ID   CARP7_CANAX             Reviewed;         588 AA.
AC   P43096;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Candidapepsin-7;
DE            EC=3.4.23.24;
DE   AltName: Full=ACP 7;
DE   AltName: Full=Aspartate protease 7;
DE   AltName: Full=Secreted aspartic protease 7;
DE   Flags: Precursor;
GN   Name=SAP7;
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=7984113; DOI=10.1111/j.1365-2958.1994.tb00429.x;
RA   Monod M., Togni G., Hube B., Sanglard D.;
RT   "Multiplicity of genes encoding secreted aspartic proteinases in Candida
RT   species.";
RL   Mol. Microbiol. 13:357-368(1994).
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; Z30193; CAA82925.1; -; Genomic_DNA.
DR   PIR; S49058; S42074.
DR   AlphaFoldDB; P43096; -.
DR   SMR; P43096; -.
DR   MEROPS; A01.065; -.
DR   VEuPathDB; FungiDB:C1_04870W_A; -.
DR   VEuPathDB; FungiDB:CAWG_00909; -.
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; Cleavage on pair of basic residues; Disulfide bond;
KW   Glycoprotein; Hydrolase; Protease; Secreted; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..211
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025860"
FT   CHAIN           212..588
FT                   /note="Candidapepsin-7"
FT                   /id="PRO_0000025861"
FT   DOMAIN          226..574
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          83..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        464
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        486
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        260..269
FT                   /evidence="ECO:0000250"
FT   DISULFID        500..540
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   588 AA;  62553 MW;  01C676FC39C21D61 CRC64;
     MQRVLELLLL SSTALAVIGD GFIALPVHKL QAGEGSAHFP NRLPIFDVVN GVAKSVEDDV
     NQIIQPIFGN GIFSGGSIQG THSGNGHSVK YEVSLPSSSA QKGSNGPSST DNKDTDPSKT
     GFSLDDLMNS ISTDFWNLIG LNKPPTSSDN GSKDADFTPS AVSQVEQPTS KSVESTAPGS
     ASSASSSSSS EAASSSQPSE DSQPSSSANK KTGAFFLSLD NTQTLYTATL KVGSPAQEVQ
     VMIDTGSSDL WFISSGNSQC KVNGGSIDCD KYGVFDKSKS SSWHDNKTDY SISYYDGDKA
     SGTMGQDNIT FADGFSIENA NFAVIDNTTS SIGVFGVGYP ELEAVKSKYT NLPFAMKEQN
     LIAKVAYSLY LDSRDAVQGY ILFGGIDHAF YTGDLKAFDI VQCNDKYVYS QIPLTSVASS
     LNNYTNAYGL PAGSNHPKVG AVIYNGTDSF NGGVDLKDTL TLLDTGTTYS YLSKDQVESI
     VGLYGNVTYN DAGKAYEVPC WVGNPGNYLE FNFKNEQYIK VPTSEFVISV GTYASGAELC
     VFGILPGTHS ILGDNFMRSV YAVFDLEDHV ISIAQAAYND NHAVVPIE