HAPX_ASPFU
ID HAPX_ASPFU Reviewed; 491 AA.
AC Q4WER3;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=bZIP transcription factor hapX {ECO:0000303|PubMed:20941352};
DE AltName: Full=Iron acquisition regulator hapX {ECO:0000303|PubMed:20941352};
GN Name=hapX {ECO:0000303|PubMed:20941352}; ORFNames=AFUA_5G03920;
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.
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=21062375; DOI=10.1111/j.1365-2958.2010.07389.x;
RA Liu H., Gravelat F.N., Chiang L.Y., Chen D., Vanier G., Ejzykowicz D.E.,
RA Ibrahim A.S., Nierman W.C., Sheppard D.C., Filler S.G.;
RT "Aspergillus fumigatus AcuM regulates both iron acquisition and
RT gluconeogenesis.";
RL Mol. Microbiol. 78:1038-1054(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20941352; DOI=10.1371/journal.ppat.1001124;
RA Schrettl M., Beckmann N., Varga J., Heinekamp T., Jacobsen I.D., Joechl C.,
RA Moussa T.A., Wang S., Gsaller F., Blatzer M., Werner E.R., Niermann W.C.,
RA Brakhage A.A., Haas H.;
RT "HapX-mediated adaption to iron starvation is crucial for virulence of
RT Aspergillus fumigatus.";
RL PLoS Pathog. 6:E1001124-E1001124(2010).
CC -!- FUNCTION: Transcription factor required for repression of genes during
CC iron starvation (PubMed:21062375). Represses iron-dependent and
CC mitochondrial-localized activities including respiration, TCA cycle,
CC amino acid metabolism, iron-sulfur-cluster and heme biosynthesis
CC (PubMed:21062375). Iron starvation causes a massive remodeling of the
CC amino acid pool and hapX is essential for the coordination of the
CC production of siderophores and their precursor ornithine
CC (PubMed:21062375). {ECO:0000269|PubMed:21062375}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- INDUCTION: Expression is repressed by iron (PubMed:21062375).
CC Expression is induced by the zinc cluster transcription factor acuM to
CC stimulate expression of genes involved in both reductive iron
CC assimilation and siderophore-mediated iron uptake (PubMed:20941352).
CC {ECO:0000269|PubMed:20941352, ECO:0000269|PubMed:21062375}.
CC -!- DISRUPTION PHENOTYPE: Causes decreased production of
CC triacetylfusarinine C (TAFC) but not fusarinine C (FsC)
CC (PubMed:21062375). Attenuates virulence in a murine model of invasive
CC aspergillosis (PubMed:21062375). Also increases zinc sensitivity
CC (PubMed:21062375). {ECO:0000269|PubMed:21062375}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000011; EAL85914.1; -; Genomic_DNA.
DR RefSeq; XP_747952.1; XM_742859.1.
DR AlphaFoldDB; Q4WER3; -.
DR SMR; Q4WER3; -.
DR STRING; 746128.CADAFUBP00005131; -.
DR EnsemblFungi; EAL85914; EAL85914; AFUA_5G03920.
DR GeneID; 3505667; -.
DR KEGG; afm:AFUA_5G03920; -.
DR VEuPathDB; FungiDB:Afu5g03920; -.
DR eggNOG; ENOG502QUE5; Eukaryota.
DR HOGENOM; CLU_014054_0_0_1; -.
DR InParanoid; Q4WER3; -.
DR OMA; MEIDFTA; -.
DR OrthoDB; 1381229at2759; -.
DR PHI-base; PHI:2512; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:AspGD.
DR GO; GO:0031171; P:ferricrocin biosynthetic process; IMP:AspGD.
DR GO; GO:1900551; P:N',N'',N'''-triacetylfusarinine C biosynthetic process; IMP:AspGD.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR018287; Hap4_TF_heteromerisation.
DR Pfam; PF10297; Hap4_Hap_bind; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..491
FT /note="bZIP transcription factor hapX"
FT /id="PRO_0000444414"
FT DOMAIN 55..95
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 19..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..79
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 83..90
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 149..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 53052 MW; B5CE042524661816 CRC64;
MSTPSIAPAP APLVPALAAK PAISPSPGPG TPGSITSKEW VIPPRPKPGR KPATDTPPTK
RKAQNRAAQR AFRERRAARV NELEEQIKKI EDEHEIHIAA FKEQITNLSR EVEQCRSEMT
WWRDRCHALE KEVSVERSAK EAIVKEFRSS LSDREAVRSD KGLAPLTTST PQARSSDRPD
NGDASNNDSG EGREEVPLGC NDCSTSHCQC IEDAFTMPGV VAQEQSRRLD TTKPGLSEPQ
IKPDPEEMEI DFTSRFAATQ QQDQSPTSVS SPAVDPCGFC SDGTPCICAE MAAQEEQRPR
RNSFENNRLA PIQNLSQFTP PPSDGDVRSD VTLPPISQAT NPCANGPGTC AQCLADPRRT
LFCKTLAASR SPSAAPSGCC GGKGADGGCC QSRNTNVSRG RSGSNNNTSS GSSAAPSLTL
SCADAYTTLS RHPNFSRATD ELSTWLPKLH TLPKPRDFPL TDRGVPRAAL EVEAASVMGV
LRYFDRRFAD K
