CARP1_CANAW
ID CARP1_CANAW Reviewed; 391 AA.
AC C4YSF6; P28872; Q5A8N4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Candidapepsin-1;
DE EC=3.4.23.24;
DE AltName: Full=ACP 1;
DE AltName: Full=Aspartate protease 1;
DE AltName: Full=Secreted aspartic protease 1;
DE Flags: Precursor;
GN Name=SAP1; Synonyms=PRA10, PRA3; ORFNames=CAWG_05021;
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 [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=7907585; DOI=10.1128/jb.176.6.1702-1710.1994;
RA Miyasaki S.H., White T.C., Agabian N.;
RT "A fourth secreted aspartyl proteinase gene (SAP4) and a CARE2 repetitive
RT element are located upstream of the SAP1 gene in Candida albicans.";
RL J. Bacteriol. 176:1702-1710(1994).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 51-65.
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).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=WO-1;
RX PubMed=7751316; DOI=10.1128/jb.177.10.2953-2955.1995;
RA White T.C., Andrews L.E., Maltby D., Agabian N.;
RT "The 'universal' leucine codon CTG in the secreted aspartyl proteinase 1
RT (SAP1) gene of Candida albicans encodes a serine in vivo.";
RL J. Bacteriol. 177:2953-2955(1995).
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; L12451; AAA34370.2; -; Genomic_DNA.
DR EMBL; L12452; AAA34371.2; -; Genomic_DNA.
DR EMBL; CM000312; EEQ46659.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YSF6; -.
DR SMR; C4YSF6; -.
DR STRING; 5476.C4YSF6; -.
DR MEROPS; A01.014; -.
DR EnsemblFungi; EEQ46659; EEQ46659; CAWG_05021.
DR VEuPathDB; FungiDB:CAWG_05021; -.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OMA; GIGYKTN; -.
DR Proteomes; UP000001429; Chromosome 6.
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..50
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8407785"
FT /id="PRO_0000413046"
FT CHAIN 51..391
FT /note="Candidapepsin-1"
FT /id="PRO_0000413047"
FT DOMAIN 64..377
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..109
FT /evidence="ECO:0000250"
FT DISULFID 305..343
FT /evidence="ECO:0000250"
FT VARIANT 131
FT /note="Y -> N (in allele 2.6)"
FT VARIANT 319
FT /note="V -> A (in allele 2.4)"
SQ SEQUENCE 391 AA; 41630 MW; 2A076AB9FEF60F3D CRC64;
MFLKNIFIAL AIALLVDASP AKRSPGFVTL DFDVIKTPVN ATGQEGKVKR QALPVTLNNE
HVSYAADITI GSNKQKFNVI VDTGSSDLWV PDASVTCDKP RPGQSADFCK GKGIYTPKSS
TTSQNLGTPF YIGYGDGSSS QGTLYKDTVG FGGASITKQV FADITKTSIP QGILGIGYKT
NEAAGDYDNV PVTLKNQGVI AKNAYSLYLN SPNAATGQII FGGVDKAKYS GSLIAVPVTS
DRELRITLNS LKAVGKNING NIDVLLDSGT TITYLQQDVA QDIIDAFQAE LKSDGQGHTF
YVTDCQTSGT VDFNFDNNVK ISVPASEFTA PLSYANGQPY PKCQLLLGIS DANILGDNFL
RSAYLVYDLD DDKISLAQVK YTSASNIAAL T
