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CPH2_CANAL
ID   CPH2_CANAL              Reviewed;         853 AA.
AC   Q59RL7; A0A1D8PPB5; Q59S18;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Transcription factor CPH2;
DE   AltName: Full=Candida pseudohyphal regulator 2;
GN   Name=CPH2; OrderedLocusNames=CAALFM_C600280WA;
GN   ORFNames=CaO19.1187, CaO19.8778;
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, AND DISRUPTION PHENOTYPE.
RX   PubMed=11595734; DOI=10.1074/jbc.m104484200;
RA   Lane S., Birse C., Zhou S., Matson R., Liu H.;
RT   "DNA array studies demonstrate convergent regulation of virulence factors
RT   by Cph1, Cph2, and Efg1 in Candida albicans.";
RL   J. Biol. Chem. 276:48988-48996(2001).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RX   PubMed=11533231; DOI=10.1128/mcb.21.19.6418-6428.2001;
RA   Lane S., Zhou S., Pan T., Dai Q., Liu H.;
RT   "The basic helix-loop-helix transcription factor Cph2 regulates hyphal
RT   development in Candida albicans partly via TEC1.";
RL   Mol. Cell. Biol. 21:6418-6428(2001).
RN   [6]
RP   FUNCTION.
RX   PubMed=12581351; DOI=10.1046/j.1365-2958.2003.03358.x;
RA   Rottmann M., Dieter S., Brunner H., Rupp S.;
RT   "A screen in Saccharomyces cerevisiae identified CaMCM1, an essential gene
RT   in Candida albicans crucial for morphogenesis.";
RL   Mol. Microbiol. 47:943-959(2003).
RN   [7]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=15999207; DOI=10.1111/j.1745-7270.2005.00063.x;
RA   Xu Z., Cao Y.B., Zhang J.D., Cao Y.Y., Gao P.H., Wang D.J., Fu X.P.,
RA   Ying K., Chen W.S., Jiang Y.Y.;
RT   "cDNA array analysis of the differential expression change in virulence-
RT   related genes during the development of resistance in Candida albicans.";
RL   Acta Biochim. Biophys. Sin. 37:463-472(2005).
RN   [8]
RP   INDUCTION.
RX   PubMed=15820985; DOI=10.1093/jac/dki088;
RA   Copping V.M.S., Barelle C.J., Hube B., Gow N.A.R., Brown A.J.P., Odds F.C.;
RT   "Exposure of Candida albicans to antifungal agents affects expression of
RT   SAP2 and SAP9 secreted proteinase genes.";
RL   J. Antimicrob. Chemother. 55:645-654(2005).
RN   [9]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=20435697; DOI=10.1128/ec.00034-10;
RA   Rosenbach A., Dignard D., Pierce J.V., Whiteway M., Kumamoto C.A.;
RT   "Adaptations of Candida albicans for growth in the mammalian intestinal
RT   tract.";
RL   Eukaryot. Cell 9:1075-1086(2010).
RN   [10]
RP   INDUCTION.
RX   PubMed=21357478; DOI=10.1128/ec.00305-10;
RA   Shareck J., Nantel A., Belhumeur P.;
RT   "Conjugated linoleic acid inhibits hyphal growth in Candida albicans by
RT   modulating Ras1p cellular levels and downregulating TEC1 expression.";
RL   Eukaryot. Cell 10:565-577(2011).
RN   [11]
RP   FUNCTION.
RX   PubMed=21407800; DOI=10.1371/journal.pone.0017046;
RA   Wachtler B., Wilson D., Haedicke K., Dalle F., Hube B.;
RT   "From attachment to damage: defined genes of Candida albicans mediate
RT   adhesion, invasion and damage during interaction with oral epithelial
RT   cells.";
RL   PLoS ONE 6:E17046-E17046(2011).
RN   [12]
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   [13]
RP   INDUCTION.
RX   PubMed=23766273; DOI=10.1111/jicd.12048;
RA   Bandara H.M., Cheung B.P., Watt R.M., Jin L.J., Samaranayake L.P.;
RT   "Secretory products of Escherichia coli biofilm modulate Candida biofilm
RT   formation and hyphal development.";
RL   J. Investig. Clin. Dent. 4:186-199(2013).
RN   [14]
RP   INDUCTION.
RX   PubMed=24260276; DOI=10.1371/journal.pone.0079671;
RA   Zhao L.X., Li D.D., Hu D.D., Hu G.H., Yan L., Wang Y., Jiang Y.Y.;
RT   "Effect of tetrandrine against Candida albicans biofilms.";
RL   PLoS ONE 8:E79671-E79671(2013).
CC   -!- FUNCTION: Transcription factor that positively controls filamentous
CC       growth, virulence, and invasiveness. Binds directly to the two SRE-1-
CC       like elements upstream of TEC1 and thus regulates positively expression
CC       of this important hyphal growth regulator. Functions independently of
CC       known signaling cascades involving EFG1. Regulates also gene expression
CC       during intestinal colonization but is not involved in host cell
CC       adhesion. {ECO:0000269|PubMed:11533231, ECO:0000269|PubMed:11595734,
CC       ECO:0000269|PubMed:12581351, ECO:0000269|PubMed:15999207,
CC       ECO:0000269|PubMed:20435697, ECO:0000269|PubMed:21407800}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: Up-regulated during the yeast-to-hypha transition and in
CC       virulent strains during intestinal colonization. Also induced upon
CC       exposure to fluconazole. Expression is down-regulated by tetrandrine
CC       and by Escherichia coli biofilm secretory products.
CC       {ECO:0000269|PubMed:15820985, ECO:0000269|PubMed:15999207,
CC       ECO:0000269|PubMed:20435697, ECO:0000269|PubMed:21357478,
CC       ECO:0000269|PubMed:23766273, ECO:0000269|PubMed:24260276}.
CC   -!- DISRUPTION PHENOTYPE: Impairs expression of hypha-specific transcripts
CC       and leads to a medium-specific impairment in hyphal development.
CC       {ECO:0000269|PubMed:11533231, ECO:0000269|PubMed:11595734,
CC       ECO:0000269|PubMed:22365851}.
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DR   EMBL; CP017628; AOW29977.1; -; Genomic_DNA.
DR   RefSeq; XP_712305.1; XM_707212.2.
DR   AlphaFoldDB; Q59RL7; -.
DR   SMR; Q59RL7; -.
DR   STRING; 237561.Q59RL7; -.
DR   PRIDE; Q59RL7; -.
DR   GeneID; 3646067; -.
DR   KEGG; cal:CAALFM_C600280WA; -.
DR   CGD; CAL0000181382; CPH2.
DR   VEuPathDB; FungiDB:C6_00280W_A; -.
DR   HOGENOM; CLU_017043_0_0_1; -.
DR   InParanoid; Q59RL7; -.
DR   OrthoDB; 526890at2759; -.
DR   PHI-base; PHI:2861; -.
DR   PRO; PR:Q59RL7; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IDA:CGD.
DR   GO; GO:0005634; C:nucleus; IDA:CGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:CGD.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:CGD.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0044403; P:biological process involved in symbiotic interaction; IMP:CGD.
DR   GO; GO:0071280; P:cellular response to copper ion; IMP:CGD.
DR   GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR   GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR   GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; 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:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR   GO; GO:1900430; P:positive regulation of filamentous growth of a population of unicellular organisms; IMP:CGD.
DR   GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic 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:1900442; P:positive regulation of filamentous growth of a population of unicellular organisms in response to neutral pH; 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; IMP:CGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:CGD.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..853
FT                   /note="Transcription factor CPH2"
FT                   /id="PRO_0000425613"
FT   DOMAIN          205..274
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          165..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..319
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   853 AA;  96046 MW;  DE562E008F50362C CRC64;
     MLSQYDEQLA AGDNNGFNKQ GNATLYSFDF VDADDFLDSI SGALPNNGHN NVNPNTNDIS
     FEDMNIMNPN IYSPVSAASG DDFTQSSGQP MISEGSNYTG QNFTDYLSDN SLEGYDKNTS
     RPLHEVDIGF SNKRSNSTST GSLSHNEEIT PISHYSVDSI VTSPEPPINK QGDFPPIKRT
     TTVSSTNSIT NTTKKPAKVT KPKSKDKNSH NMIEKKYRTN INTKILALRD AVPALRIAAG
     CDDVSIADLE GLTPASKLNK ASVLTKATEY IKHLESKNFI LKQQNIELHR LIQHANMNPK
     SLPPPPQQMQ APPQPGFGFY PPQNQSFNVT PASQYPSPQQ QVSPTQQQTV HHPPQPNRYL
     LGGMAAVMGT SLFGGSGEND FRSLSALPFS YLFPNAILNP SPLTIQLWTL TKVLLVVGSL
     ASIFIPMYKQ AQLKKEDKPN TIPETSLLDW ILISIGFKTP AKLSVSKRDA IISNLQGGND
     WSQLVSDYFY LAGCEINFEN CFLSLVLGTI IRHRFPVVAT ILNHYLSMKE ALLLNLDYKG
     FSKSLIRLNQ LISKVDGVSI FESTNLTTRL TNVFTNNRIN ANIVDGQNHV KYIEFYQRNI
     NDYYAIVFNW RLLEFIHELN VTYLEQLNDD QSQVLTDLKI IEAFFGEQDN KLFGYYQLFT
     SILNANYAPY LFESLKDKVE SSLEKFRIAY EGIDLTDHEI HNTSSEDEYE QESPVVYKYE
     PTLKSQKSLI SSLNLVNEEE FIILTCSLTI YYYKNKEYDR ALKLLNYLRL DNDSKTLSLL
     TFTSLITLIN ELIPGKIEDN VNLDSAIRIC RDWLENPDLT QYMDEDIKLE LKKIVVTKGM
     IVNGIDVNES DEE
 
 
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