ID   CARP4_CANAW             Reviewed;         417 AA.
AC   P43093; C4YSF5;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Candidapepsin-4;
DE            EC=3.4.23.24;
DE   AltName: Full=ACP 4;
DE   AltName: Full=Aspartate protease 4;
DE   AltName: Full=Secreted aspartic protease 4;
DE   Flags: Precursor;
GN   Name=SAP4; ORFNames=CAWG_05020;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=7907585; DOI=10.1128/jb.176.6.1702-1710.1994;
RA   Miyasaki S.H., White T.C., Agabian N.;
RT   "A fourth secreted aspartyl proteinase gene (SAP4) and a CARE2 repetitive
RT   element are located upstream of the SAP1 gene in Candida albicans.";
RL   J. Bacteriol. 176:1702-1710(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; L25388; AAA17877.1; -; Unassigned_DNA.
DR   EMBL; CM000312; EEQ46658.1; -; Genomic_DNA.
DR   PIR; A55524; A55524.
DR   AlphaFoldDB; P43093; -.
DR   SMR; P43093; -.
DR   STRING; 5476.P43093; -.
DR   ChEMBL; CHEMBL6179; -.
DR   MEROPS; A01.062; -.
DR   EnsemblFungi; EEQ46658; EEQ46658; CAWG_05020.
DR   VEuPathDB; FungiDB:CAWG_05020; -.
DR   HOGENOM; CLU_013253_9_1_1; -.
DR   OMA; NEAYVAD; -.
DR   BRENDA; 3.4.23.24; 1096.
DR   PHI-base; PHI:125; -.
DR   Proteomes; UP000001429; Chromosome 6.
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..75
FT                   /note="Activation peptide"
FT                   /id="PRO_0000025854"
FT   CHAIN           76..417
FT                   /note="Candidapepsin-4"
FT                   /id="PRO_0000025855"
FT   DOMAIN          89..403
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        122..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        331..369
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  45318 MW;  79634304469FB60A CRC64;
     MFLQNILSVL AFALLIDAAP VKRSTGFVTL DFNVKRSLVD PKDPTVEVKR SPLFLDIEPT
     EIPVDDTGRN DVGKRGPVAV KLDNEIITYS ADITIGSNNQ KLSVIVDTGS SDLWVPDSNA
     VCIPKWPGDR GDFCKNNGSY SPAASSTSKN LNTPFEIKYA DGSVAQGNLY QDTVGIGGVS
     VRDQLFANVR STSAHKGILG IGFQSNEATR TPYDNLPITL KKQGIISKNA YSLFLNSPEA
     SSGQIIFGGI DKAKYSGSLV DLPITSDRTL SVGLRSVNVM GQNVNVNAGV LLDSGTTISY
     FTPNIARSII YALGGQVHYD SSGNEAYVAD CKTSGTVDFQ FDRNLKISVP ASEFLYQLYY
     TNGEPYPKCE IRVRESEDNI LGDNFMRSAY IVYDLDDRKI SMAQVKYTSQ SNIVGIN