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Protein

Candidapepsin-1

Gene

SAP1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei821
Active sitei2671

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: CGD

GO - Biological processi

  • adhesion of symbiont to host Source: CGD
  • induction by symbiont of defense-related host calcium ion flux Source: CGD
  • induction by symbiont of host defense response Source: CGD
  • induction by symbiont of host immune response Source: CGD
  • nitrogen compound metabolic process Source: CGD
  • pathogenesis Source: CGD
  • protein catabolic process Source: CGD
  • protein metabolic process Source: CGD
  • proteolysis Source: CGD
  • 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. 1096.

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
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000189556. SAP1.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: CGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000041304419 – 50Activation peptideBy similarityAdd BLAST32
ChainiPRO_000041304551 – 391Candidapepsin-1Add BLAST341

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi97 ↔ 109
Disulfide bondi305 ↔ 343

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

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

Proteomic databases

PRIDEiP0CY27.

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

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 59Combined sources7
Beta strandi64 – 70Combined sources7
Turni71 – 74Combined sources4
Beta strandi75 – 82Combined sources8
Beta strandi88 – 97Combined sources10
Turni106 – 109Combined sources4
Helixi117 – 119Combined sources3
Beta strandi124 – 133Combined sources10
Beta strandi139 – 151Combined sources13
Beta strandi154 – 171Combined sources18
Beta strandi173 – 175Combined sources3
Helixi179 – 181Combined sources3
Beta strandi183 – 186Combined sources4
Helixi190 – 196Combined sources7
Beta strandi199 – 208Combined sources10
Beta strandi215 – 221Combined sources7
Beta strandi223 – 225Combined sources3
Beta strandi228 – 231Combined sources4
Beta strandi234 – 237Combined sources4
Beta strandi241 – 243Combined sources3
Beta strandi245 – 253Combined sources9
Beta strandi256 – 266Combined sources11
Beta strandi271 – 275Combined sources5
Helixi277 – 287Combined sources11
Beta strandi290 – 292Combined sources3
Beta strandi295 – 297Combined sources3
Beta strandi300 – 303Combined sources4
Beta strandi310 – 316Combined sources7
Beta strandi320 – 324Combined sources5
Helixi325 – 328Combined sources4
Beta strandi341 – 345Combined sources5
Beta strandi347 – 349Combined sources3
Helixi357 – 360Combined sources4
Beta strandi363 – 368Combined sources6
Turni369 – 372Combined sources4
Beta strandi373 – 379Combined sources7
Beta strandi387 – 389Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QZWX-ray2.05A/B51-391[»]
ProteinModelPortaliP0CY27.
SMRiP0CY27.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CY27.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 377Peptidase A1PROSITE-ProRule annotationAdd BLAST314

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni82 – 84Inhibitor bindingBy similarity3
Regioni135 – 136Inhibitor bindingBy similarity2
Regioni267 – 271Inhibitor bindingBy similarity5

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP0CY27.
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.

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:
EMBLi
GenBanki
DDBJi
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

EnsemblFungiiEAK99043; EAK99043; CaO19.13137.
EAK99117; EAK99117; CaO19.5714.
GeneIDi3640256.
3640364.
KEGGical:CaO19.13137.
cal:CaO19.5714.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QZWX-ray2.05A/B51-391[»]
ProteinModelPortaliP0CY27.
SMRiP0CY27.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP0CY27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAK99043; EAK99043; CaO19.13137.
EAK99117; EAK99117; CaO19.5714.
GeneIDi3640256.
3640364.
KEGGical:CaO19.13137.
cal:CaO19.5714.

Organism-specific databases

CGDiCAL0000189556. SAP1.

Phylogenomic databases

InParanoidiP0CY27.
KOiK06005.
OrthoDBiEOG092C3KPP.

Enzyme and pathway databases

BRENDAi3.4.23.24. 1096.

Miscellaneous databases

EvolutionaryTraceiP0CY27.

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 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: November 30, 2016
This is version 37 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.