRING; 237561.Q5A2B9; -.
DR GeneID; 3642492; -.
DR KEGG; cal:CAALFM_C105430WA; -.
DR CGD; CAL0000196043; SPT20.
DR VEuPathDB; FungiDB:C1_05430W_A; -.
DR eggNOG; ENOG502QS30; Eukaryota.
DR HOGENOM; CLU_377649_0_0_1; -.
DR InParanoid; Q5A2B9; -.
DR OMA; YNEHITP; -.
DR OrthoDB; 1194828at2759; -.
DR PHI-base; PHI:4208; -.
DR PRO; PR:Q5A2B9; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0000124; C:SAGA complex; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR021950; Spt20.
DR Pfam; PF12090; Spt20; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Virulence.
FT CHAIN 1..751
FT /note="Transcription factor SPT20"
FT /id="PRO_0000431519"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 83963 MW; 91C753AF2CC0A718 CRC64;
MIKSEVLSGS ASKTVGNSIS NGTTVSTQNQ GGKQNLIRQQ QQQQQQQQQQ QQQQQQQQLK
HRTALQNYHF ASTSEEILKK YSKYPASMSL HIFETHYRFN NSQDSQVIPK DSPMIKDFMK
HVLKEQIPVE MCELIKDFAI RPYDGCIILQ VYDHRNMVKT AVLQNRSTSS PSKDQDKKQQ
MVVSKPRTYR TLLRPTSLSI YYDLLYHTDS ALHRFTDYLS LQMESEILTA TNRELNLSVP
LNPYNYDHLR PEPEPSGDMS QNSDEEIDQV KFQHRDAVEQ PRRKIHQDEM VLHKSSEYEE
LMLLLSNKHK RPDDCSDKRL VVVSTSALPG SSLTGTSNTS TGTAAATPTP TSTTASAASQ
SSKQTTADGA STTDTKGKKG DKANGTSANQ ASASPTSVHP PIPTIPQNSV RATGQFMRLR
LIEEIRKKRE LEKLQQEAKI QAQANAIQSD SVPPSQQLAP QNTINSPVVT EPTKRSSPAA
QNQPAPKRAK KETKKQLQAK AQAQAKAQAQ AKAKVQTETP GPTPVQGQNS LSGPSVVNGS
NVTSTANTPT MNNQSSLQQP SQASQPQIGS LNNNQQSQSQ QQQQKNPQQT LQQQQQQQIF
QNSLTPEEQK VYKQIQQNMA TLAMMGQSGV TPTGQQLTPQ QKQQAIQQAK NLQQQLFQRF
PLYFQRMKQL QLIHQKRRLQ QQQQQQQQQQ QQQASNSSGG NQNNSSNQAA PQTQQFNQAL
PSTSEQSKPV TTSPEVKKKR TYQKKKNAPA N
