THX29_ASPFM
ID THX29_ASPFM Reviewed; 110 AA.
AC Q1RQJ0;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Thioredoxin Asp f 29 {ECO:0000305};
DE Short=Trx {ECO:0000303|PubMed:17182577, ECO:0000303|PubMed:19032234};
DE AltName: Allergen=Asp f 29 {ECO:0000303|PubMed:17182577, ECO:0000303|PubMed:19032234};
GN ORFNames=CDV57_00134 {ECO:0000312|EMBL:OXN30268.1};
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:CAI78450.1};
RN [1] {ECO:0000312|EMBL:CAI78450.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ALLERGEN.
RC STRAIN=ATCC 42202 / AF-102 / Ag 507 {ECO:0000312|EMBL:CAI78450.1};
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] {ECO:0000312|EMBL:OXN30268.1, ECO:0000312|Proteomes:UP000215142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 270 {ECO:0000312|EMBL:OXN30268.1};
RX PubMed=31891387; DOI=10.1093/jac/dkz534;
RA Parent-Michaud M., Dufresne P.J., Fournier E., Folch B., Martineau C.,
RA Moreira S., Doucet N., De Repentigny L., Dufresne S.F.;
RT "Prevalence and mechanisms of azole resistance in clinical isolates of
RT Aspergillus section Fumigati species in a Canadian tertiary care centre,
RT 2000 to 2013.";
RL J. Antimicrob. Chemother. 75:849-858(2020).
RN [3]
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:31891387}.
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 50% 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.
CC {ECO:0000255|PIRNR:PIRNR000077}.
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DR EMBL; AJ937745; CAI78450.1; -; mRNA.
DR EMBL; NKHT01000003; OXN30268.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1RQJ0; -.
DR SMR; Q1RQJ0; -.
DR Allergome; 2679; Asp f 29.
DR OMA; QVGVAPK; -.
DR Proteomes; UP000215142; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 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..110
FT /note="Thioredoxin Asp f 29"
FT /id="PRO_0000449239"
FT DOMAIN 1..110
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 28
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 35
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 36
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT DISULFID 34..37
FT /note="Redox-active"
FT /evidence="ECO:0000255|PIRSR:PIRSR000077-4,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 110 AA; 11976 MW; D8A6510571A7244A CRC64;
MSHNVEKITD AKVFKEKVQE GSGPVIVDCS ATWCGPCKAI SPVFQRLSTS EEFKNAKFYE
IDVDELSEVA AELGVRAMPT FMFFKDGQKV NEVVGANPPA LEAAIKAHVA
