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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)DescriptionActionsGraphical viewLength
Active sitei108PROSITE-ProRule annotation1
Active sitei294PROSITE-ProRule annotation1

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 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

Proteomic databases

PRIDEiP43094.

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

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi79 – 85Combined sources7
Beta strandi90 – 96Combined sources7
Turni97 – 100Combined sources4
Beta strandi101 – 108Combined sources8
Beta strandi114 – 123Combined sources10
Beta strandi127 – 129Combined sources3
Helixi134 – 136Combined sources3
Helixi143 – 145Combined sources3
Beta strandi150 – 159Combined sources10
Beta strandi165 – 177Combined sources13
Beta strandi180 – 193Combined sources14
Beta strandi195 – 197Combined sources3
Beta strandi199 – 201Combined sources3
Helixi205 – 207Combined sources3
Beta strandi209 – 212Combined sources4
Helixi217 – 223Combined sources7
Beta strandi226 – 235Combined sources10
Beta strandi242 – 248Combined sources7
Beta strandi250 – 252Combined sources3
Beta strandi255 – 258Combined sources4
Beta strandi261 – 264Combined sources4
Beta strandi268 – 270Combined sources3
Beta strandi272 – 280Combined sources9
Beta strandi283 – 293Combined sources11
Beta strandi298 – 302Combined sources5
Helixi304 – 314Combined sources11
Beta strandi317 – 320Combined sources4
Beta strandi326 – 330Combined sources5
Beta strandi337 – 342Combined sources6
Turni343 – 345Combined sources3
Beta strandi346 – 351Combined sources6
Helixi352 – 355Combined sources4
Beta strandi368 – 376Combined sources9
Helixi384 – 387Combined sources4
Beta strandi390 – 395Combined sources6
Turni396 – 399Combined sources4
Beta strandi400 – 406Combined sources7
Beta strandi414 – 416Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QZXX-ray2.50A/B77-418[»]
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
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP43094.
KOiK06005.
OrthoDBiEOG092C3KPP.

Family and domain databases

CDDicd05474. SAP_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR033876. SAP-like.
[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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QZXX-ray2.50A/B77-418[»]
ProteinModelPortaliP43094.
SMRiP43094.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL6019.

Protein family/group databases

MEROPSiA01.063.

Proteomic databases

PRIDEiP43094.

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.
OrthoDBiEOG092C3KPP.

Enzyme and pathway databases

BRENDAi3.4.23.24. 1096.

Miscellaneous databases

EvolutionaryTraceiP43094.
PMAP-CutDBP43094.
PROiP43094.

Family and domain databases

CDDicd05474. SAP_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR033876. SAP-like.
[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...

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: November 30, 2016
This is version 116 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.