ID B8YPJ7_CANTR Unreviewed; 281 AA.
AC B8YPJ7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=candidapepsin {ECO:0000256|ARBA:ARBA00013207};
DE EC=3.4.23.24 {ECO:0000256|ARBA:ARBA00013207};
DE Flags: Fragment;
GN Name=SAPT4 {ECO:0000313|EMBL:ACL82372.1};
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482 {ECO:0000313|EMBL:ACL82372.1};
RN [1] {ECO:0000313|EMBL:ACL82372.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CTR62 {ECO:0000313|EMBL:ACL82372.1};
RA Parra-Ortega B., Cruz-Torres H., Villa-Tanaca L., Hernandez-Rodriguez C.;
RT "Phylogeny and evolution of the aspartyl proteases family from clinically
RT relevant Candida species.";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|ARBA:ARBA00001675};
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; FJ558624; ACL82372.1; -; Genomic_DNA.
DR AlphaFoldDB; B8YPJ7; -.
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; Acid Proteases; 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; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:ACL82372.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..281
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACL82372.1"
FT NON_TER 281
FT /evidence="ECO:0000313|EMBL:ACL82372.1"
SQ SEQUENCE 281 AA; 30549 MW; 54AD46CCA911F06E CRC64;
TGSSDLWVVD KNATCVRRFE QQVQDFCKAN GTYDPITSSS AKKLGTVFDI SYGDKTNSSG
NWYKDTIKIG GITITNQQFA NVKSTSVAQG VMGIGFKTNE ASNVTYDNVP ITLKKQGIIS
KSAYSLYLNS SDSTTGEIIF GGVDNAKYTG KLIDLPVTSN RELRIHLNSL TIGVTNISAS
MDVLLDSGTT FSYLQQDVLQ HVVDKFNGQL IHDALGNPLH LVDCDLPGNI DFEFSNSSKI
SVPSSEFAVK LYTINGELYP KCQLSILTSS ANILGHNFLR S
//
