ID   THX28_ASPFM             Reviewed;         108 AA.
AC   Q1RQJ1;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Thioredoxin Asp f 28 {ECO:0000305};
DE            Short=Trx {ECO:0000303|PubMed:17182577, ECO:0000303|PubMed:19032234};
DE   AltName: Full=Allergen Asp f 28 {ECO:0000303|PubMed:17182577, ECO:0000303|PubMed:19032234};
DE   AltName: Allergen=Asp f 28.0101 {ECO:0000305};
OS   Neosartorya fumigata (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=746128 {ECO:0000312|EMBL:CAI78449.1};
RN   [1] {ECO:0000312|EMBL:CAI78449.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ALLERGEN.
RC   STRAIN=ATCC 42202 / AF-102 / Ag 507 {ECO:0000312|EMBL:CAI78449.1};
RX   PubMed=17182577; DOI=10.4049/jimmunol.178.1.389;
RA   Limacher A., Glaser A.G., Meier C., Schmid-Grendelmeier P., Zeller S.,
RA   Scapozza L., Crameri R.;
RT   "Cross-reactivity and 1.4-A crystal structure of Malassezia sympodialis
RT   thioredoxin (Mala s 13), a member of a new pan-allergen family.";
RL   J. Immunol. 178:389-396(2007).
RN   [2]
RP   FUNCTION, ALLERGEN, AND 3D-STRUCTURE MODELING.
RX   PubMed=19032234; DOI=10.1111/j.1398-9995.2008.01777.x;
RA   Glaser A.G., Menz G., Kirsch A.I., Zeller S., Crameri R., Rhyner C.;
RT   "Auto- and cross-reactivity to thioredoxin allergens in allergic
RT   bronchopulmonary aspergillosis.";
RL   Allergy 63:1617-1623(2008).
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide and
CC       catalyzes dithiol-disulfide exchange reactions.
CC       {ECO:0000269|PubMed:17182577, ECO:0000269|PubMed:19032234}.
CC   -!- ALLERGEN: Causes an allergic reaction in human (PubMed:17182577,
CC       PubMed:19032234). Recombinant protein binds to IgE in atopic eczema-
CC       suffering patients allergic to yeast M.sympodialis (PubMed:17182577).
CC       Recombinant protein binds to IgE in 30% of the 40 patients tested
CC       suffering from allergic bronchopulmonary aspergillosis (ABPA). Causes a
CC       positive skin reaction and induces proliferation of the human
CC       peripheral blood mononuclear cells in ABPA patients allergic to this
CC       protein (PubMed:19032234). {ECO:0000269|PubMed:17182577,
CC       ECO:0000269|PubMed:19032234}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AJ937744; CAI78449.1; -; mRNA.
DR   AlphaFoldDB; Q1RQJ1; -.
DR   SMR; Q1RQJ1; -.
DR   Allergome; 2678; Asp f 28.
DR   Allergome; 3119; Asp f 28.0101.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Redox-active center.
FT   CHAIN           1..108
FT                   /note="Thioredoxin Asp f 28"
FT                   /id="PRO_0000449238"
FT   DOMAIN          1..108
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        33
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   ACT_SITE        36
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   SITE            27
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   SITE            34
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   SITE            35
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   DISULFID        33..36
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   108 AA;  11937 MW;  3BA8C9C9055C5193 CRC64;
     MSHGKVIAVD NPIIYKALTS SGPVVVDFFA TWCGPCRAVA PKVGELSEKY SNVRFIQVDV
     DKVRSVAHEM NIRAMPTFVL YKDGQPLEKR VVGGNVRELE EMIKSISA