ID   STP3_CANAL              Reviewed;         436 AA.
AC   Q5ANI6; A0A1D8PJZ4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Transcriptional regulator STP3;
DE   Flags: Precursor;
GN   Name=STP3; Synonyms=STP1; OrderedLocusNames=CAALFM_C304580CA;
GN   ORFNames=CaO19.13338, CaO19.5917;
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   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PROTEOLYTIC PROCESSING.
RX   PubMed=16227594; DOI=10.1128/mcb.25.21.9435-9446.2005;
RA   Martinez P., Ljungdahl P.O.;
RT   "Divergence of Stp1 and Stp2 transcription factors in Candida albicans
RT   places virulence factors required for proper nutrient acquisition under
RT   amino acid control.";
RL   Mol. Cell. Biol. 25:9435-9446(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=18547391; DOI=10.1111/j.1365-2958.2008.06297.x;
RA   Dabas N., Morschhauser J.;
RT   "A transcription factor regulatory cascade controls secreted aspartic
RT   protease expression in Candida albicans.";
RL   Mol. Microbiol. 69:586-602(2008).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22110651; DOI=10.1371/journal.pone.0027434;
RA   Davis M.M., Alvarez F.J., Ryman K., Holm A.A., Ljungdahl P.O., Engstrom Y.;
RT   "Wild-type Drosophila melanogaster as a model host to analyze nitrogen
RT   source dependent virulence of Candida albicans.";
RL   PLoS ONE 6:E27434-E27434(2011).
CC   -!- FUNCTION: Transcription factor that activates genes required for
CC       degradation of extracellular protein and uptake of peptides such as the
CC       secreted aspartyl protease SAP2 or the oligopeptide transporter OPT1.
CC       Required for virulence. Synthesized as latent cytoplasmic precursor,
CC       which, upon a signal initiated by the plasma membrane SPS amino acid
CC       sensor system (including CSY1 and CSH3), becomes proteolytically
CC       activated and relocates to the nucleus, where it induces the expression
CC       of SPS-sensor-regulated genes. {ECO:0000269|PubMed:16227594,
CC       ECO:0000269|PubMed:18547391, ECO:0000269|PubMed:22110651}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Localizes to the cytoplasm in its unprocessed form
CC       and is targeted to the nucleus after proteolytic processing upon
CC       induction by amino acids. {ECO:0000250}.
CC   -!- INDUCTION: Expression is down-regulated in presence of extracellular
CC       amino acids. {ECO:0000269|PubMed:16227594}.
CC   -!- PTM: Activated by the amino acid-induced proteolytic removal of an N-
CC       terminal inhibitory domain.
CC   -!- DISRUPTION PHENOTYPE: Impairs expression of SAP2 and OPT1. Impairs
CC       virulence in Drosophila as a host model. {ECO:0000269|PubMed:16227594,
CC       ECO:0000269|PubMed:22110651}.
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DR   EMBL; CP017625; AOW28476.1; -; Genomic_DNA.
DR   RefSeq; XP_723130.1; XM_718037.1.
DR   AlphaFoldDB; Q5ANI6; -.
DR   STRING; 237561.Q5ANI6; -.
DR   GeneID; 3635152; -.
DR   KEGG; cal:CAALFM_C304580CA; -.
DR   CGD; CAL0000188272; STP1.
DR   VEuPathDB; FungiDB:C3_04580C_A; -.
DR   eggNOG; ENOG502S4NK; Eukaryota.
DR   HOGENOM; CLU_036916_0_0_1; -.
DR   InParanoid; Q5ANI6; -.
DR   OMA; IFPVNCA; -.
DR   OrthoDB; 1492250at2759; -.
DR   PRO; PR:Q5ANI6; -.
DR   Proteomes; UP000000559; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; ISS:CGD.
DR   GO; GO:0005634; C:nucleus; ISS:CGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:CGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:CGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; DNA-binding; Membrane; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Virulence; Zinc; Zinc-finger; Zymogen.
FT   PROPEP          1..?
FT                   /id="PRO_0000426058"
FT   CHAIN           ?..436
FT                   /note="Transcriptional regulator STP3"
FT                   /id="PRO_0000426059"
FT   ZN_FING         315..337
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          204..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  49092 MW;  D89A0347A6A4655B CRC64;
     MLILSIGLIH HTSNKSLYTI SPNKGKRYEP FTTTSLGNFQ FHVVRFLHRL IYGTQRYQEL
     FPPIQKIKNI NNVKQQRIFP VNCAADDLDL GFGESDQIEL FNHPSKDTYG QFNLIQLIDI
     FDPPQVHAPS SADEFFKSNK GSEHIDIFDM ITRQPPPFHQ HQLNIETPYF EDFATPLVLP
     PHEVSSDDVE SYFSGSVSTV SSIEPLDDEF VPPPQPPRTH TSRKRKHDSI SPPASSDSSS
     SSSYVPQLIP SSSSSVTSNG DSPVSPTTKR KYTKKKQPVF SNVDEPIVIT TTTKTNNIDV
     KKITTTKNGT VENRFDCPSC DASFKVKGYL TRHLKKHSTS KAFECPFFDN HGVHGSKCHP
     TGGFSRRDTF KVHLRALHFI YPAGVKASQR NSFNGRCAGC FQYFDNNSEW LENHIEAGKC
     TGTVQYKQNV SNLLLD