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 04-NOV-2026, entry version 127. 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; Pichiomycetes; OC Debaryomycetaceae; 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 / RC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P10977; 2 sites, No reported glycans. DR EnsemblFungi; C2_07400C_A-T; C2_07400C_A-T-p1; C2_07400C_A. DR VEuPathDB; FungiDB:C2_07400C_A; -. DR VEuPathDB; FungiDB:CAWG_05836; -. DR OMA; AACHFGG; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-ARBA. 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:EnsemblFungi. DR GO; GO:0097718; F:disordered domain specific binding; IEA:EnsemblFungi. DR GO; GO:0070492; F:oligosaccharide binding; IEA:EnsemblFungi. DR GO; GO:0032258; P:cytoplasm to vacuole targeting by the Cvt pathway; IEA:EnsemblFungi. DR GO; GO:0016237; P:microautophagy; IEA:EnsemblFungi. DR GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi. DR GO; GO:0030163; P:protein catabolic process; IEA:EnsemblFungi. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd05488; Proteinase_A_fungi; 1. DR FunFam; 2.40.70.10:FF:000036; Vacuolar aspartic protease; 1. DR FunFam; 2.40.70.10:FF:000002; Vacuolar aspartic proteinase; 1. DR Gene3D; 2.40.70.10; Acid Proteases; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1. DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1. DR Pfam; PF00026; Asp; 1. DR PRINTS; PR00792; PEPSIN. DR SUPFAM; SSF50630; Acid proteases; 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 //