CARP2_CANAW
ID CARP2_CANAW Reviewed; 398 AA.
AC C4YMJ3; P28871; P43097;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Candidapepsin-2;
DE EC=3.4.23.24;
DE AltName: Full=ACP 2;
DE AltName: Full=Aspartate protease 2;
DE AltName: Full=Secreted aspartic protease 2;
DE Flags: Precursor;
GN Name=SAP2; Synonyms=PRA11, PRA2; ORFNames=CAWG_02075;
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 57-71.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Expressed both in W (white) and in O (opaque) cells of
CC strain WO-1.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; CM000309; EEQ43824.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YMJ3; -.
DR SMR; C4YMJ3; -.
DR Allergome; 1436; Cand a CAAP.
DR MEROPS; A01.060; -.
DR EnsemblFungi; EEQ43824; EEQ43824; CAWG_02075.
DR VEuPathDB; FungiDB:CAWG_02075; -.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OMA; LWVPDVN; -.
DR Proteomes; UP000001429; Chromosome R.
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..56
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8407785"
FT /id="PRO_0000413050"
FT CHAIN 57..398
FT /note="Candidapepsin-2"
FT /id="PRO_0000413051"
FT DOMAIN 70..384
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 88..90
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT BINDING 141..142
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 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..115
FT /evidence="ECO:0000250"
FT DISULFID 312..350
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 42315 MW; 76D3516B8B9BA8F4 CRC64;
MFLKNIFIGL AIALLVDATP TTTKRSAGFV ALDFSVVKTP KAFPVTNGQE GKTSKRQAVP
VTLHNEQVTY AADITVGSNN QKLNVIVDTG SSDLWVPDVN VDCQVTYSDQ TADFCKQKGT
YDPSGSSASQ DLNTPFKIGY GDGSSSQGTL YKDTVGFGGV SIKNQVLADV DSTSIDQGIL
GVGYKTNEAG GSYDNVPVTL KKQGVIAKNA YSLYLNSPDA ATGQIIFGGV DNAKYSGSLI
ALPVTSDREL RISLGSVEVS GKTINTDNVD VLLDSGTTIT YLQQDLADQI IKAFNGKLTQ
DSNGNSFYEV DCNLSGDVVF NFSKNAKISV PASEFAASLQ GDDGQPYDKC QLLFDVNDAN
ILGDNFLRSA YIVYDLDNNE ISLAQVKYTS ASSISALT
