ID C5MDJ8_CANTT Unreviewed; 389 AA.
AC C5MDJ8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=candidapepsin {ECO:0000256|ARBA:ARBA00013207};
DE EC=3.4.23.24 {ECO:0000256|ARBA:ARBA00013207};
GN ORFNames=CTRG_03750 {ECO:0000313|EMBL:EER32079.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER32079.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER32079.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
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; GG692399; EER32079.1; -; Genomic_DNA.
DR RefSeq; XP_002549453.1; XM_002549407.1.
DR AlphaFoldDB; C5MDJ8; -.
DR EnsemblFungi; CTRG_03750-t43_1; CTRG_03750-t43_1-p1; CTRG_03750.
DR GeneID; 8297882; -.
DR KEGG; ctp:CTRG_03750; -.
DR VEuPathDB; FungiDB:CTRG_03750; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
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:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000002037};
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..389
FT /note="candidapepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002953366"
FT DOMAIN 66..375
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 84
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 271
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 98..105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 308..341
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 389 AA; 42723 MW; DD5AF180A2DCDE33 CRC64;
MQLIFFLVGL VVPFISALVL NAGSNFDDDN DRSGIISLDF QVHQVPSNRK RGFYRTQDLI
NQQIYYTADI FVGSNKQKQS VLVDTGSSDL WIIDSNSCSS ITEQCKESGV YNPRTSKSSV
NLTTPFSISY LDQSSAEGHW FLDKVKIAGA TIKNQQFANA HTITQGIGGD IVCGGTLGLG
FKGNEVADTE YDNVPITLKK QGFIKKSAYS IYLNSVSAQK GSILFGGIDH AKYTGELIAQ
PIAVEDYLAL VLGSVKVNDE IFNVHQPALL DTGSSWTYLP QEIADTIADN LNATWISSED
NEYYSVRCDN VIGNITYTFD AGASITVQFA DLVFRDTDGN CHLGIGRAPY FILGDTFLRS
AYAVFNLDDK TISLAQIKYT NKCKIRAIM
//
