ID   CARP9_CANAX             Reviewed;         544 AA.
AC   O42779;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Candidapepsin-9;
DE            EC=3.4.23.24;
DE   AltName: Full=ACP 9;
DE   AltName: Full=Aspartate protease 9;
DE   AltName: Full=Secreted aspartic protease 9;
DE   Flags: Precursor;
GN   Name=SAP9;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C74;
RX   PubMed=9802014; DOI=10.1099/00221287-144-10-2731;
RA   Monod M., Hube B., Hess D., Sanglard D.;
RT   "Differential regulation of SAP8 and SAP9, which encode two new members of
RT   the secreted aspartic proteinase family in Candida albicans.";
RL   Microbiology 144:2731-2737(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage at the carboxyl of hydrophobic amino
CC         acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-
CC         Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades
CC         keratin.; EC=3.4.23.24;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: O-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; AF043331; AAC69996.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42779; -.
DR   SMR; O42779; -.
DR   ChEMBL; CHEMBL6139; -.
DR   MEROPS; A01.067; -.
DR   PRIDE; O42779; -.
DR   VEuPathDB; FungiDB:C3_03870C_A; -.
DR   VEuPathDB; FungiDB:CAWG_02704; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR47965; PTHR47965; 1.
DR   Pfam; PF00026; Asp; 2.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..?
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025864"
FT   CHAIN           ?..544
FT                   /note="Candidapepsin-9"
FT                   /id="PRO_0000025865"
FT   DOMAIN          65..479
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          31..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
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        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        406..441
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   544 AA;  58625 MW;  E6D755A46040A486 CRC64;
     MRLNSVALLS LVATALAAKA PFKIDFEVRR GESKDDLSPE DDSNPRFVKR DGSLDMTLTN
     KQTFYMATLK IGSNEDENRV LEDTGSSDLW VMSHDLKCVS APISKRNERS FGHGTGVKLN
     ERELMQKRKN LYQPSRTIET DEEKEASEKI HNKLFGFGSI YSTVYITEGP GAYSTFSPLV
     GTEGGSGGSG GSNTCRSYGS FNTENSDTFK KNNTNDFEIQ YADDTSAIGI WGYDDVTISN
     VTVKDLSFAI ANETSSDVGV LGIGLPGLEV TTQLRYTYQN LPLKLKADGI IAKSLYSLYL
     NTADAKAGSI LFGAIDHAKY QGDLVTVKMM RTYSQISYPV RIQVPVLKID VESSSGSTTN
     ILSGTTGVVL DTGSTLSYVF SDTLQSLGKA LNGQYSNSVG AYVVNCNLAD SSRTVDIEFG
     GNKTIKVPIS DLVLQASKST CILGVMQQSS SSSYMLFGDN ILRSAYIVYD LDDYEVSLAQ
     VSYTNKESIE VIGASGITNS SGSGTTSSSG TSTSTSTRHS AGSIISNPVY GLLLSLLISY
     YVLV