ID C4YQE7_CANAW Unreviewed; 544 AA.
AC C4YQE7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=candidapepsin {ECO:0000256|ARBA:ARBA00013207};
DE EC=3.4.23.24 {ECO:0000256|ARBA:ARBA00013207};
GN ORFNames=CAWG_02704 {ECO:0000313|EMBL:EEQ44436.1};
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ44436.1, ECO:0000313|Proteomes:UP000001429};
RN [1] {ECO:0000313|EMBL:EEQ44436.1, ECO:0000313|Proteomes:UP000001429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1 {ECO:0000313|EMBL:EEQ44436.1,
RC ECO:0000313|Proteomes:UP000001429};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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}.
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; CM000310; EEQ44436.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YQE7; -.
DR MEROPS; A01.067; -.
DR PaxDb; 5476-C4YQE7; -.
DR VEuPathDB; FungiDB:CAWG_02704; -.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OMA; IWGYDDV; -.
DR Proteomes; UP000001429; Chromosome 3.
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; 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:SF109; ASPARTIC PROTEINASE 3-RELATED; 1.
DR PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..544
FT /note="candidapepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002944872"
FT DOMAIN 65..479
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 371
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 406..441
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 544 AA; 58539 MW; 34F9F487F2EC497B CRC64;
MRLNSVALLS LVATALAAKA PFKIDFEVRR GESKDDLSPE DDSNPRFVKR DGSLDMTLTN
KQTFYMATLK IGSNEDENRV LVDTGSSDLW VMSHDLKCVS APNSKRNERS FGHGTGVKLN
ERELLQKRKN LYQPSRTIET DEEKEASEKI HNKLFGFGSI YSTVYITEGP GAYSTFSPFV
GTEGGSGGSG GSNTCTSYGS FNTENSDTFK KNNTNDFEIQ YADDTSAIGI WGYDDVTISN
VTVKDLSFAI ANETSSDVGV LGIGLPGLEV TTQYGYTYQN LPLKLKADGI IAKSLYSLYL
NTADAKAGSI LFGAIDHAKY QGDLVTVKMM RTYSQISYPV RIQVPVSKID VESSSGSTTN
ILSSTTGVVL DTGSTLSYVF SDTLQSLGKA LNGQYSNSVG AYVVNCNLAD SSRTIDIEFG
GNKTIKVPIS DLVLQASKST CILGVMQQSS SSSYMLFGDN ILRSAYIVYD LDDYEVSLAQ
VSYTNKESIE VIGASGITNS SGSGTTSSSG TSTSTSTRHS AGSIISKPVY GLLLSLLISY
YVLV
//
