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P0CY27

- CARP1_CANAL

UniProt

P0CY27 - CARP1_CANAL

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Protein

Candidapepsin-1

Gene

SAP1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

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.3 Publications

Enzyme regulationi

Inhibited by pepstatin A analogs and squash aspartic peptidase inhibitor (SQAPI).2 Publications

pH dependencei

Optimum pH is 5.0.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821
Active sitei267 – 2671

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: CGD

GO - Biological processi

  1. adhesion of symbiont to host Source: CGD
  2. fungal-type cell wall organization Source: CGD
  3. induction by symbiont of defense-related host calcium ion flux Source: CGD
  4. induction by symbiont of host defense response Source: CGD
  5. induction by symbiont of host immune response Source: CGD
  6. nitrogen compound metabolic process Source: CGD
  7. pathogenesis Source: CGD
  8. protein catabolic process Source: CGD
  9. protein metabolic process Source: CGD
  10. proteolysis Source: CGD
  11. signal peptide processing Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BRENDAi3.4.23.24. 1124.

Names & Taxonomyi

Protein namesi
Recommended name:
Candidapepsin-1 (EC:3.4.23.24)
Alternative name(s):
ACP 1
Aspartate protease 1
Secreted aspartic protease 1
Gene namesi
Name:SAP1
Synonyms:PEP1, PEP10, PRA10, PRA3
ORF Names:CaO19.13137, CaO19.5714
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559: Unassembled WGS sequence

Subcellular locationi

Secreted 2 Publications

GO - Cellular componenti

  1. anchored component of plasma membrane Source: CGD
  2. cell surface Source: CGD
  3. extracellular region Source: CGD
  4. fungal-type cell wall Source: CGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 5032Activation peptideBy similarityPRO_0000413044Add
BLAST
Chaini51 – 391341Candidapepsin-1PRO_0000413045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi97 ↔ 109
Disulfide bondi305 ↔ 343

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Expressioni

Inductioni

Expressed during development of germ tubes, pseudohyphae, true hyphae and opaque cells. Expressed in greater amounts in the mature biofilms compared to early biofilms during inflammatory disorder of the palatal mucosa among denture wearers. Regulated by growth phase and alpha-pheromones.5 Publications

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 597
Beta strandi64 – 707
Turni71 – 744
Beta strandi75 – 828
Beta strandi88 – 9710
Turni106 – 1094
Helixi117 – 1193
Beta strandi124 – 13310
Beta strandi139 – 15113
Beta strandi154 – 17118
Beta strandi173 – 1753
Helixi179 – 1813
Beta strandi183 – 1864
Helixi190 – 1967
Beta strandi199 – 20810
Beta strandi215 – 2217
Beta strandi223 – 2253
Beta strandi228 – 2314
Beta strandi234 – 2374
Beta strandi241 – 2433
Beta strandi245 – 2539
Beta strandi256 – 26611
Beta strandi271 – 2755
Helixi277 – 28711
Beta strandi290 – 2923
Beta strandi295 – 2973
Beta strandi300 – 3034
Beta strandi310 – 3167
Beta strandi320 – 3245
Helixi325 – 3284
Beta strandi341 – 3455
Beta strandi347 – 3493
Helixi357 – 3604
Beta strandi363 – 3686
Turni369 – 3724
Beta strandi373 – 3797
Beta strandi387 – 3893

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZWX-ray2.05A/B51-391[»]
ProteinModelPortaliP0CY27.
SMRiP0CY27. Positions 51-391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CY27.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 843Inhibitor bindingBy similarity
Regioni135 – 1362Inhibitor bindingBy similarity
Regioni267 – 2715Inhibitor bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP0CY27.
KOiK06005.
OrthoDBiEOG71VT34.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CY27-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLKNIFIAL AIALLVDASP AKRSPGFVTL DFDVIKTPVN ATGQEGKVKR
60 70 80 90 100
QAIPVTLNNE HVSYAADITI GSNKQKFNVI VDTGSSDLWV PDASVTCDKP
110 120 130 140 150
RPGQSADFCK GKGIYTPKSS TTSQNLGTPF YIGYGDGSSS QGTLYKDTVG
160 170 180 190 200
FGGASITKQV FADITKTSIP QGILGIGYKT NEAAGDYDNV PVTLKNQGVI
210 220 230 240 250
AKNAYSLYLN SPNAATGQII FGGVDKAKYS GSLIAVPVTS DRELRITLNS
260 270 280 290 300
LKAVGKNING NIDVLLDSGT TITYLQQDVA QDIIDAFQAE LKSDGQGHTF
310 320 330 340 350
YVTDCQTSGT VDFNFDNNAK ISVPASEFTA PLSYANGQPY PKCQLLLGIS
360 370 380 390
DANILGDNFL RSAYLVYDLD DDKISLAQVK YTSASNIAAL T
Length:391
Mass (Da):41,602
Last modified:October 19, 2011 - v1
Checksum:iCF88C56943BCCCA9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000047 Genomic DNA. Translation: EAK99043.1.
AACQ01000046 Genomic DNA. Translation: EAK99117.1.
RefSeqiXP_717987.1. XM_712894.1.
XP_718053.1. XM_712960.1.

Genome annotation databases

GeneIDi3640256.
3640364.
KEGGical:CaO19.13137.
cal:CaO19.5714.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AACQ01000047 Genomic DNA. Translation: EAK99043.1 .
AACQ01000046 Genomic DNA. Translation: EAK99117.1 .
RefSeqi XP_717987.1. XM_712894.1.
XP_718053.1. XM_712960.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QZW X-ray 2.05 A/B 51-391 [» ]
ProteinModelPortali P0CY27.
SMRi P0CY27. Positions 51-391.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3640256.
3640364.
KEGGi cal:CaO19.13137.
cal:CaO19.5714.

Phylogenomic databases

InParanoidi P0CY27.
KOi K06005.
OrthoDBi EOG71VT34.

Enzyme and pathway databases

BRENDAi 3.4.23.24. 1124.

Miscellaneous databases

EvolutionaryTracei P0CY27.

Family and domain databases

Gene3Di 2.40.70.10. 2 hits.
InterProi IPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR021109. Peptidase_aspartic_dom.
[Graphical view ]
PANTHERi PTHR13683. PTHR13683. 1 hit.
Pfami PF00026. Asp. 1 hit.
[Graphical view ]
PRINTSi PR00792. PEPSIN.
SUPFAMi SSF50630. SSF50630. 1 hit.
PROSITEi PS00141. ASP_PROTEASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.
  2. "Transcription of the gene for a pepsinogen, PEP1, is regulated by white-opaque switching in Candida albicans."
    Morrow B., Srikantha T., Soll D.R.
    Mol. Cell. Biol. 12:2997-3005(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  3. "Analysis of secreted aspartic proteinases from Candida albicans: purification and characterization of individual Sap1, Sap2 and Sap3 isoenzymes."
    Smolenski G., Sullivan P.A., Cutfield S.M., Cutfield J.F.
    Microbiology 143:349-356(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  4. "Misexpression of the opaque-phase-specific gene PEP1 (SAP1) in the white phase of Candida albicans confers increased virulence in a mouse model of cutaneous infection."
    Kvaal C., Lachke S.A., Srikantha T., Daniels K., McCoy J., Soll D.R.
    Infect. Immun. 67:6652-6662(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, FUNCTION.
  5. "Evidence that members of the secretory aspartyl proteinase gene family, in particular SAP2, are virulence factors for Candida vaginitis."
    De Bernardis F., Arancia S., Morelli L., Hube B., Sanglard D., Schafer W., Cassone A.
    J. Infect. Dis. 179:201-208(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
  6. "Intra- and intermolecular events direct the propeptide-mediated maturation of the Candida albicans secreted aspartic proteinase Sap1p."
    Beggah S., Lechenne B., Reichard U., Foundling S., Monod M.
    Microbiology 146:2765-2773(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROPEPTIDE.
  7. "Different isoforms of secreted aspartyl proteinases (Sap) are expressed by Candida albicans during oral and cutaneous candidosis in vivo."
    Schaller M., Januschke E., Schackert C., Woerle B., Korting H.C.
    J. Med. Microbiol. 50:743-747(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Analysis of the interaction between the aspartic peptidase inhibitor SQAPI and aspartic peptidases using surface plasmon resonance."
    Farley P.C., Christeller J.T., Sullivan M.E., Sullivan P.A., Laing W.A.
    J. Mol. Recognit. 15:135-144(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "Alpha-pheromone-induced 'shmooing' and gene regulation require white-opaque switching during Candida albicans mating."
    Lockhart S.R., Zhao R., Daniels K.J., Soll D.R.
    Eukaryot. Cell 2:847-855(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "The secreted aspartyl proteinases Sap1 and Sap2 cause tissue damage in an in vitro model of vaginal candidiasis based on reconstituted human vaginal epithelium."
    Schaller M., Bein M., Korting H.C., Baur S., Hamm G., Monod M., Beinhauer S., Hube B.
    Infect. Immun. 71:3227-3234(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Candida albicans-secreted aspartic proteinases modify the epithelial cytokine response in an in vitro model of vaginal candidiasis."
    Schaller M., Korting H.C., Borelli C., Hamm G., Hube B.
    Infect. Immun. 73:2758-2765(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The yeast Candida albicans evades human complement attack by secretion of aspartic proteases."
    Gropp K., Schild L., Schindler S., Hube B., Zipfel P.F., Skerka C.
    Mol. Immunol. 47:465-475(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The Inflammatory response induced by aspartic proteases of Candida albicans is independent of proteolytic activity."
    Pietrella D., Rachini A., Pandey N., Schild L., Netea M., Bistoni F., Hube B., Vecchiarelli A.
    Infect. Immun. 78:4754-4762(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Comprehensive characterization of secreted aspartic proteases encoded by a virulence gene family in Candida albicans."
    Aoki W., Kitahara N., Miura N., Morisaka H., Yamamoto Y., Kuroda K., Ueda M.
    J. Biochem. 150:431-438(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  15. "In vitro Candida albicans biofilm induced proteinase activity and SAP8 expression correlates with in vivo denture stomatitis severity."
    Ramage G., Coco B., Sherry L., Bagg J., Lappin D.F.
    Mycopathologia 174:11-19(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  16. "In vitro study of secreted aspartyl proteinases Sap1 to Sap3 and Sap4 to Sap6 expression in Candida albicans pleomorphic forms."
    Staniszewska M., Bondaryk M., Siennicka K., Kurek A., Orlowski J., Schaller M., Kurzatkowski W.
    Pol. J. Microbiol. 61:247-256(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  17. "Design, synthesis, inhibition studies, and molecular modeling of pepstatin analogues addressing different secreted aspartic proteinases of Candida albicans."
    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.
    Biochem. Pharmacol. 85:881-887(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  18. "Secreted aspartic peptidases of Candida albicans liberate bactericidal hemocidins from human hemoglobin."
    Bochenska O., Rapala-Kozik M., Wolak N., Bras G., Kozik A., Dubin A., Aoki W., Ueda M., Mak P.
    Peptides 48:49-58(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "X-ray structures of Sap1 and Sap5: structural comparison of the secreted aspartic proteinases from Candida albicans."
    Borelli C., Ruge E., Lee J.H., Schaller M., Vogelsang A., Monod M., Korting H.C., Huber R., Maskos K.
    Proteins 72:1308-1319(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 51-391.

Entry informationi

Entry nameiCARP1_CANAL
AccessioniPrimary (citable) accession number: P0CY27
Secondary accession number(s): P28872, Q5A8N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: October 29, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3