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Protein

Candidapepsin-5

Gene

SAP5

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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. During infection, plays an important role in penetration into deeper tissues and interaction with host defense. 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.2 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.1 Publication

Enzyme regulationi

Inhibited by pepstatin A analogs.1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081PROSITE-ProRule annotation
Active sitei294 – 2941PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BRENDAi3.4.23.24. 1096.

Protein family/group databases

MEROPSiA01.063.

Names & Taxonomyi

Protein namesi
Recommended name:
Candidapepsin-5 (EC:3.4.23.24)
Alternative name(s):
ACP 5
Aspartate protease 5
Secreted aspartic protease 5
Gene namesi
Name:SAP5
ORF Names:CaO19.13032, CaO19.5585
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL6019.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 7658Activation peptideSequence analysisPRO_0000025856Add
BLAST
Chaini77 – 418342Candidapepsin-5PRO_0000025857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi123 ↔ 135By similarity
Disulfide bondi332 ↔ 370By similarity

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

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

Miscellaneous databases

PMAP-CutDBP43094.

Expressioni

Inductioni

Expressed during development of germ tubes, pseudohyphae and true hyphae. Induced during host infection.3 Publications

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi79 – 857Combined sources
Beta strandi90 – 967Combined sources
Turni97 – 1004Combined sources
Beta strandi101 – 1088Combined sources
Beta strandi114 – 12310Combined sources
Beta strandi127 – 1293Combined sources
Helixi134 – 1363Combined sources
Helixi143 – 1453Combined sources
Beta strandi150 – 15910Combined sources
Beta strandi165 – 17713Combined sources
Beta strandi180 – 19314Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi199 – 2013Combined sources
Helixi205 – 2073Combined sources
Beta strandi209 – 2124Combined sources
Helixi217 – 2237Combined sources
Beta strandi226 – 23510Combined sources
Beta strandi242 – 2487Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi261 – 2644Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi272 – 2809Combined sources
Beta strandi283 – 29311Combined sources
Beta strandi298 – 3025Combined sources
Helixi304 – 31411Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi326 – 3305Combined sources
Beta strandi337 – 3426Combined sources
Turni343 – 3453Combined sources
Beta strandi346 – 3516Combined sources
Helixi352 – 3554Combined sources
Beta strandi368 – 3769Combined sources
Helixi384 – 3874Combined sources
Beta strandi390 – 3956Combined sources
Turni396 – 3994Combined sources
Beta strandi400 – 4067Combined sources
Beta strandi414 – 4163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZXX-ray2.50A/B77-418[»]
ProteinModelPortaliP43094.
SMRiP43094. Positions 77-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43094.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 404315Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 1103Inhibitor bindingBy similarity
Regioni161 – 1622Inhibitor bindingBy similarity
Regioni294 – 2985Inhibitor bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP43094.
KOiK06005.
OrthoDBiEOG71VT34.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
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.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P43094-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLKNILSVL AFALLIDAAP VKRSPGFVTL DFNVKRSLVD PDDPTVEAKR
60 70 80 90 100
SPLFLEFTPS EFPVDETGRD GDVDKRGPVA VTLHNEAITY TADITVGSDN
110 120 130 140 150
QKLNVIVDTG SSDLWIPDSN VICIPKWRGD KGDFCKSAGS YSPASSRTSQ
160 170 180 190 200
NLNTRFDIKY GDGSYAKGKL YKDTVGIGGV SVRDQLFANV WSTSARKGIL
210 220 230 240 250
GIGFQSGEAT EFDYDNLPIS LRNQGIIGKA AYSLYLNSAE ASTGQIIFGG
260 270 280 290 300
IDKAKYSGSL VDLPITSEKK LTVGLRSVNV RGRNVDANTN VLLDSGTTIS
310 320 330 340 350
YFTRSIVRNI LYAIGAQMKF DSAGNKVYVA DCKTSGTIDF QFGNNLKISV
360 370 380 390 400
PVSEFLFQTY YTSGKPFPKC EVRIRESEDN ILGDNFLRSA YVVYNLDDKK
410
ISMAPVKYTS ESDIVAIN
Length:418
Mass (Da):45,649
Last modified:November 1, 1995 - v1
Checksum:i185B00E6BA4AD1E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30191 Genomic DNA. Translation: CAA82923.1.
AACQ01000034 Genomic DNA. Translation: EAL00252.1.
AACQ01000033 Genomic DNA. Translation: EAL00375.1.
PIRiS49056. S42072.
RefSeqiXP_719147.1. XM_714054.1.
XP_719265.1. XM_714172.1.

Genome annotation databases

EnsemblFungiiEAL00252; EAL00252; CaO19.5585.
EAL00375; EAL00375; CaO19.13032.
GeneIDi3639155.
3639268.
KEGGical:CaO19.13032.
cal:CaO19.5585.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30191 Genomic DNA. Translation: CAA82923.1.
AACQ01000034 Genomic DNA. Translation: EAL00252.1.
AACQ01000033 Genomic DNA. Translation: EAL00375.1.
PIRiS49056. S42072.
RefSeqiXP_719147.1. XM_714054.1.
XP_719265.1. XM_714172.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZXX-ray2.50A/B77-418[»]
ProteinModelPortaliP43094.
SMRiP43094. Positions 77-418.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL6019.

Protein family/group databases

MEROPSiA01.063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAL00252; EAL00252; CaO19.5585.
EAL00375; EAL00375; CaO19.13032.
GeneIDi3639155.
3639268.
KEGGical:CaO19.13032.
cal:CaO19.5585.

Phylogenomic databases

InParanoidiP43094.
KOiK06005.
OrthoDBiEOG71VT34.

Enzyme and pathway databases

BRENDAi3.4.23.24. 1096.

Miscellaneous databases

EvolutionaryTraceiP43094.
PMAP-CutDBP43094.
PROiP43094.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
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.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiplicity of genes encoding secreted aspartic proteinases in Candida species."
    Monod M., Togni G., Hube B., Sanglard D.
    Mol. Microbiol. 13:357-368(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C74.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], INDUCTION.
    Strain: SC5314 / ATCC MYA-2876.
  3. "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.
  4. "Profile of Candida albicans-secreted aspartic proteinase elicited during vaginal infection."
    Taylor B.N., Staib P., Binder A., Biesemeier A., Sehnal M., Rollinghoff M., Morschhauser J., Schroppel K.
    Infect. Immun. 73:1828-1835(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "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.
  6. "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.
  7. "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.
  8. "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.

Entry informationi

Entry nameiCARP5_CANAL
AccessioniPrimary (citable) accession number: P43094
Secondary accession number(s): Q5ABW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 112 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.