ID   CAS5_CANAL              Reviewed;         821 AA.
AC   Q5AMH6; A0A1D8PL77;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Cell wall integrity transcriptional regulator CAS5;
DE   AltName: Full=Caspofungin sensitivity protein 5;
GN   Name=CAS5; OrderedLocusNames=CAALFM_C401190WA;
GN   ORFNames=CaO19.12140, CaO19.4670;
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=16552442; DOI=10.1371/journal.ppat.0020021;
RA   Bruno V.M., Kalachikov S., Subaran R., Nobile C.J., Kyratsous C.,
RA   Mitchell A.P.;
RT   "Control of the C. albicans cell wall damage response by transcriptional
RT   regulator Cas5.";
RL   PLoS Pathog. 2:E21-E21(2006).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19666778; DOI=10.1128/ec.00163-09;
RA   Pukkila-Worley R., Peleg A.Y., Tampakakis E., Mylonakis E.;
RT   "Candida albicans hyphal formation and virulence assessed using a
RT   Caenorhabditis elegans infection model.";
RL   Eukaryot. Cell 8:1750-1758(2009).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19463063; DOI=10.1086/599363;
RA   Chamilos G., Nobile C.J., Bruno V.M., Lewis R.E., Mitchell A.P.,
RA   Kontoyiannis D.P.;
RT   "Candida albicans Cas5, a regulator of cell wall integrity, is required for
RT   virulence in murine and toll mutant fly models.";
RL   J. Infect. Dis. 200:152-157(2009).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22359502; DOI=10.1371/journal.ppat.1002525;
RA   Finkel J.S., Xu W., Huang D., Hill E.M., Desai J.V., Woolford C.A.,
RA   Nett J.E., Taff H., Norice C.T., Andes D.R., Lanni F., Mitchell A.P.;
RT   "Portrait of Candida albicans adherence regulators.";
RL   PLoS Pathog. 8:E1002525-E1002525(2012).
CC   -!- FUNCTION: Transcription factor involved in the cell wall damage
CC       response. Acts with ADA2 to promote cell wall integrity. Required for
CC       expression of numerous cell wall biosynthesis inhibitor caspofungin-
CC       responsive genes. Plays a key role in adherence, hyphal development,
CC       and virulence. {ECO:0000269|PubMed:16552442,
CC       ECO:0000269|PubMed:19463063, ECO:0000269|PubMed:19666778,
CC       ECO:0000269|PubMed:22359502}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Leads to sensitivity to caspofungin and affects
CC       expression of many genes including caspofungin-responsive genes.
CC       Results in hyphal defect during C.elegans infection and exhibits
CC       attenuated virulence in flies and mice models for candidiasis.
CC       {ECO:0000269|PubMed:16552442, ECO:0000269|PubMed:19463063,
CC       ECO:0000269|PubMed:19666778, ECO:0000269|PubMed:22359502}.
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DR   EMBL; CP017626; AOW28904.1; -; Genomic_DNA.
DR   RefSeq; XP_722740.1; XM_717647.2.
DR   AlphaFoldDB; Q5AMH6; -.
DR   SMR; Q5AMH6; -.
DR   BioGRID; 1218537; 2.
DR   STRING; 237561.Q5AMH6; -.
DR   PRIDE; Q5AMH6; -.
DR   GeneID; 3635652; -.
DR   KEGG; cal:CAALFM_C401190WA; -.
DR   CGD; CAL0000197117; CAS5.
DR   VEuPathDB; FungiDB:C4_01190W_A; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_385415_0_0_1; -.
DR   InParanoid; Q5AMH6; -.
DR   OMA; THRNYNE; -.
DR   OrthoDB; 1468017at2759; -.
DR   PHI-base; PHI:3503; -.
DR   PRO; PR:Q5AMH6; -.
DR   Proteomes; UP000000559; Chromosome 4.
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: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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0070417; P:cellular response to cold; IMP:CGD.
DR   GO; GO:0044114; P:development of symbiont in host; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR   GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR   GO; GO:1900189; P:positive regulation of cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:CGD.
DR   GO; GO:0032443; P:regulation of ergosterol biosynthetic process; IMP:CGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
DR   GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   4: Predicted;
KW   Cell adhesion; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Virulence; Zinc; Zinc-finger.
FT   CHAIN           1..821
FT                   /note="Cell wall integrity transcriptional regulator CAS5"
FT                   /id="PRO_0000426062"
FT   ZN_FING         748..770
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         776..801
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          42..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..717
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  92784 MW;  97E6299448FB60C7 CRC64;
     MENYLLSSPT QLSQPYDDGT NSLLFMDNYE LSQNLSQPLD QHLQSLQQQS QVQSQAPQQV
     QSLNQHQQLP QIQPFPTLVN NQQYAQETFQ QLSQQHQQQQ QQQQQFSPFQ QSQLQQQFQY
     QYSQQQQQQH FQQPVTIEEE IVPASNNTNI QISKFFDDNK GDDEDIANSG NFNEFDHSRN
     ISLDDTTITD LHRRENSINP PTGLPHSISS NTIYSYSSFE SPQSHIQSQP SYSQGYHNQN
     SLSTPLRRNK SYSISSANFN QSPVNLATTA MNKIMKTPLR GHTRSRSKVD VNAAVTAAMN
     LGQATKSNST SSYNSTLNPF YTPSQQLSST DDDDISTPLL TPGTKLHTSK STFFSPYNKD
     DLEDQDDDAV KQLRKAKSYT SLLRKKKRED MTPSKQNQQH QQQQQQQQQQ QQSRQSGGGH
     IQNLSFPNST SQPKIDLLAY DQNPMTSYPP MDKSILKNLN QSISPFNKPK LSPPPSNFPS
     ISIDLTTIAT NKSSSFSSST THRNYNENTP FNSANSTSGG LLPPMATFTV PTVIKEELQV
     HNLQEEEQEH QDEQMEIDSF ESNEKNARPT LSTSSLVRSM KMANLEISND QQMSSNEDEN
     IVTEAVVKQE KNGPVVDDVN GTGTNSKKPR KKQKSKSKEN CNKKGKVATG NGKDNDKNNE
     CLVNKGNKTN NNDTSNDKLD NDNKNTNGNG NNDNDNDSEE NNDNVDDADD DDDGTVTIPI
     PEDLNVTKVK VRNNRSKSND KSDPKKKHKC PICESRFQRP EHVKRHLKSH SSEKPFECQM
     PNCGKRFNRK DNLKAHLKKI HGLVKGQEEF TRVLNENKEV S