HAPX_ARTBC
ID HAPX_ARTBC Reviewed; 474 AA.
AC D4AQY2;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=bZIP transcription factor hapX {ECO:0000303|PubMed:26960149};
DE AltName: Full=Iron acquisition regulator hapX {ECO:0000303|PubMed:26960149};
GN Name=hapX {ECO:0000303|PubMed:26960149}; ORFNames=ARB_06811;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=26960149; DOI=10.1371/journal.pone.0150701;
RA Kroeber A., Scherlach K., Hortschansky P., Shelest E., Staib P.,
RA Kniemeyer O., Brakhage A.A.;
RT "HapX mediates iron homeostasis in the pathogenic dermatophyte Arthroderma
RT benhamiae but is dispensable for virulence.";
RL PLoS ONE 11:E0150701-E0150701(2016).
CC -!- FUNCTION: Iron regulator crucial for the adaptation to iron starvation
CC and iron excess, but is dispensable for virulence (PubMed:26960149).
CC SreA represses the expression of hapX and the siderophore system during
CC iron sufficient conditions by an iron-sensing mechanism, while hapX
CC represses sreA and activates the siderophore system during iron-
CC limiting conditions, resulting in efficient iron uptake and inhibition
CC of iron-consuming pathways (PubMed:26960149). HapX targets include
CC genes encoding a number of key iron-regulated factors such as the
CC vacuolar iron importer cccA, as well as hemA, cycA and lysF involved in
CC heme biosynthesis, respiration and lysine biosynthesis, respectively
CC (PubMed:26960149). Activation of the vacuolar iron importer cccA during
CC high iron conditions is essential for iron detoxification
CC (PubMed:26960149). {ECO:0000269|PubMed:26960149}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- INDUCTION: Expression is highly up-regulated during iron starvation
CC (PubMed:26960149). {ECO:0000269|PubMed:26960149}.
CC -!- DISRUPTION PHENOTYPE: Leads to reduced growth and decreased conidiation
CC during iron starvation, but not during iron-replete conditions
CC (PubMed:26960149). Showed a reddish pigmentation of mycelia during
CC iron-depleted conditions probably due to the accumulation of iron-free
CC precursors of heme (PubMed:26960149). Results in a lacking activation
CC of the siderophore biosynthesis genes sidA and sidC during iron
CC starvation and in a decreased production of extracellular ferrichrome
CC C, but not ferricrocin (PubMed:26960149). Results also in complete
CC deregulation of genes from iron-dependent pathways such as vacuolar
CC iron storage, amino acid metabolism, respiration and heme biosynthesis
CC during iron limitation (PubMed:26960149).
CC {ECO:0000269|PubMed:26960149}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; ABSU01000006; EFE34411.1; -; Genomic_DNA.
DR RefSeq; XP_003015051.1; XM_003015005.1.
DR AlphaFoldDB; D4AQY2; -.
DR SMR; D4AQY2; -.
DR STRING; 663331.D4AQY2; -.
DR EnsemblFungi; EFE34411; EFE34411; ARB_06811.
DR GeneID; 9520774; -.
DR KEGG; abe:ARB_06811; -.
DR eggNOG; ENOG502QUE5; Eukaryota.
DR HOGENOM; CLU_014054_0_0_1; -.
DR OMA; MEIDFTA; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR018287; Hap4_TF_heteromerisation.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF10297; Hap4_Hap_bind; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome.
FT CHAIN 1..474
FT /note="bZIP transcription factor hapX"
FT /id="PRO_0000444415"
FT DOMAIN 67..108
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..91
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 95..102
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 201..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 51706 MW; 1471B9D11651B0FE CRC64;
MSTSAGTPTS AHAPLSIAPA STPHQRSLSV KPLAAAPSPA PVTQCSITSK EWIVPPRPKP
GRKPATDTPP TKRKAQNRAA QRAFRERRAA RVGELEEQIK KIEEENEREE AALKKTIQQQ
QQQIEEYKSQ LLWWKNRCKA VEDELMTEKV AKEDAIKQLE RINNSGRTTN NGNSVIGGCE
RCSSTRCQCI DDAFNIANIT QMQTDDPHSK RGRSPSQGAT QKRHRSNPEI KTEPEDLETD
FTHSFSLRRH SRTGNDATTP ILLDPCGFCQ DGSPCICAEM AEDQPSDRSN QPSQLTKLPP
IQNISQFTPP PSEGDVLSKS ATLVSSNKSN PCANGPGTCA QCLADPRSSV FCKSLAASRA
STRQEGGCCG GGGGKDGCCK NRSSGSDSSK QATSPITLSC ADTFTTLSLH PKFASASNEL
SNWIPQLHTL PNPQNLNPDR RRDQNLTNRP ALEVEAASVM GVLRYFDRRF ADSK
