STP2_CANAL
ID STP2_CANAL Reviewed; 584 AA.
AC Q5AL16; A0A1D8PFM6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Transcriptional regulator STP2;
DE Flags: Precursor;
GN Name=STP2; OrderedLocusNames=CAALFM_C113350WA;
GN ORFNames=CaO19.12426, CaO19.4961;
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, 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=21586647; DOI=10.1128/mbio.00055-11;
RA Vylkova S., Carman A.J., Danhof H.A., Collette J.R., Zhou H., Lorenz M.C.;
RT "The fungal pathogen Candida albicans autoinduces hyphal morphogenesis by
RT raising extracellular pH.";
RL MBio 2:E00055-E00055(2011).
RN [6]
RP FUNCTION.
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).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=22365851; DOI=10.1016/j.cub.2012.01.062;
RA Shapiro R.S., Sellam A., Tebbji F., Whiteway M., Nantel A., Cowen L.E.;
RT "Pho85, Pcl1, and Hms1 signaling governs Candida albicans morphogenesis
RT induced by high temperature or Hsp90 compromise.";
RL Curr. Biol. 22:461-470(2012).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=23873867; DOI=10.1128/ec.00311-12;
RA Langford M.L., Hargarten J.C., Patefield K.D., Marta E., Blankenship J.R.,
RA Fanning S., Nickerson K.W., Atkin A.L.;
RT "Candida albicans Czf1 and Efg1 coordinate the response to farnesol during
RT quorum sensing, white-opaque thermal dimorphism, and cell death.";
RL Eukaryot. Cell 12:1281-1292(2013).
CC -!- FUNCTION: Transcription factor involved in the regulation of gene
CC expression in response to extracellular amino acid levels. Synthesized
CC as latent cytoplasmic precursor, which, upon a signal initiated by the
CC plasma membrane SPS amino acid sensor system (including CSY1 and CSH3),
CC becomes proteolytically activated and relocates to the nucleus, where
CC it induces the expression of SPS-sensor-regulated genes. Required for
CC efficient alkalinization through the release of ammonia from the cells
CC produced during the breakdown of amino acids, and subsequent switch to
CC the hyphal form. {ECO:0000269|PubMed:16227594,
CC ECO:0000269|PubMed:21586647, 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 -!- PTM: Proteolytically cleaved: activated by the amino acid-induced
CC proteolytic removal of an N-terminal inhibitory domain.
CC {ECO:0000269|PubMed:16227594}.
CC -!- DISRUPTION PHENOTYPE: Exhibits reduced capacity to take up amino acids
CC and to switch to the hyphal form, and impairs response to farnesol.
CC {ECO:0000269|PubMed:16227594, ECO:0000269|PubMed:22365851,
CC ECO:0000269|PubMed:23873867}.
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DR EMBL; CP017623; AOW26940.1; -; Genomic_DNA.
DR RefSeq; XP_722171.1; XM_717078.2.
DR AlphaFoldDB; Q5AL16; -.
DR BioGRID; 1219149; 1.
DR STRING; 237561.Q5AL16; -.
DR PRIDE; Q5AL16; -.
DR GeneID; 3636214; -.
DR KEGG; cal:CAALFM_C113350WA; -.
DR CGD; CAL0000195044; STP2.
DR VEuPathDB; FungiDB:C1_13350W_A; -.
DR eggNOG; ENOG502S1NP; Eukaryota.
DR HOGENOM; CLU_027007_0_0_1; -.
DR InParanoid; Q5AL16; -.
DR OrthoDB; 1250204at2759; -.
DR PHI-base; PHI:4193; -.
DR PRO; PR:Q5AL16; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; ISS:CGD.
DR GO; GO:0005634; C:nucleus; IDA: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:0043090; P:amino acid import; IMP:CGD.
DR GO; GO:0071469; P:cellular response to alkaline pH; IMP:CGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:1900439; P:positive regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus; 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 SMART; SM00355; ZnF_C2H2; 2.
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_0000426056"
FT CHAIN ?..584
FT /note="Transcriptional regulator STP2"
FT /id="PRO_0000426057"
FT ZN_FING 225..247
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 67011 MW; 4CF132637C6523BA CRC64;
MSVAITSNNN KQPQPQPQPH LKVVNNNSTF NLYTWLRSVF QYCISLIISY TSNWLLVNND
NNNNNININY KSNNNDNNNA STSLQPKISN VKAESMKIFP DLQKSNFTTY YTTEKPLHQD
VLKPVICSTG ITSRILPYTN EKGELEWKFT EVQGKELDEF KMHPQQQQQQ QEVKQELSPA
ESNESNESLA KDSSTTPASI SDSPSHSETE STVSSTIIAN SNQIFKCPSC DAEFRVRGYL
TRHMKKHSTK KAYTCPFHDK SIYVDENNIT HKCHSSGGFS RRDTYKTHLK SRHFNYAKPI
KSAERSKVPG QCAMCGEHFN SAEIWCEIHV EGGECKFLPM GFKGKSRIKN RLKKQIQKNK
MIDPELVPFA SKVLEEVEQE RQKKKNYRTT GTGSESSIQS QESESSINST PLSMQISAPV
PMPVSIQQQH QHQHQHHHHV QNQHQQHVNQ QQSIATPASI YSSSASSTSS YESTHSPYTP
QSSRSPLSHM YNPQQPPYFN QIAQAHQQDG QKNQVKDDYD DEYCLDVDQL NTTFVNETVA
NYLQIHDFHS MNQYQPGQQQ QQQQQQQQQQ QQRQHQQQQP SMYF
