ID H8X154_CANO9 Unreviewed; 584 AA.
AC H8X154;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=candidapepsin {ECO:0000256|ARBA:ARBA00013207};
DE EC=3.4.23.24 {ECO:0000256|ARBA:ARBA00013207};
GN ORFNames=CORT_0B03860 {ECO:0000313|EMBL:CCG22094.1};
OS Candida orthopsilosis (strain 90-125) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG22094.1, ECO:0000313|Proteomes:UP000005018};
RN [1] {ECO:0000313|EMBL:CCG22094.1, ECO:0000313|Proteomes:UP000005018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT "Sequence and analysis of the genome of the pathogenic yeast Candida
RT orthopsilosis.";
RL PLoS ONE 7:e35750-e35750(2012).
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; HE681720; CCG22094.1; -; Genomic_DNA.
DR RefSeq; XP_003867531.1; XM_003867483.1.
DR AlphaFoldDB; H8X154; -.
DR MEROPS; A01.067; -.
DR GeneID; 14538551; -.
DR KEGG; cot:CORT_0B03860; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000005018; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 3.
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:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 2.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
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 ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..584
FT /note="candidapepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003616696"
FT DOMAIN 82..515
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 117..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 100
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 408
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 443..477
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 584 AA; 62685 MW; 27376D0F4ECE7098 CRC64;
MKFINNVSLT ASLLSLIPFI SAAATPDNIS SPQGSFKIGF NVRRGSSKEN LSPADDQKPR
FVKRADGDGS FNLELINEQT FYLAELHIGS NKDKNQVLVD TGSSDLWVMS HDLKCVSASS
SSSSGSSSKK KKRDPKNVFG YGTGTGVKFP FEEDQEEPKQ SREDHVEEEQ KRETPSKSEN
VGEDANKRAD SYYTTIYLSE LPDGTNFPAP GGGGIGSGSS SSGGSGSGSN TCTSYGSFNT
GNSDTFKRND TDSFQIQYAD GTYAKGIWGY DTVRMGNISV PDLSFAIANE TSSDIGVLGI
GLPGLETTTS YGYMYENLPI KMKSDGIIKR VLFSLYLDQA DADSGSLLFG AIDHAKYEGS
LETIPMLKTY RQIDYPVRFE VEVSNITLNN NQGVTANVMT DSVGAVLDSG STLSYLYSEQ
IQAVGEALQG RYSSSAGAYI VDCRFLETNS TLDIQFSGKT IKVPVSDLVL QASRSTCYLG
LFEQSSSSSY ILFGDNVLRS AYIVYDLEEY EVHIGQVYYT DDEDIEVVDG SVTTGGGQNS
TRVGGGSGSS SSSSSSNKNG ALSAFNLSWS FVLVGLLVSM GSTL
//
