ID   CARP2_CANPA             Reviewed;         412 AA.
AC   P32950;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Candidapepsin-2;
DE            EC=3.4.23.24;
DE   AltName: Full=ACP 2;
DE   AltName: Full=Aspartate protease 2;
DE   Flags: Precursor;
GN   Name=SAPP2; Synonyms=ACPL;
OS   Candida parapsilosis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate CHUV E18;
RX   PubMed=8436951; DOI=10.1099/00221287-139-2-335;
RA   de Viragh P.A., Sanglard D., Togni G., Falchetto R., Monod M.;
RT   "Cloning and sequencing of two Candida parapsilosis genes encoding acid
RT   proteases.";
RL   J. Gen. Microbiol. 139:335-342(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 62-68.
RC   STRAIN=Isolate CHUV E18;
RX   PubMed=8335087; DOI=10.1016/0014-5793(93)81050-a;
RA   Fusek M., Smith E.A., Monod M., Foundling S.I.;
RT   "Candida parapsilosis expresses and secretes two aspartic proteinases.";
RL   FEBS Lett. 327:108-112(1993).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; Z11918; CAA77976.1; -; Genomic_DNA.
DR   AlphaFoldDB; P32950; -.
DR   SMR; P32950; -.
DR   MEROPS; A01.076; -.
DR   VEuPathDB; FungiDB:CPAR2_102580; -.
DR   BRENDA; 3.4.23.24; 1133.
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   1: Evidence at protein level;
KW   Aspartyl protease; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Signal; Zymogen.
FT   SIGNAL          1..25
FT                   /note="Or 18, or 21"
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..61
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:8335087"
FT                   /id="PRO_0000025871"
FT   CHAIN           62..412
FT                   /note="Candidapepsin-2"
FT                   /id="PRO_0000025872"
FT   DOMAIN          75..383
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        108..113
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..345
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   412 AA;  44443 MW;  6D4DE8B954ADC8B3 CRC64;
     MTTIAIFTKN VLLAIAFALF AQGAAIPDPA KRDDNPGFVA LDFEVTRKPL DVNATSELSK
     RSSPSSPLYF EGPSYGIRVS VGSNKQEQQV VLDTGSSDFW VVDSSASCQK GNCKQYGTFD
     PHSSTSFKSL GSSFRSIGYG DKSSSIGTWG QDTIYLGGTS ITNQRFADVT STSVNQGILG
     VGRVETESAN PPYDNVPITL KKQGKIKTNA YSLYLNSPGA ATGTIIFGGV DNAKYSGKLI
     EEPLVSDRYL AVNLKSLNYN GDNSNAGFGV VVDSGTTISY LPDSIVNDLA NKVGAYLEPV
     GLGNELYFID CNANPQGSAS FTFDNGAKIT VPLSEFVLQS TANACVWGLQ SSDRQNVPPI
     LGDNFLRHAY AFQLDKETVL SRSGEVHFCL KCFSNLETSI VWKAFFYNRY IQ