ID   CARP8_CANAX             Reviewed;         405 AA.
AC   O42778;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Candidapepsin-8;
DE            EC=3.4.23.24;
DE   AltName: Full=ACP 8;
DE   AltName: Full=Aspartate protease 8;
DE   AltName: Full=Secreted aspartic protease 8;
DE   Flags: Precursor;
GN   Name=SAP8;
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; AF043330; AAC69995.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42778; -.
DR   SMR; O42778; -.
DR   ChEMBL; CHEMBL6050; -.
DR   MEROPS; A01.066; -.
DR   VEuPathDB; FungiDB:C3_02510C_A; -.
DR   VEuPathDB; FungiDB:CAWG_02575; -.
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; 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..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..?
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025862"
FT   CHAIN           ?..405
FT                   /note="Candidapepsin-8"
FT                   /id="PRO_0000025863"
FT   DOMAIN          89..392
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          52..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        292
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        122..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        327..358
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  43051 MW;  912FC91979FE39C0 CRC64;
     MVSIITFTKN VLVTLAFALL AQGLAIPEDI DKRAEKVVSL DFTVTRKPFN ATAHGQHHQS
     QQQQQQQQQQ PAQKRGTVQT SLINEGPSYA ATITVGSNKQ QQTVIVDTGS SDLWVVDSAA
     VCQVTYPGQS PTFCKQDGTY KPSSSTTSQN LGKAFSIRYE DGSSSQGTVY KDTIGLGGAS
     ITNQQFADVT TTSVDQGILG IGFTGDESSP TYDNVPVTLK KQGIINKNAY SLYLNSASAS
     SGTIIFGGVD NAKYTGSLTA LPITSSNELR VQLSTINIAG TTVSASTTPV LDSGTTLTYF
     SQTIADKLAA AVGAKWNSYY QLYTSSCNLA GNIVFNFAKG VTISVPLSEF VLQDGNSCYF
     GVSRDSATIL GDNFLRRAYA VYDLDGNTIS LAQVKYTTSS SISTL