ID   SUB3_TRIRU              Reviewed;         397 AA.
AC   Q69F56;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Subtilisin-like protease 3;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB3;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=15363848; DOI=10.1016/j.gene.2004.06.024;
RA   Jousson O., Lechenne B., Bontems O., Mignon B., Reichard U., Barblan J.,
RA   Quadroni M., Monod M.;
RT   "Secreted subtilisin gene family in Trichophyton rubrum.";
RL   Gene 339:79-88(2004).
RN   [2]
RP   INDUCTION.
RX   PubMed=19098130; DOI=10.1128/ec.00208-08;
RA   Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J.,
RA   Bueno M., Giddey K., Staib P.;
RT   "Gene expression profiling in the human pathogenic dermatophyte
RT   Trichophyton rubrum during growth on proteins.";
RL   Eukaryot. Cell 8:241-250(2009).
CC   -!- FUNCTION: Secreted subtilisin-like serine protease with keratinolytic
CC       activity that contributes to pathogenicity.
CC       {ECO:0000269|PubMed:15363848}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15363848}.
CC   -!- INDUCTION: Expression is strongly increased during growth on protein-
CC       rich medium. Expressed at even higher levels when keratin is present in
CC       the protein-rich medium. {ECO:0000269|PubMed:19098130}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AY343501; AAR11462.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q69F56; -.
DR   SMR; Q69F56; -.
DR   MEROPS; S08.115; -.
DR   PRIDE; Q69F56; -.
DR   VEuPathDB; FungiDB:TERG_03815; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..116
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380780"
FT   CHAIN           117..397
FT                   /note="Subtilisin-like protease 3"
FT                   /id="PRO_0000380781"
FT   DOMAIN          35..116
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          126..397
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        189
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        344
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   397 AA;  41001 MW;  3C99AE8EB268F38E CRC64;
     MGCIKVISVF LAAVAAVDAR AFFHNRGGND VIPNSYIVVM KDGVTAEDFD SHISSVAATH
     SLNKAKRGSE TVGHKDSFNI NGWRAYNGHF DEATIESILK DDKVNYVEHD RVVKLAALTT
     QPNAPTWGLG RVSHKAPGNK DFVYDSSAGQ GITIYGVDTG IDIHHSEFAG RIRWGTNTVD
     NDNTDGNGHG THTAGTFAGT TYGVAKKANI VAVKVLSAGG SGSTSGVIKG IDWCVTDARS
     KNTLGKAALN LSLGGSFSQA SNDAVTRAQE AGIFVAVAAG NDNRDAKNSS PASAPAVCTA
     ASSTIDDQKS SFSNWGTIVD IYAPGSNILS AAPGGGTRTL SGTSMASPHV CGVGAAMLAQ
     GVSVAQACNR LKQIGNAVIR NPGTGTTNRL LYNGSGR