SUB6_TRIRU
ID SUB6_TRIRU Reviewed; 412 AA.
AC Q9UW97;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Subtilisin-like protease 6;
DE EC=3.4.21.-;
DE AltName: Allergen=Tri r 2;
DE Flags: Precursor;
GN Name=SUB6;
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 [MRNA].
RX PubMed=9792655; DOI=10.1074/jbc.273.45.29489;
RA Woodfolk J.A., Wheatley L.M., Piyasena R.V., Benjamin D.C.,
RA Platts-Mills T.A.E.;
RT "Trichophyton antigens associated with IgE antibodies and delayed type
RT hypersensitivity. Sequence homology to two families of serine
RT proteinases.";
RL J. Biol. Chem. 273:29489-29496(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14001;
RX PubMed=15243098; DOI=10.1128/jcm.42.7.3298-3299.2004;
RA Gao J., Takashima A.;
RT "Cloning and characterization of Trichophyton rubrum genes encoding actin,
RT Tri r2, and Tri r4.";
RL J. Clin. Microbiol. 42:3298-3299(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Capoccia S., Lechenne B., Zaugg C., Monod M.;
RT "Trichophyton rubrum encoding alkaline protease.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: Expression is strongly increased during growth on protein-
CC rich medium. {ECO:0000269|PubMed:19098130}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AF082515; AAD52013.1; -; mRNA.
DR EMBL; AF420485; AAN32713.1; -; Genomic_DNA.
DR EMBL; AY525330; AAS19460.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UW97; -.
DR SMR; Q9UW97; -.
DR Allergome; 3505; Tri r 2.0101.
DR Allergome; 652; Tri r 2.
DR VEuPathDB; FungiDB:TERG_02990; -.
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; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
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; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Virulence; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..126
FT /evidence="ECO:0000250"
FT /id="PRO_0000380810"
FT CHAIN 127..412
FT /note="Subtilisin-like protease 6"
FT /id="PRO_0000380811"
FT DOMAIN 36..120
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 135..412
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 358
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
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 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 412 AA; 42709 MW; 66DEF37259660AC3 CRC64;
MGFITKAIPI VLAALSTVNG ARILEAGPHA EAIPNKYIVV MKREVSDEAF NAHTTWLSQS
LNSRIMRRAG SSKPMAGMQD KYSLGGIFRA YSGEFDDAMI KDISSHDDVD FIEPDFVVRT
TTNGTNLTHQ DNVPSWGLAR VGSKKPGGTT YYYDPSAGKG VTAYIIDTGI DIDHEDFQGR
AKWGENFVDQ QNTDCNGHGT HVAGTVGGTK YGLAKGVSLV AVKVLDCDGS GSNSGVIKGM
EWAMRQASGG GNGTAKAAGK SVMNMSLGGP RSEASNQAAK AISDAGIFMA VAAGNENMDA
QHSSPASEPS VCTVAASTKD DGKADFSNYG AVVDVYAPGK DITSLKPGGS TDTLSGTSMA
SPHVCGLGAY LIGLGKQGGP GLCDTIKKMA NDVIQSPGEG TTGKLIYNGS GK
