THIO_MALSM
ID THIO_MALSM Reviewed; 105 AA.
AC Q1RQI9;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Thioredoxin {ECO:0000303|PubMed:17182577, ECO:0000303|PubMed:19032234, ECO:0000312|EMBL:CAI78451.1};
DE Short=Trx {ECO:0000303|PubMed:17182577, ECO:0000303|PubMed:19032234};
DE AltName: Full=Allergen Mala s 13 {ECO:0000303|PubMed:17182577, ECO:0000303|PubMed:19032234};
DE AltName: Allergen=Mala s 13.0101 {ECO:0000305};
DE Flags: Fragment;
OS Malassezia sympodialis (Atopic eczema-associated yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=76777 {ECO:0000312|EMBL:CAI78451.1};
RN [1] {ECO:0000312|EMBL:CAI78451.1, ECO:0007744|PDB:2J23}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS),
RP FUNCTION, SUBUNIT, ALLERGEN, AND DISULFIDE BOND.
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, AND ALLERGEN.
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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17182577}.
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 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. {ECO:0000305}.
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DR EMBL; AJ937746; CAI78451.1; -; mRNA.
DR PDB; 2J23; X-ray; 1.41 A; A/B=1-105.
DR PDBsum; 2J23; -.
DR AlphaFoldDB; Q1RQI9; -.
DR SMR; Q1RQI9; -.
DR Allergome; 2680; Mala s 13.
DR Allergome; 3368; Mala s 13.0101.
DR VEuPathDB; FungiDB:MSYG_0361; -.
DR EvolutionaryTrace; Q1RQI9; -.
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 3D-structure; Allergen; Disulfide bond; Redox-active center.
FT CHAIN <1..105
FT /note="Thioredoxin"
FT /id="PRO_0000449240"
FT DOMAIN <1..105
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 29
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 23
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 30
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 31
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT DISULFID 29..32
FT /note="Redox-active"
FT /evidence="ECO:0000255|PIRSR:PIRSR000077-4,
FT ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:17182577, ECO:0007744|PDB:2J23"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAI78451.1"
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:2J23"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:2J23"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2J23"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:2J23"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:2J23"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2J23"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:2J23"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2J23"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:2J23"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:2J23"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:2J23"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:2J23"
SQ SEQUENCE 105 AA; 11456 MW; D3F16024B8ED5D5C CRC64;
VQVISSYDQF KQVTGGDKVV VIDFWATWCG PCKMIGPVFE KISDTPAGDK VGFYKVDVDE
QSQIAQEVGI RAMPTFVFFK NGQKIDTVVG ADPSKLQAAI TQHSA
