ID   CARP6_CANAX             Reviewed;         418 AA.
AC   P43095;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Candidapepsin-6;
DE            EC=3.4.23.24;
DE   AltName: Full=ACP 6;
DE   AltName: Full=Aspartate protease 6;
DE   AltName: Full=Secreted aspartic protease 6;
DE   Flags: Precursor;
GN   Name=SAP6;
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=7984113; DOI=10.1111/j.1365-2958.1994.tb00429.x;
RA   Monod M., Togni G., Hube B., Sanglard D.;
RT   "Multiplicity of genes encoding secreted aspartic proteinases in Candida
RT   species.";
RL   Mol. Microbiol. 13:357-368(1994).
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; Z30192; CAA82924.1; -; Genomic_DNA.
DR   PIR; S49057; S42073.
DR   AlphaFoldDB; P43095; -.
DR   SMR; P43095; -.
DR   ChEMBL; CHEMBL6178; -.
DR   MEROPS; A01.064; -.
DR   VEuPathDB; FungiDB:C6_02710C_A; -.
DR   VEuPathDB; FungiDB:CAWG_05098; -.
DR   BRENDA; 3.4.23.24; 1096.
DR   PHI-base; PHI:127; -.
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; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Cleavage on pair of basic residues; Disulfide bond;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..76
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025858"
FT   CHAIN           77..418
FT                   /note="Candidapepsin-6"
FT                   /id="PRO_0000025859"
FT   DOMAIN          90..404
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        123..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        332..370
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   418 AA;  45469 MW;  D32AAF203E096083 CRC64;
     MFLKNILSVL RFALLIDAAP VKRSPGFVTL DFNVKRSLVV PDDPTAESKR SPLFLDLDPT
     QIPVDDTGRN VGVDKRGPVA VKLDNEIITY SADITVGSNN QKLSVIVDTG SSDLWIPDSK
     AICIPKWRGD CGDFCKNNGS YSPAASSTSK NLNTRFEIKY ADGSYAKGNL YQDTVGIGGA
     SVKNQLFANV WSTSAHKGIL GIGFQTNEAT RTPYDNLPIS LKKQGIIAKN AYSLFLNSPE
     ASSGQIIFGG IDKAKYSGSL VELPITSDRT LSVGLRSVNV MGRNVNVNAG VLLDSGTTIS
     YFTPSIARSI IYALGGQVHF DSAGNKAYVA DCKTSGTVDF QFDKNLKISV PASEFLYQLY
     YTNGKPYPKC EIRVRESEDN ILGDNFMRSA YIVYDLDDKK ISMAQVKYTS ESNIVAIN