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Candidapepsin-3 (EC 3.4.23.24) (ACP 3) (Aspartate protease 3) (Secreted aspartic protease 3)

 CARP3_CANAL             Reviewed;         398 AA.
P0CY29; A0A1D8PKC8; P43092; Q5ANA2;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 1.
05-JUL-2017, entry version 40.
RecName: Full=Candidapepsin-3;
EC=3.4.23.24;
AltName: Full=ACP 3;
AltName: Full=Aspartate protease 3;
AltName: Full=Secreted aspartic protease 3;
Flags: Precursor;
Name=SAP3; OrderedLocusNames=CAALFM_C305230WA;
ORFNames=CaO19.13422, CaO19.6001;
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]
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).
[5]
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).
[6]
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).
[7]
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).
[8]
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).
[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]
ENZYME REGULATION.
PubMed=23262278; DOI=10.1016/j.bcp.2012.12.008;
Cadicamo C.D., Mortier J., Wolber G., Hell M., Heinrich I.E.,
Michel D., Semlin L., Berger U., Korting H.C., Holtje H.D., Koksch B.,
Borelli C.;
"Design, synthesis, inhibition studies, and molecular modeling of
pepstatin analogues addressing different secreted aspartic proteinases
of Candida albicans.";
Biochem. Pharmacol. 85:881-887(2013).
[11]
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).
[12]
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).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 59-396 IN COMPLEX WITH ZINC
AND PEPSTATIN A.
PubMed=17510964; DOI=10.1002/prot.21425;
Borelli C., Ruge E., Schaller M., Monod M., Korting H.C., Huber R.,
Maskos K.;
"The crystal structure of the secreted aspartic proteinase 3 from
Candida albicans and its complex with pepstatin A.";
Proteins 68:738-748(2007).
-!- 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:19880183,
ECO:0000269|PubMed:20713630, 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 pepstatin A analogs.
{ECO:0000269|PubMed:23262278}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 3.0. {ECO:0000269|PubMed:21646240,
ECO:0000269|PubMed:9043112};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- INDUCTION: Expressed during development of germ tubes,
pseudohyphae and true hyphae. {ECO:0000269|PubMed:23484407}.
-!- PTM: O-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP017625; AOW28538.1; -; Genomic_DNA.
RefSeq; XP_723210.1; XM_718117.1.
PDB; 2H6S; X-ray; 2.20 A; A=59-398.
PDB; 2H6T; X-ray; 1.90 A; A=59-398.
PDBsum; 2H6S; -.
PDBsum; 2H6T; -.
ProteinModelPortal; P0CY29; -.
SMR; P0CY29; -.
MEROPS; A01.061; -.
PRIDE; P0CY29; -.
GeneID; 3635197; -.
KEGG; cal:CAALFM_C305230WA; -.
CGD; CAL0000201569; SAP3.
InParanoid; P0CY29; -.
KO; K06005; -.
OrthoDB; EOG092C3KPP; -.
BRENDA; 3.4.23.24; 1096.
EvolutionaryTrace; P0CY29; -.
PRO; PR:P0CY29; -.
Proteomes; UP000000559; Chromosome 3.
GO; GO:0005576; C:extracellular region; IDA:CGD.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD.
GO; GO:0052391; P:induction by symbiont of defense-related host calcium ion flux; IDA:CGD.
GO; GO:0006807; P:nitrogen compound metabolic process; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
GO; GO:0030163; P:protein catabolic process; IMP: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;
3D-structure; Aspartyl protease; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Protease;
Reference proteome; Secreted; Signal; Virulence; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 58 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000413052.
CHAIN 59 398 Candidapepsin-3.
/FTId=PRO_0000413053.
DOMAIN 72 384 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
REGION 90 92 Inhibitor binding.
REGION 140 143 Inhibitor binding.
REGION 274 278 Inhibitor binding.
ACT_SITE 90 90
ACT_SITE 274 274
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 313 313 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 105 116
DISULFID 312 350
STRAND 61 67 {ECO:0000244|PDB:2H6T}.
STRAND 69 78 {ECO:0000244|PDB:2H6T}.
TURN 79 82 {ECO:0000244|PDB:2H6T}.
STRAND 83 90 {ECO:0000244|PDB:2H6T}.
STRAND 96 105 {ECO:0000244|PDB:2H6T}.
HELIX 115 117 {ECO:0000244|PDB:2H6T}.
HELIX 124 126 {ECO:0000244|PDB:2H6T}.
STRAND 131 140 {ECO:0000244|PDB:2H6T}.
STRAND 146 158 {ECO:0000244|PDB:2H6T}.
STRAND 161 174 {ECO:0000244|PDB:2H6T}.
STRAND 176 178 {ECO:0000244|PDB:2H6T}.
STRAND 180 182 {ECO:0000244|PDB:2H6T}.
HELIX 190 192 {ECO:0000244|PDB:2H6T}.
HELIX 197 203 {ECO:0000244|PDB:2H6T}.
STRAND 206 215 {ECO:0000244|PDB:2H6T}.
STRAND 222 228 {ECO:0000244|PDB:2H6T}.
STRAND 230 232 {ECO:0000244|PDB:2H6T}.
STRAND 235 244 {ECO:0000244|PDB:2H6T}.
STRAND 248 250 {ECO:0000244|PDB:2H6T}.
STRAND 252 260 {ECO:0000244|PDB:2H6T}.
STRAND 263 273 {ECO:0000244|PDB:2H6T}.
STRAND 278 282 {ECO:0000244|PDB:2H6T}.
HELIX 284 293 {ECO:0000244|PDB:2H6T}.
STRAND 297 300 {ECO:0000244|PDB:2H6T}.
STRAND 306 310 {ECO:0000244|PDB:2H6T}.
STRAND 316 323 {ECO:0000244|PDB:2H6T}.
STRAND 327 331 {ECO:0000244|PDB:2H6T}.
HELIX 332 335 {ECO:0000244|PDB:2H6T}.
STRAND 336 340 {ECO:0000244|PDB:2H6T}.
STRAND 346 356 {ECO:0000244|PDB:2H6T}.
HELIX 364 367 {ECO:0000244|PDB:2H6T}.
STRAND 370 375 {ECO:0000244|PDB:2H6T}.
TURN 376 379 {ECO:0000244|PDB:2H6T}.
STRAND 380 386 {ECO:0000244|PDB:2H6T}.
STRAND 394 396 {ECO:0000244|PDB:2H6T}.
SEQUENCE 398 AA; 42806 MW; D9A8687FBAD4C448 CRC64;
MFLKNIFIAL AIALLADATP TTFNNSPGFV ALNFDVIKTH KNVTGPQGEI NTNVNVKRQT
VPVKLINEQV SYASDITVGS NKQKLTVVID TGSSDLWVPD SQVSCQAGQG QDPNFCKNEG
TYSPSSSSSS QNLNSPFSIE YGDGTTSQGT WYKDTIGFGG ISITKQQFAD VTSTSVDQGI
LGIGYKTHEA EGNYDNVPVT LKNQGIISKN AYSLYLNSRQ ATSGQIIFGG VDNAKYSGTL
IALPVTSDNE LRIHLNTVKV AGQSINADVD VLLDSGTTIT YLQQGVADQV ISAFNGQETY
DANGNLFYLV DCNLSGSVDF AFDKNAKISV PASEFTAPLY TEDGQVYDQC QLLFGTSDYN
ILGDNFLRSA YIVYDLDDNE ISLAQVKYTT ASNIAALT


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