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P0CY27

- CARP1_CANAL

UniProt

P0CY27 - CARP1_CANAL

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
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    • History
      Entry version 22 (01 Oct 2014)
      Sequence version 1 (19 Oct 2011)
      Previous versions | rss
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    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

    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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    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

    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

    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

    MFLKNIFIAL AIALLVDASP AKRSPGFVTL DFDVIKTPVN ATGQEGKVKR    50
    QAIPVTLNNE HVSYAADITI GSNKQKFNVI VDTGSSDLWV PDASVTCDKP 100
    RPGQSADFCK GKGIYTPKSS TTSQNLGTPF YIGYGDGSSS QGTLYKDTVG 150
    FGGASITKQV FADITKTSIP QGILGIGYKT NEAAGDYDNV PVTLKNQGVI 200
    AKNAYSLYLN SPNAATGQII FGGVDKAKYS GSLIAVPVTS DRELRITLNS 250
    LKAVGKNING NIDVLLDSGT TITYLQQDVA QDIIDAFQAE LKSDGQGHTF 300
    YVTDCQTSGT VDFNFDNNAK ISVPASEFTA PLSYANGQPY PKCQLLLGIS 350
    DANILGDNFL RSAYLVYDLD DDKISLAQVK YTSASNIAAL T 391
    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

    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

    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 1, 2014
    This is version 22 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