CARP3_CANAW
ID CARP3_CANAW Reviewed; 398 AA.
AC C4YNQ5; P43092; Q5ANA2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Candidapepsin-3;
DE EC=3.4.23.24;
DE AltName: Full=ACP 3;
DE AltName: Full=Aspartate protease 3;
DE AltName: Full=Secreted aspartic protease 3;
DE Flags: Precursor;
GN Name=SAP3; ORFNames=CAWG_02837;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., 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.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2]
RP PROTEIN SEQUENCE OF 59-73.
RC STRAIN=WO-1;
RX PubMed=8407785; DOI=10.1128/jb.175.19.6126-6133.1993;
RA White T.C., Miyasaki S.H., Agabian N.;
RT "Three distinct secreted aspartyl proteinases in Candida albicans.";
RL J. Bacteriol. 175:6126-6133(1993).
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 -!- MISCELLANEOUS: Expressed exclusively in O (opaque) cells and not in W
CC (white) cells of strain WO-1.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; CM000310; EEQ44564.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YNQ5; -.
DR SMR; C4YNQ5; -.
DR STRING; 5476.C4YNQ5; -.
DR MEROPS; A01.061; -.
DR EnsemblFungi; EEQ44564; EEQ44564; CAWG_02837.
DR VEuPathDB; FungiDB:CAWG_02837; -.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OMA; MHRIDIQ; -.
DR Proteomes; UP000001429; Chromosome 3.
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; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Secreted; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..58
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8407785"
FT /id="PRO_0000413054"
FT CHAIN 59..398
FT /note="Candidapepsin-3"
FT /id="PRO_0000413055"
FT DOMAIN 72..384
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 103..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 90..92
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT BINDING 140..143
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT BINDING 274..278
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..116
FT /evidence="ECO:0000250"
FT DISULFID 312..350
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 42716 MW; BED7CFA1CBC50399 CRC64;
MFLKNIFIAL AIALLADATP TTSNNSPGFV ALNFDVIKTH KNVTGPQGEI NTNVNVKRQT
VPVKLINEQV SYASDITVGS NKQKLTVVID TGSSDLWVPD SQVSCQAGQG QDPNFCKNEG
TYSPSSSSSS QNLNSPFSIE YGDGTTSQGT WYKDTIGFGG ISITKQQFAD VTSTSVDQGI
LGIGYKTHEA EGNYDNVPVT LKNQGIISKN AYSLYLNSRQ ATSGQIIFGG VDNAKYSGAL
IALPVTSDNE LRIHLNTVKV AGQSINADVD VLLDSGTTIT YLQQGVADQV ISAFNGQETY
DANGNLFYLV DCNLSGSVDF AFDKNAKISV PASEFTAPLY TEDGQVYDQC QLLFGTSDYN
ILGDNFLRSA YIVYDLDDNE ISLAQVKYTT ASNIAALT
