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Candidapepsin-2 (EC 3.4.23.24) (ACP 2) (Aspartate protease 2) (Secreted aspartic protease 2)

 CARP2_CANAL             Reviewed;         398 AA.
P0DJ06; A0A1D8PTK5; P28871; P43097; Q59MV8; Q8NKF0; Q8NKF1;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 1.
05-JUL-2017, entry version 39.
RecName: Full=Candidapepsin-2;
EC=3.4.23.24;
AltName: Full=ACP 2;
AltName: Full=Aspartate protease 2;
AltName: Full=Secreted aspartic protease 2;
Flags: Precursor;
Name=SAP2; Synonyms=PEP11, PRA11, PRA2;
OrderedLocusNames=CAALFM_CR07800WA; ORFNames=CaO19.11193, CaO19.3708;
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 [GENOMIC DNA], AND VARIANTS GLY-9 AND LEU-273.
STRAIN=SC5314 / CAI4 / ATCC MYA-682;
PubMed=12028383; DOI=10.1046/j.1365-2958.2002.02967.x;
Staib P., Kretschmar M., Nichterlein T., Hof H., Morschhauser J.;
"Host versus in vitro signals and intrastrain allelic differences in
the expression of a Candida albicans virulence gene.";
Mol. Microbiol. 44:1351-1366(2002).
[2]
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).
[3]
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).
[4]
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).
[5]
PROTEIN SEQUENCE OF 57-71.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=1879921;
Ganesan K., Banerjee A., Datta A.;
"Molecular cloning of the secretory acid proteinase gene from Candida
albicans and its use as a species-specific probe.";
Infect. Immun. 59:2972-2977(1991).
[6]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9043112; DOI=10.1099/00221287-143-2-349;
Smolenski G., Sullivan P.A., Cutfield S.M., Cutfield J.F.;
"Analysis of secreted aspartic proteinases from Candida albicans:
purification and characterization of individual Sap1, Sap2 and Sap3
isoenzymes.";
Microbiology 143:349-356(1997).
[7]
SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=9841840; DOI=10.1086/314546;
De Bernardis F., Arancia S., Morelli L., Hube B., Sanglard D.,
Schafer W., Cassone A.;
"Evidence that members of the secretory aspartyl proteinase gene
family, in particular SAP2, are virulence factors for Candida
vaginitis.";
J. Infect. Dis. 179:201-208(1999).
[8]
FUNCTION.
PubMed=11478679;
Schaller M., Januschke E., Schackert C., Woerle B., Korting H.C.;
"Different isoforms of secreted aspartyl proteinases (Sap) are
expressed by Candida albicans during oral and cutaneous candidosis in
vivo.";
J. Med. Microbiol. 50:743-747(2001).
[9]
ENZYME REGULATION.
PubMed=12203839; DOI=10.1002/jmr.568;
Farley P.C., Christeller J.T., Sullivan M.E., Sullivan P.A.,
Laing W.A.;
"Analysis of the interaction between the aspartic peptidase inhibitor
SQAPI and aspartic peptidases using surface plasmon resonance.";
J. Mol. Recognit. 15:135-144(2002).
[10]
FUNCTION.
PubMed=12761103; DOI=10.1128/IAI.71.6.3227-3234.2003;
Schaller M., Bein M., Korting H.C., Baur S., Hamm G., Monod M.,
Beinhauer S., Hube B.;
"The secreted aspartyl proteinases Sap1 and Sap2 cause tissue damage
in an in vitro model of vaginal candidiasis based on reconstituted
human vaginal epithelium.";
Infect. Immun. 71:3227-3234(2003).
[11]
FUNCTION.
PubMed=15845479; DOI=10.1128/IAI.73.5.2758-2765.2005;
Schaller M., Korting H.C., Borelli C., Hamm G., Hube B.;
"Candida albicans-secreted aspartic proteinases modify the epithelial
cytokine response in an in vitro model of vaginal candidiasis.";
Infect. Immun. 73:2758-2765(2005).
[12]
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).
[13]
FUNCTION.
PubMed=19880183; DOI=10.1016/j.molimm.2009.08.019;
Gropp K., Schild L., Schindler S., Hube B., Zipfel P.F., Skerka C.;
"The yeast Candida albicans evades human complement attack by
secretion of aspartic proteases.";
Mol. Immunol. 47:465-475(2009).
[14]
FUNCTION.
PubMed=20713630; DOI=10.1128/IAI.00789-10;
Pietrella D., Rachini A., Pandey N., Schild L., Netea M., Bistoni F.,
Hube B., Vecchiarelli A.;
"The Inflammatory response induced by aspartic proteases of Candida
albicans is independent of proteolytic activity.";
Infect. Immun. 78:4754-4762(2010).
[15]
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).
[16]
FUNCTION, AND INDUCTION.
PubMed=22302440; DOI=10.1007/s11046-012-9522-2;
Ramage G., Coco B., Sherry L., Bagg J., Lappin D.F.;
"In vitro Candida albicans biofilm induced proteinase activity and
SAP8 expression correlates with in vivo denture stomatitis severity.";
Mycopathologia 174:11-19(2012).
[17]
INDUCTION.
PubMed=23484407;
Staniszewska M., Bondaryk M., Siennicka K., Kurek A., Orlowski J.,
Schaller M., Kurzatkowski W.;
"In vitro study of secreted aspartyl proteinases Sap1 to Sap3 and Sap4
to Sap6 expression in Candida albicans pleomorphic forms.";
Pol. J. Microbiol. 61:247-256(2012).
[18]
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. Induces host inflammatory cytokine production in a
proteolytic activity-independent way. Plays a role in tissue
damage during superficial infection. 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.
{ECO:0000269|PubMed:11478679, ECO:0000269|PubMed:12761103,
ECO:0000269|PubMed:15820985, ECO:0000269|PubMed:15845479,
ECO:0000269|PubMed:19880183, ECO:0000269|PubMed:20713630,
ECO:0000269|PubMed:22302440, 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,
ECO:0000269|PubMed:9043112, ECO:0000269|PubMed:9841840}.
-!- ENZYME REGULATION: Inhibited by squash aspartic peptidase
inhibitor (SQAPI). {ECO:0000269|PubMed:12203839}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 4.0. {ECO:0000269|PubMed:21646240,
ECO:0000269|PubMed:9043112};
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9841840}.
-!- INDUCTION: Expressed during development of germ tubes,
pseudohyphae and true hyphae. Expressed in greater amounts in the
mature biofilms compared to early biofilms during inflammatory
disorder of the palatal mucosa among denture wearers. Induced by
fluconazole. {ECO:0000269|PubMed:15820985,
ECO:0000269|PubMed:22302440, ECO:0000269|PubMed:23484407}.
-!- PTM: O-glycosylated.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF481100; AAM21050.1; -; Genomic_DNA.
EMBL; AF481101; AAM21051.1; -; Genomic_DNA.
EMBL; CP017630; AOW31471.1; -; Genomic_DNA.
PIR; A45280; A45280.
RefSeq; XP_711047.1; XM_705955.2.
ProteinModelPortal; P0DJ06; -.
SMR; P0DJ06; -.
DrugBank; DB03241; 1-Amino-1-Carbonyl Pentane.
DrugBank; DB04387; 1-Hydroxy-2-Amino-3-Cyclohexylpropane.
DrugBank; DB04451; 4-Methylpiperazin-1-Yl Carbonyl Group.
DrugBank; DB03659; Butylamine.
DrugBank; DB03090; Ethylaminobenzylmethylcarbonyl Group.
MEROPS; A01.060; -.
PRIDE; P0DJ06; -.
GeneID; 3647354; -.
KEGG; cal:CAALFM_CR07800WA; -.
CGD; CAL0000196689; SAP2.
InParanoid; P0DJ06; -.
KO; K06005; -.
OrthoDB; EOG092C3KPP; -.
BRENDA; 3.4.23.24; 1096.
EvolutionaryTrace; P0DJ06; -.
PRO; PR:P0DJ06; -.
Proteomes; UP000000559; Chromosome R.
GO; GO:0005576; C:extracellular region; IDA:CGD.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD.
GO; GO:0044257; P:cellular protein catabolic process; IMP:CGD.
GO; GO:0052391; P:induction by symbiont of defense-related host calcium ion flux; IDA:CGD.
GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
GO; GO:0006807; P:nitrogen compound metabolic process; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IDA:CGD.
GO; GO:0030163; P:protein catabolic process; IDA:CGD.
GO; GO:0019538; P:protein metabolic process; IDA:CGD.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0006465; P:signal peptide processing; 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; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
Aspartyl protease; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
Signal; Virulence; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 56 Activation peptide.
{ECO:0000269|PubMed:1879921}.
/FTId=PRO_0000413048.
CHAIN 57 398 Candidapepsin-2.
/FTId=PRO_0000413049.
DOMAIN 70 384 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
REGION 88 90 Inhibitor binding.
REGION 141 142 Inhibitor binding.
REGION 274 278 Inhibitor binding.
ACT_SITE 88 88
ACT_SITE 274 274
CARBOHYD 313 313 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 103 115
DISULFID 312 350
VARIANT 9 9 A -> G (in allele SAP2-1).
{ECO:0000269|PubMed:12028383}.
VARIANT 273 273 V -> L (in allele SAP2-1).
{ECO:0000269|PubMed:12028383}.
SEQUENCE 398 AA; 42316 MW; 53F2AF1ADDBFADAA CRC64;
MFLKNIFIAL AIALLVDATP TTTKRSAGFV ALDFSVVKTP KAFPVTNGQE GKTSKRQAVP
VTLHNEQVTY AADITVGSNN QKLNVIVDTG SSDLWVPDVN VDCQVTYSDQ TADFCKQKGT
YDPSGSSASQ DLNTPFKIGY GDGSSSQGTL YKDTVGFGGV SIKNQVLADV DSTSIDQGIL
GVGYKTNEAG GSYDNVPVTL KKQGVIAKNA YSLYLNSPDA ATGQIIFGGV DNAKYSGSLI
ALPVTSDREL RISLGSVEVS GKTINTDNVD VLVDSGTTIT YLQQDLADQI IKAFNGKLTQ
DSNGNSFYEV DCNLSGDVVF NFSKNAKISV PASEFAASLQ GDDGQPYDKC QLLFDVNDAN
ILGDNFLRSA YIVYDLDDNE ISLAQVKYTS ASSISALT


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