ID   CARP1_CANAX             Reviewed;         391 AA.
AC   P0CY26; P28872; Q5A8N4;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Candidapepsin-1;
DE            EC=3.4.23.24;
DE   AltName: Full=ACP 1;
DE   AltName: Full=Aspartate protease 1;
DE   AltName: Full=Secreted aspartic protease 1;
DE   Flags: Precursor;
GN   Name=SAP1; Synonyms=PRA10, PRA3;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX   PubMed=1880680;
RA   Hube B., Turver C.J., Odds F.C., Eiffert H., Boulnois G.J., Koechel H.,
RA   Ruechel R.;
RT   "Sequence of the Candida albicans gene encoding the secretory aspartate
RT   proteinase.";
RL   J. Med. Vet. Mycol. 29:129-132(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SS;
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   [3]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX   PubMed=9043112; DOI=10.1099/00221287-143-2-349;
RA   Smolenski G., Sullivan P.A., Cutfield S.M., Cutfield J.F.;
RT   "Analysis of secreted aspartic proteinases from Candida albicans:
RT   purification and characterization of individual Sap1, Sap2 and Sap3
RT   isoenzymes.";
RL   Microbiology 143:349-356(1997).
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.
CC   -!- MISCELLANEOUS: Expressed exclusively in O (opaque) cells and not in W
CC       (white) cells of strain WO-1.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; X56867; CAA40192.1; -; Genomic_DNA.
DR   EMBL; L12449; AAA34368.2; -; Genomic_DNA.
DR   EMBL; L12450; AAA34369.2; -; Genomic_DNA.
DR   AlphaFoldDB; P0CY26; -.
DR   SMR; P0CY26; -.
DR   ChEMBL; CHEMBL6022; -.
DR   MEROPS; A01.014; -.
DR   VEuPathDB; FungiDB:C6_03490C_A; -.
DR   VEuPathDB; FungiDB:CAWG_05021; -.
DR   PHI-base; PHI:68; -.
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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..50
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025848"
FT   CHAIN           51..391
FT                   /note="Candidapepsin-1"
FT                   /id="PRO_0000025849"
FT   DOMAIN          64..377
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        97..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        305..343
FT                   /evidence="ECO:0000250"
FT   VARIANT         53
FT                   /note="I -> L (in strain: SS; in allele 2.4)"
FT   VARIANT         61
FT                   /note="L -> H (in strain: SS; allele 2.4 and allele 2.8)"
FT   VARIANT         128
FT                   /note="S -> T (in strain: SS; allele 2.4 and allele 2.8)"
SQ   SEQUENCE   391 AA;  41564 MW;  47B8EA960CA99BC3 CRC64;
     MFLKNIFIAL AIALLVDASP AKRSPGFVTL DFDVIKTPVN ATGQEGKVKR QAIPVTLNNE
     LVSYAADITI GSNKQKFNVI VDTGSSDLWV PDASVTCDKP RPGQSADFCK GKGIYTPKSS
     TTSQNLGSPF YIGYGDGSSS QGTLYKDTVG FGGASITKQV FADITKTSIP QGILGIGYKT
     NEAAGDYDNV PVTLKNQGVI AKNAYSLYLN SPNAATGQII FGGVDKAKYS GSLIAVPVTS
     DRELRITLNS LKAVGKNING NIDVLLDSGT TITYLQQDVA QDIIDAFQAE LKSDGQGHTF
     YVTDCQTSGT VDFNFDNNAK ISVPASEFTA PLSYANGQPY PKCQLLLGIS DANILGDNFL
     RSAYLVYDLD DDKISLAQVK YTSASNIAAL T