WETA_ASPFU
ID WETA_ASPFU Reviewed; 566 AA.
AC Q4WQL4;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Developmental regulatory protein wetA {ECO:0000305};
GN Name=wetA {ECO:0000303|PubMed:18298443}; ORFNames=AFUA_4G13230;
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 INDUCTION.
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 [3]
RP INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20966095; DOI=10.1099/mic.0.044271-0;
RA Tao L., Yu J.H.;
RT "AbaA and WetA govern distinct stages of Aspergillus fumigatus
RT development.";
RL Microbiology 157:313-326(2011).
RN [4]
RP INDUCTION.
RX PubMed=22822234; DOI=10.1128/ec.00032-12;
RA Lamoth F., Juvvadi P.R., Fortwendel J.R., Steinbach W.J.;
RT "Heat shock protein 90 is required for conidiation and cell wall integrity
RT in Aspergillus fumigatus.";
RL Eukaryot. Cell 11:1324-1332(2012).
RN [5]
RP FUNCTION.
RX PubMed=24123270; DOI=10.1128/ec.00217-13;
RA Upadhyay S., Torres G., Lin X.;
RT "Laccases involved in 1,8-dihydroxynaphthalene melanin biosynthesis in
RT Aspergillus fumigatus are regulated by developmental factors and copper
RT homeostasis.";
RL Eukaryot. Cell 12:1641-1652(2013).
RN [6]
RP INDUCTION.
RX PubMed=26190922; DOI=10.5941/myco.2015.43.2.150;
RA Seo Y.H., Kim S.S., Shin K.S.;
RT "In vitro antifungal activity and mode of action of 2',4'-dihydroxychalcone
RT against Aspergillus fumigatus.";
RL Mycobiology 43:150-156(2015).
CC -!- FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore
CC development and conidium maturation (By similarity). They act
CC individually and together to regulate their own expression and that of
CC numerous other sporulation-specific genes (By similarity). Plays an
CC essential role in the completion of conidial maturation and is
CC essential for trehalose biogenesis in conidia (PubMed:20966095).
CC Negatively regulates expression of the melanin biosynthetic gene
CC cluster (PubMed:24123270). Also plays an a role in the early phase of
CC fungal growth including proper hyphal branching (PubMed:20966095).
CC {ECO:0000250|UniProtKB:P22022, ECO:0000269|PubMed:20966095,
CC ECO:0000269|PubMed:24123270}.
CC -!- INDUCTION: Highly expressed during conidiation (PubMed:18298443,
CC PubMed:20966095). Expression is positively regulated by hsp90
CC (PubMed:22822234). Expression is also controlled by upstream regulators
CC calA and crzA (PubMed:18298443). Expression is decreased by 2',4'-
CC Dihydroxychalcone (2',4'-DHC) (PubMed:26190922).
CC {ECO:0000269|PubMed:18298443, ECO:0000269|PubMed:20966095,
CC ECO:0000269|PubMed:22822234, ECO:0000269|PubMed:26190922}.
CC -!- DISRUPTION PHENOTYPE: Causes the formation of defective spore walls and
CC a lack of trehalose biogenesis, leading to a rapid loss of spore
CC viability and reduced tolerance to various stresses (PubMed:20966095).
CC Leads also to delayed germtube formation and reduced hyphal branching
CC (PubMed:20966095). {ECO:0000269|PubMed:20966095}.
CC -!- SIMILARITY: Belongs to the wetA family. {ECO:0000305}.
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DR EMBL; AAHF01000005; EAL89470.1; -; Genomic_DNA.
DR RefSeq; XP_751508.1; XM_746415.1.
DR AlphaFoldDB; Q4WQL4; -.
DR STRING; 746128.CADAFUBP00006832; -.
DR EnsemblFungi; EAL89470; EAL89470; AFUA_4G13230.
DR GeneID; 3509534; -.
DR KEGG; afm:AFUA_4G13230; -.
DR VEuPathDB; FungiDB:Afu4g13230; -.
DR eggNOG; ENOG502S8IT; Eukaryota.
DR HOGENOM; CLU_030750_0_0_1; -.
DR InParanoid; Q4WQL4; -.
DR OMA; MAYQEAW; -.
DR OrthoDB; 638649at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0042243; P:asexual spore wall assembly; IMP:AspGD.
DR GO; GO:0048315; P:conidium formation; IMP:CACAO.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:AspGD.
DR InterPro; IPR040112; WetA.
DR PANTHER; PTHR22934:SF23; PTHR22934:SF23; 1.
PE 2: Evidence at transcript level;
KW Activator; Conidiation; Reference proteome; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..566
FT /note="Developmental regulatory protein wetA"
FT /id="PRO_0000435926"
FT REGION 116..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 61506 MW; 0CF923CEA35523BD CRC64;
MFAQPFDHAF NDLFSQYVDM DSSMVDGNKD VSIPSDFDQI FSLDSLSSDC GDHSPPVPTK
PTHQSPQPWA TDLWSLPQDA ASSASQCSFT FQDTVHPSAV SDLSFHLEAP PTSHPVPAVT
CKASSRSPST PPATPHHKST KSALVTPKSI RRHRDSHERK LLRKQSFSPS LMRPSQLQAG
RMMYPEAWAQ RFQNFSLHSS GEHLPLSPPP SDILVQHENT PADNVVTHMN HSTEGLSRNP
AEMPSHYETG IFNQSPAISM PSPSAKLLAQ QQQHNYLSQS NNSTMATSSP PSGDDIFSSP
HSSDPQSLSS WHSDSLGGSA LPFTPELQAH DGQAWWPSMP SRVPRQPSYQ HVVSSPAPQR
SIQSNNQHDL MQGGLMIQFD SSFDGSTSAD PSFSSVVTSA PMPQENQNMY SHIPVTPQKY
MNLSAYATPP VQHTSRSPSL SPRGRGSPTQ GSPLRNEAST KTSPHRRGYH GRKLSSQSMN
TPKPVKGPNS SSPGSGSNKS LTVSFVNFTP NDSKKILTGV APSGSSKTKA RREQEARDRR
RKLSEAAINA VRKAGGDVEA LEAVLC
