ID CAR10_CANAL Reviewed; 453 AA.
AC Q5A651; A0A1D8PM25;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 117.
DE RecName: Full=Secreted aspartic protease 10 {ECO:0000303|PubMed:16269404};
DE Short=ACP 10 {ECO:0000305};
DE Short=Aspartate protease 10 {ECO:0000305};
DE EC=3.4.23.24 {ECO:0000269|PubMed:21646240};
DE AltName: Full=Candidapepsin-10 {ECO:0000305};
DE Flags: Precursor;
GN Name=SAP10 {ECO:0000303|PubMed:16269404}; Synonyms=YPS3;
GN OrderedLocusNames=CAALFM_C404470WA; ORFNames=CaO19.11320, CaO19.3839;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16269404; DOI=10.1074/jbc.m509297200;
RA Albrecht A., Felk A., Pichova I., Naglik J.R., Schaller M., de Groot P.,
RA Maccallum D., Odds F.C., Schafer W., Klis F., Monod M., Hube B.;
RT "Glycosylphosphatidylinositol-anchored proteases of Candida albicans target
RT proteins necessary for both cellular processes and host-pathogen
RT interactions.";
RL J. Biol. Chem. 281:688-694(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21646240; DOI=10.1093/jb/mvr073;
RA Aoki W., Kitahara N., Miura N., Morisaka H., Yamamoto Y., Kuroda K.,
RA Ueda M.;
RT "Comprehensive characterization of secreted aspartic proteases encoded by a
RT virulence gene family in Candida albicans.";
RL J. Biochem. 150:431-438(2011).
CC -!- FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten acidic
CC hydrolases considered as key virulence factors (PubMed:16269404,
CC PubMed:21646240). These enzymes supply the fungus with nutrient amino
CC acids as well as are able to degrade the selected host's proteins
CC involved in the immune defense. Required for cell surface integrity and
CC cell separation during budding (PubMed:16269404, PubMed:21646240).
CC {ECO:0000269|PubMed:16269404, ECO:0000269|PubMed:21646240}.
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; Evidence={ECO:0000269|PubMed:21646240};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:21646240};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16269404}. Cell
CC membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC {ECO:0000269|PubMed:16269404}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; CP017626; AOW29196.1; -; Genomic_DNA.
DR RefSeq; XP_717243.1; XM_712150.2.
DR AlphaFoldDB; Q5A651; -.
DR SMR; Q5A651; -.
DR STRING; 237561.Q5A651; -.
DR MEROPS; A01.085; -.
DR GlyCosmos; Q5A651; 8 sites, No reported glycans.
DR EnsemblFungi; C4_04470W_A-T; C4_04470W_A-T-p1; C4_04470W_A.
DR GeneID; 3641126; -.
DR KEGG; cal:CAALFM_C404470WA; -.
DR CGD; CAL0000201140; SAP10.
DR VEuPathDB; FungiDB:C4_04470W_A; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR InParanoid; Q5A651; -.
DR OMA; QCYLAIM; -.
DR OrthoDB; 1996178at2759; -.
DR PRO; PR:Q5A651; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:CGD.
DR GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0006508; P:proteolysis; IDA:CGD.
DR CDD; cd05474; SAP_like; 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; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; 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; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cell membrane; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Protease; Reference proteome; Repeat; Secreted; Signal; Virulence; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..429
FT /note="Secreted aspartic protease 10"
FT /id="PRO_0000424306"
FT PROPEP 430..453
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424307"
FT DOMAIN 52..372
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 387..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 70..72
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT BINDING 138..139
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT BINDING 266..270
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT LIPID 429
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..112
FT /evidence="ECO:0000250|UniProtKB:P0CY27"
FT DISULFID 301..333
FT /evidence="ECO:0000250|UniProtKB:P0CY27"
SQ SEQUENCE 453 AA; 49333 MW; D26DDFF460BCFC37 CRC64;
MDLVIMNFVF LLYLTSVVKC SIKLDFNKVS TPSKYTKRDA LPMPLINDKI LYTTELEIGS
NKDKVSVSID TGSYDLWVMS NDAVCYKVSE FQTEGAPQLP DIFNDIDQDY SCTFNGTYNS
KSSKTFKNTS EDFSIGYVDG SAAQGVWGYD SVQFGQYGVT GLKIGIANRS SVSDGILGIG
IANGYDNFPV LLQKQGLINK IAYSVYLNSS NSTTGTILFG AIDHAKYKGA LSTVPVDSKS
QLSVNVTNLK TKNGNVASGG HSILLDTGST FSIFPDEWID ALGHSLNATY DEDESVYEIE
CDGYDEHFFG FSIGDSDFSV PIQDLKTEKD GQCYLAIMSN SVIGGGGILF GDDILRQIYL
VYDLQDMTIS VAPVVYTEDE DIEEILNPNE DQNEVPTSTS FTQSASSSGS QPSSTISGEN
MDKNTTSSSS GNCQTRSWIA ILSALFLVYI HII
//
