CRZA_ASPFU
ID CRZA_ASPFU Reviewed; 754 AA.
AC Q4WJ81;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=C2H2 finger domain transcription factor crzA {ECO:0000305};
GN Name=crzA {ECO:0000303|PubMed:18298443, ECO:0000303|PubMed:18456861};
GN ORFNames=AFUA_1G06900;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18456861; DOI=10.1128/ec.00086-08;
RA Cramer R.A. Jr., Perfect B.Z., Pinchai N., Park S., Perlin D.S.,
RA Asfaw Y.G., Heitman J., Perfect J.R., Steinbach W.J.;
RT "Calcineurin target CrzA regulates conidial germination, hyphal growth, and
RT pathogenesis of Aspergillus fumigatus.";
RL Eukaryot. Cell 7:1085-1097(2008).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=18298443; DOI=10.1111/j.1365-2958.2008.06122.x;
RA Soriani F.M., Malavazi I., da Silva Ferreira M.E., Savoldi M.,
RA Von Zeska Kress M.R., de Souza Goldman M.H., Loss O., Bignell E.,
RA Goldman G.H.;
RT "Functional characterization of the Aspergillus fumigatus CRZ1 homologue,
RT CrzA.";
RL Mol. Microbiol. 67:1274-1291(2008).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19015336; DOI=10.1128/aac.01154-08;
RA Fortwendel J.R., Juvvadi P.R., Pinchai N., Perfect B.Z., Alspaugh J.A.,
RA Perfect J.R., Steinbach W.J.;
RT "Differential effects of inhibiting chitin and 1,3-{beta}-D-glucan
RT synthesis in ras and calcineurin mutants of Aspergillus fumigatus.";
RL Antimicrob. Agents Chemother. 53:476-482(2009).
RN [5]
RP FUNCTION.
RX PubMed=20078882; DOI=10.1186/1471-2180-10-12;
RA Soriani F.M., Malavazi I., Savoldi M., Espeso E., Dinamarco T.M.,
RA Bernardes L.A., Ferreira M.E., Goldman M.H., Goldman G.H.;
RT "Identification of possible targets of the Aspergillus fumigatus CRZ1
RT homologue, CrzA.";
RL BMC Microbiol. 10:12-12(2010).
RN [6]
RP FUNCTION.
RX PubMed=22649543; DOI=10.1371/journal.pone.0037591;
RA Dinamarco T.M., Freitas F.Z., Almeida R.S., Brown N.A., dos Reis T.F.,
RA Ramalho L.N., Savoldi M., Goldman M.H., Bertolini M.C., Goldman G.H.;
RT "Functional characterization of an Aspergillus fumigatus calcium
RT transporter (PmcA) that is essential for fungal infection.";
RL PLoS ONE 7:E37591-E37591(2012).
RN [7]
RP FUNCTION, AND PROMOTER-BINDING.
RX PubMed=25196896; DOI=10.1111/mmi.12785;
RA de Castro P.A., Chen C., de Almeida R.S., Freitas F.Z., Bertolini M.C.,
RA Morais E.R., Brown N.A., Ramalho L.N., Hagiwara D., Mitchell T.K.,
RA Goldman G.H.;
RT "ChIP-seq reveals a role for CrzA in the Aspergillus fumigatus high-
RT osmolarity glycerol response (HOG) signalling pathway.";
RL Mol. Microbiol. 94:655-674(2014).
CC -!- FUNCTION: Transcription factor involved in the regulation of calcium
CC ion homeostasis (PubMed:18298443). Regulates genes encoding calcium
CC transporters, transcription factors and genes that could be directly or
CC indirectly involved in calcium metabolism (PubMed:20078882). Supports
CC especially pmcA, pmcB and pmcC expression encoding for calcium-
CC translocating P-type ATPases (PubMed:18298443, PubMed:22649543). Binds
CC target promoters at motif A[GT][CG]CA[AC][AG] (PubMed:25196896). Plays
CC an essential role germination, radial growth, and asexual development
CC (PubMed:18456861, PubMed:18298443). Also plays a major role in proper
CC chitin and glucan incorporation into the cell wall (PubMed:19015336).
CC Involved in the high-osmolarity glycerol response (HOG) signaling
CC pathway (PubMed:25196896). Required for pathogenicity in an
CC experimental murine model of invasive pulmonary aspergillosis
CC (PubMed:18456861, PubMed:18298443, PubMed:22649543, PubMed:25196896).
CC {ECO:0000269|PubMed:18298443, ECO:0000269|PubMed:18456861,
CC ECO:0000269|PubMed:19015336, ECO:0000269|PubMed:20078882,
CC ECO:0000269|PubMed:22649543, ECO:0000269|PubMed:25196896}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18298443}. Cytoplasm
CC {ECO:0000269|PubMed:18298443}. Note=Localizes predominantly to the
CC cytosol of the cell in the absence of added calcium and translocates to
CC the nucleus following exposure to CaCl(2).
CC {ECO:0000269|PubMed:18298443}.
CC -!- DISRUPTION PHENOTYPE: Leads to reduced levels of beta-1,3-glucan in the
CC cell wall and impairs pathogenicity in an experimental murine model of
CC invasive pulmonary aspergillosis (PubMed:18456861, PubMed:18298443,
CC PubMed:19015336). Increases sensitivity to heat shock
CC (PubMed:18298443). {ECO:0000269|PubMed:18298443,
CC ECO:0000269|PubMed:18456861}.
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DR EMBL; AAHF01000007; EAL88401.1; -; Genomic_DNA.
DR RefSeq; XP_750439.1; XM_745346.1.
DR AlphaFoldDB; Q4WJ81; -.
DR STRING; 746128.CADAFUBP00000716; -.
DR EnsemblFungi; EAL88401; EAL88401; AFUA_1G06900.
DR GeneID; 3507698; -.
DR KEGG; afm:AFUA_1G06900; -.
DR VEuPathDB; FungiDB:Afu1g06900; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_014490_0_0_1; -.
DR InParanoid; Q4WJ81; -.
DR OMA; TQKHPAT; -.
DR OrthoDB; 629102at2759; -.
DR PHI-base; PHI:2509; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IDA:AspGD.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
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:0071277; P:cellular response to calcium ion; IMP:AspGD.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:AspGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009847; P:spore germination; IMP:AspGD.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:AspGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
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 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Virulence; Zinc; Zinc-finger.
FT CHAIN 1..754
FT /note="C2H2 finger domain transcription factor crzA"
FT /id="PRO_0000435644"
FT ZN_FING 548..570
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 576..598
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 604..635
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 81905 MW; BBC9628267D3B26D CRC64;
MASQEMFPEL GQSPAPGVKS RGVSRSPHPH QQQQQQQHQQ HQGQFTGTVT GLDLDSSIAT
ASSFANSSFD PNSNNVSPSA ESYGYTAAGY LSGTPASQTD QNYANSLQIP QSYGTGLVPQ
FNESRGLPIQ QQSQQQHHQQ PSLDDNFSDL LNSNATEYDF NTVYQTHSPS SNTAPEYDSS
LLLDPQVHQQ SHPTQIPSSH SSTSPQISPL EQQQHSSPGP MSTQGSTTVA YYTPQHSRHA
SLDPATAAFL TSNTHPDWQA VMGNSAAFQG HRRAPSEVSE ISSAAPSPYL SQHESFDGVD
NNPSPLLAPQ NDPSLYDSAL GIENFTLSEQ HQQHQGFSPA HSPYISPRLM PQQGQEMMPN
VPYLSGPAPN TQYPTPPNDM YGNGAEGMMN MSQGTHPSVD IGQASQMAPP SINVEFAPPS
RIPSFGPSKP ASNLDSLSPP PSSTRSRGRS KSDPYAHPST SRLRSSSTSS SLDPLAPTTP
RSLSPFDSFG RQQQSNPSSR DPSPSRSNRR LSTSSIDSRN YILGLADPQR PGASPNDSKR
VQKHPATFQC NLCPKRFTRA YNLRSHLRTH TDERPFVCTV CGKAFARQHD RKRHEGLHSG
EKKFVCQGEL SRGGQWGCGR RFARADALGR HFRSEAGRIC IKPLLDEESQ ERERSLMDQQ
QHHLQPLPQQ VMVPVDNPHA GNFVLPAALL AQYPALQTLQ WDQIAASADD PSDIGGRSSF
DASSGNEFGF EDDDSGLSSV SGINAGYSAA GNFY
