ID   DEFTR_TRIIM             Reviewed;          85 AA.
AC   A0A059J5P2;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Fungal defensin triintsin {ECO:0000303|PubMed:30102941};
DE   Flags: Precursor;
GN   ORFNames=H109_04975;
OS   Trichophyton interdigitale (strain MR816).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=1215338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR816;
RX   PubMed=29467168; DOI=10.1534/genetics.117.300573;
RA   Persinoti G.F., Martinez D.A., Li W., Doegen A., Billmyre R.B.,
RA   Averette A., Goldberg J.M., Shea T., Young S., Zeng Q., Oliver B.G.,
RA   Barton R., Metin B., Hilmioglu-Polat S., Ilkit M., Graeser Y.,
RA   Martinez-Rossi N.M., White T.C., Heitman J., Cuomo C.A.;
RT   "Whole-genome analysis illustrates global clonal population structure of
RT   the ubiquitous dermatophyte pathogen Trichophyton rubrum.";
RL   Genetics 208:1657-1669(2018).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SYNTHESIS OF 48-85, AND
RP   3D-STRUCTURE MODELING.
RC   STRAIN=H6;
RX   PubMed=30102941; DOI=10.1016/j.peptides.2018.08.003;
RA   Shen B., Song J., Zhao Y., Zhang Y., Liu G., Li X., Guo X., Li W., Cao Z.,
RA   Wu Y.;
RT   "Triintsin, a human pathogenic fungus-derived defensin with broad-spectrum
RT   antimicrobial activity.";
RL   Peptides 107:61-67(2018).
CC   -!- FUNCTION: Antimicrobial peptide with broad-spectrum activity against
CC       Gram-positive bacteria, Gram-negative bacteria, and fungi. Also
CC       inhibits clinical isolates, including methicillin-resistant S.aureus
CC       (MRSA) (MIC=32 uM), K.pneumoniae, C.albicans and C.parapsilosis.
CC       Displays minimal inhibitory concentration (MIC) values similar to
CC       minimal bactericidal concentrations (MBC), suggesting a disruptive
CC       mechanism mode of action associated with membrane lysis. In vitro,
CC       shows hemolytic activity against human red blood cells.
CC       {ECO:0000269|PubMed:29467168}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Disulfide bonds are essential for antimicrobial activity.
CC       {ECO:0000269|PubMed:30102941}.
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=03010";
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DR   EMBL; AOKY01000319; KDB23160.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059J5P2; -.
DR   SMR; A0A059J5P2; -.
DR   EnsemblFungi; KDB23160; KDB23160; H109_04975.
DR   HOGENOM; CLU_116797_0_0_1; -.
DR   OMA; CPLNERE; -.
DR   Proteomes; UP000024533; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF01097; Defensin_2; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Cytolysis;
KW   Defensin; Disulfide bond; Fungicide; Immunity; Innate immunity;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..47
FT                   /evidence="ECO:0000305|PubMed:30102941"
FT                   /id="PRO_0000449381"
FT   CHAIN           48..85
FT                   /note="Fungal defensin triintsin"
FT                   /id="PRO_5001579330"
FT   DISULFID        51..72
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7,
FT                   ECO:0000305|PubMed:30102941"
FT   DISULFID        58..80
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7,
FT                   ECO:0000305|PubMed:30102941"
FT   DISULFID        62..82
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7,
FT                   ECO:0000305|PubMed:30102941"
SQ   SEQUENCE   85 AA;  8882 MW;  06D1665F8D68B19A CRC64;
     MQFTKLATVL IVSLMGSAAI AAPSVDNAPA VAAEEVAAAP AENLEKRGFG CPLNERECHS
     HCQSIGRKFG YCGGTLRLTC ICGKE