CARP_CANTR
ID CARP_CANTR Reviewed; 394 AA.
AC Q00663;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Candidapepsin;
DE EC=3.4.23.24;
DE AltName: Full=ACP;
DE AltName: Full=Aspartate protease;
DE AltName: Full=Secreted aspartic proteinase;
DE Short=SAPT;
DE Flags: Precursor;
GN Name=SAPT1;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 61-88.
RC STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX PubMed=1864366; DOI=10.1016/0014-5793(91)80969-a;
RA Togni G., Sanglard D., Falchetto R., Monod M.;
RT "Isolation and nucleotide sequence of the extracellular acid protease gene
RT (ACP) from the yeast Candida tropicalis.";
RL FEBS Lett. 286:181-185(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 61-394 IN COMPLEX WITH SUBSTRATE
RP PEPTIDE.
RC STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX PubMed=9335526; DOI=10.1021/bi970613x;
RA Symersky J., Monod M., Foundling S.I.;
RT "High-resolution structure of the extracellular aspartic proteinase from
RT Candida tropicalis yeast.";
RL Biochemistry 36:12700-12710(1997).
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.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; X61438; CAA43678.1; -; Genomic_DNA.
DR PIR; S16971; S16971.
DR PDB; 1J71; X-ray; 1.80 A; A=61-394.
DR PDBsum; 1J71; -.
DR AlphaFoldDB; Q00663; -.
DR SMR; Q00663; -.
DR MEROPS; A01.037; -.
DR VEuPathDB; FungiDB:CTMYA2_048760; -.
DR VEuPathDB; FungiDB:CTRG_02432; -.
DR BRENDA; 3.4.23.24; 1146.
DR EvolutionaryTrace; Q00663; -.
DR PHI-base; PHI:17; -.
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..23
FT /evidence="ECO:0000255"
FT PROPEP 24..60
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1864366"
FT /id="PRO_0000025867"
FT CHAIN 61..394
FT /note="Candidapepsin"
FT /id="PRO_0000025868"
FT DOMAIN 74..381
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 92
FT ACT_SITE 278
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..119
FT DISULFID 314..347
FT CONFLICT 191
FT /note="V -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="S -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="C -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="D -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="V -> F (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:1J71"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:1J71"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1J71"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 149..161
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 164..181
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1J71"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1J71"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 267..277
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:1J71"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1J71"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:1J71"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:1J71"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:1J71"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:1J71"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:1J71"
SQ SEQUENCE 394 AA; 42559 MW; 80E071BE1B58CC25 CRC64;
MATIFLFTKN VFIALAFALF AQGLTIPDGI EKRTDKVVSL DFTVIRKPFN ATAHRLIQKR
SDVPTTLINE GPSYAADIVV GSNQQKQTVV IDTGSSDLWV VDTDAECQVT YSGQTNNFCK
QEGTFDPSSS SSAQNLNQDF SIEYGDLTSS QGSFYKDTVG FGGISIKNQQ FADVTTTSVD
QGIMGIGFTA VEAGYNLYSN VPVTLKKQGI INKNAYSCDL NSEDASTGKI IFGGVDNAKY
TGTLTALPVT SSVELRVHLG SINFDGTSVS TNADVVLDSG TTITYFSQST ADKFARIVGA
TWDSRNEIYR LPSCDLSGDA VVNFDQGVKI TVPLSELILK DSDSSICYFG ISRNDANILG
DNFLRRAYIV YDLDDKTISL AQVKYTSSSD ISAL
