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Protein

Candidapepsin-5

Gene

SAP5

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: -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

Activity regulationi

Inhibited by pepstatin A analogs.1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei108PROSITE-ProRule annotation1
Active sitei294PROSITE-ProRule annotation1

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: CGD

GO - Biological processi

  • adhesion of symbiont to host Source: CGD
  • cellular nitrogen compound catabolic process Source: CGD
  • nitrogen compound metabolic process Source: CGD
  • pathogenesis Source: CGD
  • protein catabolic process Source: CGD
  • proteolysis Source: CGD
  • single-species biofilm formation Source: CGD

Keywordsi

Molecular functionAspartyl protease, Hydrolase, Protease
Biological processVirulence

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
Ordered Locus Names:CAALFM_C603030WA
ORF Names:CaO19.13032, CaO19.5585
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Chromosome 6

Organism-specific databases

CGDiCAL0000193807 SAP5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL6019

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002585619 – 76Activation peptideSequence analysisAdd BLAST58
ChainiPRO_000002585777 – 418Candidapepsin-5Add BLAST342

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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-CutDBiP43094

Expressioni

Inductioni

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

Structurei

Secondary structure

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP43094
SMRiP43094
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43094

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini90 – 404Peptidase A1PROSITE-ProRule annotationAdd BLAST315

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni108 – 110Inhibitor bindingBy similarity3
Regioni161 – 162Inhibitor bindingBy similarity2
Regioni294 – 298Inhibitor bindingBy similarity5

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP43094
KOiK06005
OMAiIRESEDN
OrthoDBiEOG092C3KPP

Family and domain databases

CDDicd05474 SAP_like, 1 hit
Gene3Di2.40.70.10, 2 hits
InterProiView protein in InterPro
IPR001461 Aspartic_peptidase_A1
IPR001969 Aspartic_peptidase_AS
IPR033121 PEPTIDASE_A1
IPR021109 Peptidase_aspartic_dom_sf
IPR033876 SAP-like
PANTHERiPTHR13683 PTHR13683, 1 hit
PfamiView protein in Pfam
PF00026 Asp, 1 hit
PRINTSiPR00792 PEPSIN
SUPFAMiSSF50630 SSF50630, 1 hit
PROSITEiView protein in PROSITE
PS00141 ASP_PROTEASE, 2 hits
PS51767 PEPTIDASE_A1, 1 hit

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
CP017628 Genomic DNA Translation: AOW30234.1
PIRiS49056 S42072
RefSeqiXP_719147.1, XM_714054.1

Genome annotation databases

EnsemblFungiiAOW30234; AOW30234; CAALFM_C603030WA
GeneIDi3639268
KEGGical:CAALFM_C603030WA

Similar proteinsi

Entry informationi

Entry nameiCARP5_CANAL
AccessioniPrimary (citable) accession number: P43094
Secondary accession number(s): A0A1D8PQ36, Q5ABW5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 12, 2018
This is version 126 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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