ID   SCH21_STACH             Reviewed;         144 AA.
AC   C7E9W0;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Antigenic protein SchS21 {ECO:0000303|PubMed:21109751};
DE   AltName: Full=21 kDa secretory protein {ECO:0000303|PubMed:21109751};
DE   AltName: Full=Alkaline exodeoxyribonuclease {ECO:0000303|PubMed:21109751};
DE            EC=3.1.11.- {ECO:0000269|PubMed:21109751};
DE   AltName: Full=SchS21 {ECO:0000303|PubMed:21109751};
DE   AltName: Allergen=Sta c 3.0101 {ECO:0000305};
DE   Flags: Fragment;
OS   Stachybotrys chartarum (Toxic black mold) (Stilbospora chartarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=74722 {ECO:0000312|EMBL:ACT37324.1};
RN   [1] {ECO:0000312|EMBL:ACT37324.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-16; 3-13 AND 75-92,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, AND ALLERGEN.
RC   STRAIN=DAOM 235557 {ECO:0000303|PubMed:21109751};
RC   TISSUE=Mycelium {ECO:0000303|PubMed:21109751};
RX   PubMed=21109751; DOI=10.1159/000317243;
RA   Shi C., Smith M.L., Miller J.D.;
RT   "Characterization of human antigenic proteins SchS21 and SchS34 from
RT   Stachybotrys chartarum.";
RL   Int. Arch. Allergy Immunol. 155:74-85(2011).
RN   [2]
RP   SUBCELLULAR LOCATION, ALLERGEN, REGION, SITES, MUTAGENESIS OF PRO-96;
RP   GLU-98; ARG-100 AND LYS-101, AND 3D-STRUCTURE MODELING.
RX   PubMed=22424314; DOI=10.1016/j.molimm.2012.02.002;
RA   Shi C., Miller J.D.;
RT   "Sta c 3 epitopes and their application as biomarkers to detect specific
RT   IgE.";
RL   Mol. Immunol. 50:271-277(2012).
CC   -!- FUNCTION: Has exodeoxyribonuclease activity with lambda-DNA and salmon
CC       testes dsDNA. No activity with circular plasmid DNA. The physiological
CC       role of this enzyme may be to degrade environmental DNA, and thus
CC       mobilize nitrogen for uptake. {ECO:0000269|PubMed:21109751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:21109751};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.00329 mg/ml for salmon testes dsDNA (at pH 9 and 37 degrees
CC         Celsius) {ECO:0000269|PubMed:21109751};
CC       pH dependence:
CC         Optimum pH is 9. No activity between pH 3-6.
CC         {ECO:0000269|PubMed:21109751};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. Activity is about 80% of
CC         the maximum activity at 35 and 50 degrees Celsius.
CC         {ECO:0000269|PubMed:21109751};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21109751}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22424314}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Natural protein binds
CC       to IgE of patients allergic to toxic black mold fungus
CC       (PubMed:21109751, PubMed:22424314). Recombinant protein binds to IgE of
CC       patients allergic to toxic black mold fungus (PubMed:21109751). Binds
CC       to IgG (PubMed:22424314). {ECO:0000269|PubMed:21109751,
CC       ECO:0000269|PubMed:22424314}.
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DR   EMBL; GQ258855; ACT37324.1; -; mRNA.
DR   Allergome; 9071; Sta c 3.
DR   Allergome; 9507; Sta c 3.0101.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Exonuclease; Glycoprotein; Hydrolase;
KW   Nuclease; Secreted.
FT   CHAIN           <1..144
FT                   /note="Antigenic protein SchS21"
FT                   /id="PRO_0000455632"
FT   REGION          91..105
FT                   /note="IgE-binding epitope"
FT                   /evidence="ECO:0000269|PubMed:22424314"
FT   SITE            100
FT                   /note="Critical for IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:22424314"
FT   SITE            101
FT                   /note="Critical for IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:22424314"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   MUTAGEN         96
FT                   /note="P->A: Increased IgE-binding of the 91-V--P-102 and
FT                   94-M--G-105 peptides."
FT                   /evidence="ECO:0000269|PubMed:22424314"
FT   MUTAGEN         98
FT                   /note="E->A: Increased IgE-binding of the 91-V--P-102 and
FT                   94-M--G-105 peptides."
FT                   /evidence="ECO:0000269|PubMed:22424314"
FT   MUTAGEN         100
FT                   /note="R->A: Significant decrease in IgE-binding of the 91-
FT                   V--P-102 and 94-M--G-105 peptides."
FT                   /evidence="ECO:0000269|PubMed:22424314"
FT   MUTAGEN         101
FT                   /note="K->A: Significant decrease in IgE-binding of the 91-
FT                   V--P-102 and 94-M--G-105 peptides."
FT                   /evidence="ECO:0000269|PubMed:22424314"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ACT37324.1"
SQ   SEQUENCE   144 AA;  15726 MW;  213528A7833A0068 CRC64;
     ASVTFWTLDN VDRTLVFTGN PGSAAIETIT VGPAENTTVE FPGSWVGNWY AYPTDAEDVP
     GMLGEVQFGG WNGLTYFDVS AIVNPTDHDN VKQMWPAESR KPMSGCEVFP CDNAYWLPDD
     IQTKVTHEVD LWTTLGAGST GLTF