CARP1_CANPA
ID CARP1_CANPA Reviewed; 402 AA.
AC P32951;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Candidapepsin-1;
DE EC=3.4.23.24;
DE AltName: Full=ACP 1;
DE AltName: Full=Aspartate protease 1;
DE Flags: Precursor;
GN Name=SAPP1; Synonyms=ACPR;
OS Candida parapsilosis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5480;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 63-77.
RC STRAIN=Isolate CHUV E18;
RX PubMed=8436951; DOI=10.1099/00221287-139-2-335;
RA de Viragh P.A., Sanglard D., Togni G., Falchetto R., Monod M.;
RT "Cloning and sequencing of two Candida parapsilosis genes encoding acid
RT proteases.";
RL J. Gen. Microbiol. 139:335-342(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:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; Z11919; CAA77977.1; -; Genomic_DNA.
DR PIR; B47701; B47701.
DR PDB; 3FV3; X-ray; 1.85 A; A/B/C/D/E/F/G/H=63-402.
DR PDB; 3TNE; X-ray; 2.40 A; A/B=63-402.
DR PDB; 7AGB; X-ray; 1.70 A; A/B/C/D=63-402.
DR PDB; 7AGC; X-ray; 1.35 A; A/B/D/F=63-402.
DR PDB; 7AGD; X-ray; 1.80 A; A/B/C/D=63-402.
DR PDB; 7AGE; X-ray; 1.30 A; A/B/D/F=63-402.
DR PDBsum; 3FV3; -.
DR PDBsum; 3TNE; -.
DR PDBsum; 7AGB; -.
DR PDBsum; 7AGC; -.
DR PDBsum; 7AGD; -.
DR PDBsum; 7AGE; -.
DR AlphaFoldDB; P32951; -.
DR SMR; P32951; -.
DR MEROPS; A01.038; -.
DR PRIDE; P32951; -.
DR VEuPathDB; FungiDB:CPAR2_102410; -.
DR BRENDA; 3.4.23.24; 1133.
DR EvolutionaryTrace; P32951; -.
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 3D-structure; Aspartyl protease; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Secreted; Signal; Zymogen.
FT SIGNAL 1..25
FT /note="Or 18, or 21"
FT /evidence="ECO:0000255"
FT PROPEP 26..62
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8436951"
FT /id="PRO_0000025869"
FT CHAIN 63..402
FT /note="Candidapepsin-1"
FT /id="PRO_0000025870"
FT DOMAIN 76..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..115
FT /evidence="ECO:0000250"
FT DISULFID 320..354
FT /evidence="ECO:0000250"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:7AGE"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7AGC"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 145..157
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 160..177
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:7AGE"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:7AGE"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 271..281
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:7AGE"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:7AGE"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:7AGE"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 354..363
FT /evidence="ECO:0007829|PDB:7AGE"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:7AGE"
FT TURN 381..384
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:7AGE"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:7AGE"
SQ SEQUENCE 402 AA; 42833 MW; 38B06222F52BC1EA CRC64;
MVAIVTLTRQ VLLTIALALF AQGAAIPEEA AKRDDNPGFV ALDFDVLRKP LNLTEALLRE
KRDSISLSLI NEGPSYASKV SVGSNKQQQT VIIDTGSSDF WVVDSNAQCG KGVDCKSSGT
FTPSSSSSYK NLGAAFTIRY GDGSTSQGTW GKDTVTINGV SITGQQIADV TQTSVDQGIL
GIGYTSNEAV YDTSGRQTTP NYDNVPVTLK KQGKIRTNAY SLYLNSPSAE TGTIIFGGVD
NAKYSGKLVA EQVTSSQPLT ISLASVNLKG SSFSFGDGAL LDSGTTLTYF PSDFAAQLAD
KAGARLVQVA RDQYLYFIDC NTDTSGTTVF NFGNGAKITV PNTEYVYQNG DGTCLWGIQP
SDDTILGDNF LRHAYYLLYN LDANTISIAQ VKYTTDSSIS AV
