ID   SUB4_TRIRU              Reviewed;         399 AA.
AC   Q69F35;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Subtilisin-like protease 4;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=SUB4;
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. Expression levels are the same whether keratin is present
CC       or not in the protein-rich medium. {ECO:0000269|PubMed:19098130}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AY344481; AAR02423.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q69F35; -.
DR   SMR; Q69F35; -.
DR   MEROPS; S08.115; -.
DR   PRIDE; Q69F35; -.
DR   VEuPathDB; FungiDB:TERG_01617; -.
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..118
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380790"
FT   CHAIN           119..399
FT                   /note="Subtilisin-like protease 4"
FT                   /id="PRO_0000380791"
FT   DOMAIN          38..117
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          128..399
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        160
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        191
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        346
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   399 AA;  42197 MW;  9DBFB3AAE1092B63 CRC64;
     MVCLKTLSVF LAAFAAADAR AVFKTQGHKN SEMIPDNYIV VMKDGVSQDD FKAHISSVSS
     IHSTNKAKRG TNTEGMKREF DIMNWRGYHG HFDRDTLEEI LNDSKVDYVE QDQVVRISGL
     VTQRSAPSWG LGRVSHRQAG SRDYVFDDSA GRGVTIYGVD TGIDINHQDF RGRARWGTNT
     ADRDNADRHG HGTHTASTFA GTAYGIAKNA NIVAVKVLGS DGSGSTSGII AGINYCVQDA
     QQRGILGKAA MNLSLGGGFS QANNDAVTRA QNAGIFVAVA AGNDNKDARN YSPASAPAVC
     TVASSTINDS KSSFSNWGPV VDIYAPGSDI IAARPGGGST TMSGTSMASP HVAGMGAYMI
     GMGANPRQVC DRLKQLATAA IRNPGFSTTN RLLYNGSGQ