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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821
Active sitei267 – 2671

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)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 – 597Combined sources
Beta strandi64 – 707Combined sources
Turni71 – 744Combined sources
Beta strandi75 – 828Combined sources
Beta strandi88 – 9710Combined sources
Turni106 – 1094Combined sources
Helixi117 – 1193Combined sources
Beta strandi124 – 13310Combined sources
Beta strandi139 – 15113Combined sources
Beta strandi154 – 17118Combined sources
Beta strandi173 – 1753Combined sources
Helixi179 – 1813Combined sources
Beta strandi183 – 1864Combined sources
Helixi190 – 1967Combined sources
Beta strandi199 – 20810Combined sources
Beta strandi215 – 2217Combined sources
Beta strandi223 – 2253Combined sources
Beta strandi228 – 2314Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi241 – 2433Combined sources
Beta strandi245 – 2539Combined sources
Beta strandi256 – 26611Combined sources
Beta strandi271 – 2755Combined sources
Helixi277 – 28711Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi300 – 3034Combined sources
Beta strandi310 – 3167Combined sources
Beta strandi320 – 3245Combined sources
Helixi325 – 3284Combined sources
Beta strandi341 – 3455Combined sources
Beta strandi347 – 3493Combined sources
Helixi357 – 3604Combined sources
Beta strandi363 – 3686Combined sources
Turni369 – 3724Combined sources
Beta strandi373 – 3797Combined sources
Beta strandi387 – 3893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZWX-ray2.05A/B51-391[»]
ProteinModelPortaliP0CY27.
SMRiP0CY27. Positions 51-391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CY27.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 377314Peptidase A1PROSITE-ProRule annotationAdd
BLAST

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
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP0CY27.
KOiK06005.
OrthoDBiEOG092C3KPP.

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZWX-ray2.05A/B51-391[»]
ProteinModelPortaliP0CY27.
SMRiP0CY27. Positions 51-391.
ModBaseiSearch...
MobiDBiSearch...

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

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...

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: September 7, 2016
This is version 34 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.