ID   CARP3_CANAX             Reviewed;         398 AA.
AC   P0CY28; P43092; Q5ANA2;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Candidapepsin-3;
DE            EC=3.4.23.24;
DE   AltName: Full=ACP 3;
DE   AltName: Full=Aspartate protease 3;
DE   AltName: Full=Secreted aspartic protease 3;
DE   Flags: Precursor;
GN   Name=SAP3;
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=SS;
RX   PubMed=8407785; DOI=10.1128/jb.175.19.6126-6133.1993;
RA   White T.C., Miyasaki S.H., Agabian N.;
RT   "Three distinct secreted aspartyl proteinases in Candida albicans.";
RL   J. Bacteriol. 175:6126-6133(1993).
RN   [2]
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L22358; AAA34372.1; -; Genomic_DNA.
DR   PIR; A36926; A36926.
DR   AlphaFoldDB; P0CY28; -.
DR   SMR; P0CY28; -.
DR   ChEMBL; CHEMBL5644; -.
DR   MEROPS; A01.061; -.
DR   VEuPathDB; FungiDB:C3_05230W_A; -.
DR   VEuPathDB; FungiDB:CAWG_02837; -.
DR   PhylomeDB; P0CY28; -.
DR   PHI-base; PHI:73; -.
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; Disulfide bond;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..58
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025852"
FT   CHAIN           59..398
FT                   /note="Candidapepsin-3"
FT                   /id="PRO_0000025853"
FT   DOMAIN          72..384
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          103..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   BINDING         90..92
FT                   /ligand="pepstatin A"
FT                   /ligand_id="ChEBI:CHEBI:190525"
FT                   /ligand_note="inhibitor"
FT                   /evidence="ECO:0000250|UniProtKB:P0CY29"
FT   BINDING         140..143
FT                   /ligand="pepstatin A"
FT                   /ligand_id="ChEBI:CHEBI:190525"
FT                   /ligand_note="inhibitor"
FT                   /evidence="ECO:0000250|UniProtKB:P0CY29"
FT   BINDING         274..278
FT                   /ligand="pepstatin A"
FT                   /ligand_id="ChEBI:CHEBI:190525"
FT                   /ligand_note="inhibitor"
FT                   /evidence="ECO:0000250|UniProtKB:P0CY29"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..116
FT                   /evidence="ECO:0000250"
FT   DISULFID        312..350
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  42806 MW;  D9A8687FBAD4C448 CRC64;
     MFLKNIFIAL AIALLADATP TTFNNSPGFV ALNFDVIKTH KNVTGPQGEI NTNVNVKRQT
     VPVKLINEQV SYASDITVGS NKQKLTVVID TGSSDLWVPD SQVSCQAGQG QDPNFCKNEG
     TYSPSSSSSS QNLNSPFSIE YGDGTTSQGT WYKDTIGFGG ISITKQQFAD VTSTSVDQGI
     LGIGYKTHEA EGNYDNVPVT LKNQGIISKN AYSLYLNSRQ ATSGQIIFGG VDNAKYSGTL
     IALPVTSDNE LRIHLNTVKV AGQSINADVD VLLDSGTTIT YLQQGVADQV ISAFNGQETY
     DANGNLFYLV DCNLSGSVDF AFDKNAKISV PASEFTAPLY TEDGQVYDQC QLLFGTSDYN
     ILGDNFLRSA YIVYDLDDNE ISLAQVKYTT ASNIAALT