CARPV_CANAX
ID CARPV_CANAX Reviewed; 419 AA.
AC P10977;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Vacuolar aspartic protease;
DE EC=3.4.23.-;
DE AltName: Full=ACP;
DE AltName: Full=Aspartate protease;
DE Flags: Precursor;
GN Name=APR1; Synonyms=PRA, PRA1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061 / FMJ 1011;
RX PubMed=9084153; DOI=10.1111/j.1574-6968.1997.tb10296.x;
RA Niimi M., Niimi K., Cannon R.D.;
RT "Temperature-related expression of the vacuolar aspartic proteinase (APR1)
RT gene and beta-N-acetylglucosaminidase (HEX1) gene during Candida albicans
RT morphogenesis.";
RL FEMS Microbiol. Lett. 148:247-254(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-419.
RC STRAIN=ATCC 2091 / CBS 2730 / DSM 1665 / CIP 1180.79 / NBRC 1393 / 132;
RX PubMed=2646602; DOI=10.1093/nar/17.4.1779;
RA Lott T.J., Boiron P., Page L.S., Benson J., Reiss E.;
RT "Nucleotide sequence of the Candida albicans aspartyl proteinase gene.";
RL Nucleic Acids Res. 17:1779-1779(1989).
CC -!- SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; U36754; AAA79879.1; -; Genomic_DNA.
DR EMBL; X13669; CAA31962.1; -; Genomic_DNA.
DR PIR; S03433; S03433.
DR AlphaFoldDB; P10977; -.
DR SMR; P10977; -.
DR MEROPS; A01.018; -.
DR VEuPathDB; FungiDB:C2_07400C_A; -.
DR VEuPathDB; FungiDB:CAWG_05836; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0032991; C:protein-containing complex; IEA:EnsemblFungi.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:EnsemblFungi.
DR GO; GO:0070492; F:oligosaccharide binding; IEA:EnsemblFungi.
DR GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0016237; P:lysosomal microautophagy; IEA:EnsemblFungi.
DR GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006624; P:vacuolar protein processing; IEA:EnsemblFungi.
DR CDD; cd05488; Proteinase_A_fungi; 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; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; PTHR47966; 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 3: Inferred from homology;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Signal; Vacuole.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..419
FT /note="Vacuolar aspartic protease"
FT /id="PRO_0000025866"
FT DOMAIN 104..415
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT MOTIF 417..419
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 135..140
FT /evidence="ECO:0000250"
FT DISULFID 341..374
FT /evidence="ECO:0000250"
FT CONFLICT 39..40
FT /note="DA -> MH (in Ref. 2; CAA31962)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="K -> E (in Ref. 2; CAA31962)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="Q -> E (in Ref. 2; CAA31962)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="V -> A (in Ref. 2; CAA31962)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..175
FT /note="IS -> HI (in Ref. 2; CAA31962)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="G -> A (in Ref. 2; CAA31962)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="A -> D (in Ref. 2; CAA31962)"
FT /evidence="ECO:0000305"
FT CONFLICT 367..368
FT /note="IL -> Y (in Ref. 2; CAA31962)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="T -> S (in Ref. 2; CAA31962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 45421 MW; C283B2968EAED887 CRC64;
MQLSLSALTT VALALTSSLV DAKAHSIKLS KLSNEETLDA SNFQEYTNSL ANKYLNLFNT
AHGNPSNFGL QHVLTNQEAE VPFVTPKKGG KYDAPLTNYL NAQYFTEIQI GTPGQPFKVI
LDTGSSNLWV PSQDCTSLAC FLHAKYDHDA SSTYKVNGSE FSIQYGSGSM EGYISQDVLT
IGDLVIPGQD FAEATSEPGL AFAFGKFDGI LGLAYDTISV NHIVPPIYNA INQGLLEKPQ
FGFYLGSTDK DENDGGLATF GGYDASLFQG KITWLPIRRK AYWEVSFEGI GLGDEYAELH
KTGAAIDTGT SLITLPSSLA EIINAKIGAT KSWSGQYQVD CAKRDSLPDL TLTFAGYNFT
LTPYDYILEV SGSCISVFTP MDFPQPIGDL AIVGDAFLRK YYSIYDLDKN AVGLAPTKV
