ID   NPIIA_TRIRU             Reviewed;         360 AA.
AC   C0IPP1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Probable neutral protease 2 homolog A;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin A;
DE   Flags: Precursor;
GN   Name=NpII-A;
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].
RA   Monod M., Lechenne B., Zaugg C.;
RT   "Trichophyton rubrum secreted neutral proteases II.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable secreted metalloprotease that shows high activities
CC       on basic nuclear substrates such as histone and protamine (By
CC       similarity). May be involved in virulence. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC         P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.;
CC         EC=3.4.24.39;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P46076};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P46076};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; EU445234; ACC65885.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0IPP1; -.
DR   SMR; C0IPP1; -.
DR   MEROPS; M35.001; -.
DR   VEuPathDB; FungiDB:TERG_03599; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW   Virulence; Zinc; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..183
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000388462"
FT   CHAIN           184..360
FT                   /note="Probable neutral protease 2 homolog A"
FT                   /id="PRO_0000388463"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        191..262
FT                   /evidence="ECO:0000250|UniProtKB:P46076"
FT   DISULFID        269..287
FT                   /evidence="ECO:0000250|UniProtKB:P46076"
FT   DISULFID        300..360
FT                   /evidence="ECO:0000250|UniProtKB:P46076"
SQ   SEQUENCE   360 AA;  38803 MW;  4C13BAC89716CFDE CRC64;
     MQFTALLAAL GAPLALAASI PAAAHNHTMI DVQLAATGNS MIKATITNTG DRTLNLLKFN
     TIMDEHPTRK VMVYQDGAEV QFTGMLPRYK MSDLTPEYFV NLGPKASVEH SFDLAATHDL
     SRGGKITVKA HGMVPTAEEN ATTITGHTLY ESNELTMDVD GKQAAAVEQA MGGDDSTGVI
     DKRSNIVTSS CRGSQLRVLQ TALSNASRLS RAAASAAQRN PSKMREYFKT ADKPHRPEGA
     SRFLSVARES SSGSTGRTTY YCNDNRGGCH PGVLAYTLPS RNQVFNCPSY YQLPALNNRC
     HGQDQATTTL HELTHNPAVV TPFCEDLGYG YQRVSALPAS KAIQNADTYS LFANAIYLGC