ACE2_CANGA
ID ACE2_CANGA Reviewed; 703 AA.
AC Q6FJQ9;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Cell wall transcription factor ACE2;
GN Name=ACE2; OrderedLocusNames=CAGL0M04323g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=15075283; DOI=10.1128/ec.3.2.546-552.2004;
RA Kamran M., Calcagno A.M., Findon H., Bignell E., Jones M.D., Warn P.,
RA Hopkins P., Denning D.W., Butler G., Rogers T., Muhlschlegel F.A.,
RA Haynes K.;
RT "Inactivation of transcription factor gene ACE2 in the fungal pathogen
RT Candida glabrata results in hypervirulence.";
RL Eukaryot. Cell 3:546-552(2004).
RN [3]
RP FUNCTION.
RX PubMed=15825152; DOI=10.1002/pmic.200401064;
RA Stead D., Findon H., Yin Z., Walker J., Selway L., Cash P., Dujon B.A.,
RA Hennequin C., Brown A.J., Haynes K.;
RT "Proteomic changes associated with inactivation of the Candida glabrata
RT ACE2 virulence-moderating gene.";
RL Proteomics 5:1838-1848(2005).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=16926418; DOI=10.1128/iai.00817-06;
RA MacCallum D.M., Findon H., Kenny C.C., Butler G., Haynes K., Odds F.C.;
RT "Different consequences of ACE2 and SWI5 gene disruptions for virulence of
RT pathogenic and nonpathogenic yeasts.";
RL Infect. Immun. 74:5244-5248(2006).
RN [5]
RP FUNCTION.
RX PubMed=19941307; DOI=10.1002/pmic.200800706;
RA Stead D.A., Walker J., Holcombe L., Gibbs S.R., Yin Z., Selway L.,
RA Butler G., Brown A.J., Haynes K.;
RT "Impact of the transcriptional regulator, Ace2, on the Candida glabrata
RT secretome.";
RL Proteomics 10:212-223(2010).
CC -!- FUNCTION: Transcription factor involved in the RAM (regulation of ACE2
CC transcription factor and polarized morphogenesis) signaling network
CC that regulates polarized morphogenesis. Regulates expression of genes
CC involved in cell separation or other cell wall genes. Required for
CC regulation of morphogenesis, cell separation, adherence, biofilm
CC formation, invasion, as well as virulence.
CC {ECO:0000269|PubMed:15825152, ECO:0000269|PubMed:19941307}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localized in the
CC nuclei of daughter cells. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Leads to systemic infections characterized by
CC fungal escape from the vasculature, tissue penetration, proliferation
CC in vivo, and considerable overstimulation of the pro-inflammatory arm
CC of the innate immune response. {ECO:0000269|PubMed:15075283,
CC ECO:0000269|PubMed:16926418}.
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DR EMBL; CR380959; CAG62511.1; -; Genomic_DNA.
DR RefSeq; XP_449535.1; XM_449535.1.
DR AlphaFoldDB; Q6FJQ9; -.
DR SMR; Q6FJQ9; -.
DR STRING; 5478.XP_449535.1; -.
DR PRIDE; Q6FJQ9; -.
DR EnsemblFungi; CAG62511; CAG62511; CAGL0M04323g.
DR GeneID; 2891544; -.
DR KEGG; cgr:CAGL0M04323g; -.
DR CGD; CAL0136273; ACE2.
DR VEuPathDB; FungiDB:CAGL0M04323g; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_021006_0_0_1; -.
DR InParanoid; Q6FJQ9; -.
DR OMA; FQHTPTK; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IEA:EnsemblFungi.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0060196; P:positive regulation of antisense RNA transcription; IEA:EnsemblFungi.
DR GO; GO:2001043; P:positive regulation of septum digestion after cytokinesis; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 3: Inferred from homology;
KW Cell adhesion; Cell wall biogenesis/degradation; Coiled coil;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Virulence; Zinc; Zinc-finger.
FT CHAIN 1..703
FT /note="Cell wall transcription factor ACE2"
FT /id="PRO_0000422793"
FT ZN_FING 523..547
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..577
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..602
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 148..187
FT /evidence="ECO:0000255"
FT COMPBIAS 465..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 79480 MW; E0960AA4A2AAF171 CRC64;
MNTFQADWGE IPQMPKDQVF TPQDQLTNYN DNMMDNLLDF NYNDVDALLS EELKDLDIPL
APSPRDLNMN AEQSLNWMQD IQGHRSNKPS MSHKRGMSGT AIFGFKNHNK TLSIASFSKN
TDIINEAENE NVKGNTDNQN GFVLSQVLLK QQEELRLALE KQKEVNRNLE RQLRENRLQQ
EHIQRVLHDQ EAVTSQLTAQ NVTESPSKQR SPTKYQGDDA IIVTKNSSSG GYVFPPPPRV
TLNNEAVTPP LSFSRFSNID QMESSDPLNY LQPNADFTEA YASHKTPESS FGKEHASVLS
TSEFLRPTNA ARESSSKAMY SSPNSMISPH RKKDSVLSTV STILQPQDDY QNTASPPSQM
LNLEEANLEN EQKNNGKMLR APVEIMPTIP GSKNNTPMTA NKSGFMPQKH TFQHTPVKAK
NNVDMNERSL VRPELSGTPL NKSVQNGMHF REEDDSNILH HISEIPQGST SHNNTTAGDD
SNVSNRLQFS NTESSPSRQR KKPTTLPPGY IDRYVKELPD KNFECLFPNC GKFFRRRYNI
KSHIQTHLED KPYKCDFEGC TKAFVRNHDL ARHKKTHDKH FSCPCGKKFS SEQSMMKHKN
RHNCTGPARV PDSKMVSKSP RKQSSPTKLS SAIMNSPIKE NYLKENTNLH IDQLRMDPKM
RNALEDGGLL KPVERTEAMA FPSPLSGYSD LGSPFRDLGT IEE