SKO1_CANAL
ID SKO1_CANAL Reviewed; 578 AA.
AC Q59VR1; A0A1D8PD41;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Transcriptional regulator SKO1;
GN Name=SKO1; OrderedLocusNames=CAALFM_C103770WA;
GN ORFNames=CaO19.1032, CaO19.8634;
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=16339080; DOI=10.1091/mbc.e05-06-0501;
RA Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P.,
RA Quinn J.;
RT "Role of the Hog1 stress-activated protein kinase in the global
RT transcriptional response to stress in the fungal pathogen Candida
RT albicans.";
RL Mol. Biol. Cell 17:1018-1032(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PHOSPHORYLATION.
RX PubMed=18434592; DOI=10.1091/mbc.e08-02-0191;
RA Rauceo J.M., Blankenship J.R., Fanning S., Hamaker J.J., Deneault J.S.,
RA Smith F.J., Nantel A., Mitchell A.P.;
RT "Regulation of the Candida albicans cell wall damage response by
RT transcription factor Sko1 and PAS kinase Psk1.";
RL Mol. Biol. Cell 19:2741-2751(2008).
RN [6]
RP INDUCTION.
RX PubMed=18653474; DOI=10.1091/mbc.e07-09-0946;
RA Ramsdale M., Selway L., Stead D., Walker J., Yin Z., Nicholls S.M.,
RA Crowe J., Sheils E.M., Brown A.J.;
RT "MNL1 regulates weak acid-induced stress responses of the fungal pathogen
RT Candida albicans.";
RL Mol. Biol. Cell 19:4393-4403(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20388546; DOI=10.1016/j.fgb.2010.03.009;
RA Alonso-Monge R., Roman E., Arana D.M., Prieto D., Urrialde V., Nombela C.,
RA Pla J.;
RT "The Sko1 protein represses the yeast-to-hypha transition and regulates the
RT oxidative stress response in Candida albicans.";
RL Fungal Genet. Biol. 47:587-601(2010).
CC -!- FUNCTION: Transcription repressor involved in cell wall damage
CC response. Regulates 79 caspofungin-responsive genes, including several
CC cell wall biogenesis genes such as CRH11, MNN2, and SKN1. Controls also
CC the expression of pathogenesis and hyphal related genes and represses
CC the yeast-to-hypha transition. Mediates the response to oxidative
CC stress. {ECO:0000269|PubMed:18434592, ECO:0000269|PubMed:20388546}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- INDUCTION: Expression is induced by cell wall damage caused by
CC caspofungin, and by osmotic stress through the HOG1 pathway. Expression
CC is positively regulated by MNL1. {ECO:0000269|PubMed:16339080,
CC ECO:0000269|PubMed:18434592, ECO:0000269|PubMed:18653474}.
CC -!- PTM: Undergoes HOG1-dependent phosphorylation after osmotic stress.
CC {ECO:0000269|PubMed:18434592}.
CC -!- DISRUPTION PHENOTYPE: Leads to caspofungin hypersensitivity and
CC increases filamentation. {ECO:0000269|PubMed:18434592,
CC ECO:0000269|PubMed:20388546}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26054.1; -; Genomic_DNA.
DR RefSeq; XP_019330633.1; XM_019475088.1.
DR AlphaFoldDB; Q59VR1; -.
DR SMR; Q59VR1; -.
DR STRING; 237561.Q59VR1; -.
DR GeneID; 3644688; -.
DR KEGG; cal:CAALFM_C103770WA; -.
DR CGD; CAL0000176357; SKO1.
DR VEuPathDB; FungiDB:C1_03770W_A; -.
DR eggNOG; KOG1414; Eukaryota.
DR HOGENOM; CLU_694587_0_0_1; -.
DR InParanoid; Q59VR1; -.
DR OrthoDB; 1253555at2759; -.
DR PRO; PR:Q59VR1; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR021755; TF_Aft1_HRA.
DR Pfam; PF11786; Aft1_HRA; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Stress response; Transcription; Transcription regulation.
FT CHAIN 1..578
FT /note="Transcriptional regulator SKO1"
FT /id="PRO_0000426091"
FT DOMAIN 483..546
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 39..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..505
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 508..515
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 39..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 61987 MW; 3A07F77835153138 CRC64;
MSSDHKSKFD LELNPFERSF ATKESSSVSL NELAAASNND AISDVNSVAT SGSSINNGSS
SNKHNLHIPN ISSVNQQQGV NGKLPGITPP LFTPGGRRLP PIGLSPGGTT SRQYSNSTNS
GSLQSNTDTL GSNIWGGLPT NQTFQPQPQP QPQPQQQQQP QQQQQTQQPH NFNQFMSGMR
KTGLTPNESN IRSGLTPGGL TNFGFGSNLV PGLSTPGALL NGPITPGLSS LLGITQTPSS
LLVPTTSSFS QNNQSHLIQP AANTSVGPIP ESTALGPHVN IPQANQLQQD QSSQALVGGL
PPSQPQPQPQ PVIAQQIHTI PENQSIAFDM TQPAVANAHL PESKPDLSET ANLQRDLNPT
ADTTTNTTTA TKKRKNDTAG GTNKKAKVAK GKKKEPKSKS KGKNNQEDDQ NASNKPEDEN
VPGKENGNEE NHKVEAESKE EHLQNGNETT TTKTNNTGNS SNGTTTTTTT KSKSKKNSNV
SEDDKRKNFL ERNRVAASKC RQRKKLLIQK MEEELEFYSN GYRELSAEVN ELRGAILLLK
EKHNIQDEII DGLLSKPTTV PTNVTSIPST IPTTLNPT
