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Candidapepsin-9 (EC 3.4.23.24) (ACP 9) (Aspartate protease 9) (Secreted aspartic protease 9)

 CARP9_CANAL             Reviewed;         544 AA.
Q59SU1; A0A1D8PJX2;
13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 2.
07-JUN-2017, entry version 93.
RecName: Full=Candidapepsin-9;
EC=3.4.23.24;
AltName: Full=ACP 9;
AltName: Full=Aspartate protease 9;
AltName: Full=Secreted aspartic protease 9;
Flags: Precursor;
Name=SAP9; Synonyms=YPS1; OrderedLocusNames=CAALFM_C303870CA;
ORFNames=CaO19.14190, CaO19.6928;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
INDUCTION.
PubMed=9802014; DOI=10.1099/00221287-144-10-2731;
Monod M., Hube B., Hess D., Sanglard D.;
"Differential regulation of SAP8 and SAP9, which encode two new
members of the secreted aspartic proteinase family in Candida
albicans.";
Microbiology 144:2731-2737(1998).
[5]
FUNCTION, AND INDUCTION.
PubMed=15820985; DOI=10.1093/jac/dki088;
Copping V.M.S., Barelle C.J., Hube B., Gow N.A.R., Brown A.J.P.,
Odds F.C.;
"Exposure of Candida albicans to antifungal agents affects expression
of SAP2 and SAP9 secreted proteinase genes.";
J. Antimicrob. Chemother. 55:645-654(2005).
[6]
GLYCOSYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=16269404; DOI=10.1074/jbc.M509297200;
Albrecht A., Felk A., Pichova I., Naglik J.R., Schaller M.,
de Groot P., Maccallum D., Odds F.C., Schafer W., Klis F., Monod M.,
Hube B.;
"Glycosylphosphatidylinositol-anchored proteases of Candida albicans
target proteins necessary for both cellular processes and host-
pathogen interactions.";
J. Biol. Chem. 281:688-694(2006).
[7]
FUNCTION.
PubMed=19805528; DOI=10.1128/IAI.00723-09;
Hornbach A., Heyken A., Schild L., Hube B., Loffler J., Kurzai O.;
"The glycosylphosphatidylinositol-anchored protease Sap9 modulates the
interaction of Candida albicans with human neutrophils.";
Infect. Immun. 77:5216-5224(2009).
[8]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=21622905; DOI=10.1128/EC.05011-11;
Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S.,
de Koster C.G., de Koning L.J., Klis F.M.;
"Effects of fluconazole on the secretome, the wall proteome, and wall
integrity of the clinical fungus Candida albicans.";
Eukaryot. Cell 10:1071-1081(2011).
[9]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=21646240; DOI=10.1093/jb/mvr073;
Aoki W., Kitahara N., Miura N., Morisaka H., Yamamoto Y., Kuroda K.,
Ueda M.;
"Comprehensive characterization of secreted aspartic proteases encoded
by a virulence gene family in Candida albicans.";
J. Biochem. 150:431-438(2011).
[10]
FUNCTION.
PubMed=23927842; DOI=10.1016/j.peptides.2013.07.023;
Bochenska O., Rapala-Kozik M., Wolak N., Bras G., Kozik A., Dubin A.,
Aoki W., Ueda M., Mak P.;
"Secreted aspartic peptidases of Candida albicans liberate
bactericidal hemocidins from human hemoglobin.";
Peptides 48:49-58(2013).
-!- FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten
acidic hydrolases considered as key virulence factors. These
enzymes supply the fungus with nutrient amino acids as well as are
able to degrade the selected host's proteins involved in the
immune defense. Involved in triggering host polymorphonuclear
neutrophils chemotaxis toward germ tubes. Moreover, acts toward
human hemoglobin though limited proteolysis to generate a variety
of antimicrobial hemocidins, enabling to compete with the other
microorganisms of the same physiological niche using the
microbicidal peptides generated from the host protein. Required
for cell surface integrity and cell separation during budding.
{ECO:0000269|PubMed:15820985, ECO:0000269|PubMed:16269404,
ECO:0000269|PubMed:19805528, ECO:0000269|PubMed:23927842}.
-!- CATALYTIC ACTIVITY: Preferential cleavage at the carboxyl of
hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-
Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates
trypsinogen, and degrades keratin. {ECO:0000269|PubMed:21646240}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.5. {ECO:0000269|PubMed:21646240};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor,
GPI-anchor {ECO:0000305}. Secreted, cell wall
{ECO:0000269|PubMed:16269404, ECO:0000269|PubMed:21622905}.
-!- INDUCTION: Induced by fluconazole. Expression is regulated by
growth phase, temperature, and white-opaque switch.
{ECO:0000269|PubMed:15820985, ECO:0000269|PubMed:21622905,
ECO:0000269|PubMed:9802014}.
-!- PTM: O-glycosylated. {ECO:0000250}.
-!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
reticulum and serves to target the protein to the cell surface.
There, the glucosamine-inositol phospholipid moiety is cleaved off
and the GPI-modified mannoprotein is covalently attached via its
lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer
cell wall layer.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP017625; AOW28414.1; -; Genomic_DNA.
RefSeq; XP_712729.2; XM_707636.2.
ProteinModelPortal; Q59SU1; -.
PRIDE; Q59SU1; -.
GeneID; 3645625; -.
KEGG; cal:CAALFM_C303870CA; -.
CGD; CAL0000194661; SAP9.
InParanoid; Q59SU1; -.
OrthoDB; EOG092C3KPP; -.
BRENDA; 3.4.23.24; 1096.
PRO; PR:Q59SU1; -.
Proteomes; UP000000559; Chromosome 3.
GO; GO:0031225; C:anchored component of membrane; IDA:CGD.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:CGD.
GO; GO:0009986; C:cell surface; IDA:CGD.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD.
GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
GO; GO:0052155; P:modulation by symbiont of host cell-mediated immune response; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; IDA:CGD.
CDD; cd05474; SAP_like; 1.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom.
InterPro; IPR033876; SAP-like.
PANTHER; PTHR13683; PTHR13683; 1.
Pfam; PF00026; Asp; 2.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 2.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
Aspartyl protease; Cell membrane; Cell wall;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix; Virulence; Zymogen.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 520 Candidapepsin-9.
/FTId=PRO_0000424304.
PROPEP 521 544 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000424305.
TRANSMEM 524 544 Helical. {ECO:0000255}.
DOMAIN 65 479 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
COMPBIAS 449 453 Poly-Ser.
ACT_SITE 83 83 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 371 371 {ECO:0000255|PROSITE-ProRule:PRU10094}.
LIPID 520 520 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 422 422 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 499 499 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 98 195 {ECO:0000250}.
SEQUENCE 544 AA; 58483 MW; 4EC6144F27F97B47 CRC64;
MRLNSVALLS LVATALAAKA PFKIDFEVRR GESKDDLSPE DDSNPRFVKR DGSLDMTLTN
KQTFYMATLK IGSNEDENRV LVDTGSSDLW VMSHDLKCVS APNSKRNERS FGHGTGVKLN
ERELMQKRKN LYQPSRTIET DEEKEASEKI HNKLFGFGSI YSTVYITEGP GAYSTFSPFV
GTEGGSGGSG GSNTCTSYGS FNTENSDTFK KNNTNDFEIQ YADDTSAIGI WGYDDVTISN
VTVKDLSFAI ANETSSDVGV LGIGLPGLEV TTQYGYTYQN LPLKLKADGI IAKSLYSLYL
NTADAKAGSI LFGAIDHAKY QGDLVTVKMM RTYSQISYPV RIQVPVSKID VESSSGSTTN
ILSSTTGVVL DTGSTLSYVF SDTLQSLGKA LNGQYSNSVG AYVVNCNLAD SSRTVDIEFG
GNKTIKVPIS DLVLQASKST CILGVMQQSS SSSYMLFGDN ILRSAYIVYD LDDYEVSLAQ
VSYTNKESIE VIGASGITNS SGSGTTSSSG TSTSTSTRHS AGSIISKPVY GLLLSLLISC
YVLV


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