UniProtKB - P0CY27 (CARP1_CANAL)
Candidapepsin-1
SAP1
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 PublicationsCatalytic 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 EC:3.4.23.24
Activity regulationi
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 82 | 1 | ||
Active sitei | 267 | 1 |
GO - Molecular functioni
- aspartic-type endopeptidase activity Source: UniProtKB
GO - Biological processi
- adhesion of symbiont to host Source: CGD
- fungal-type cell wall organization Source: GO_Central
- 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
- protein catabolic process Source: CGD
- protein metabolic process Source: CGD
- proteolysis Source: UniProtKB
- signal peptide processing Source: CGD
Keywordsi
Molecular function | Aspartyl protease, Hydrolase, Protease |
Biological process | Virulence |
Enzyme and pathway databases
BRENDAi | 3.4.23.24, 1096 |
Protein family/group databases
MEROPSi | A01.014 |
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 Ordered Locus Names:CAALFM_C603490CA ORF Names:CaO19.13137, CaO19.5714 |
Organismi | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
Taxonomic identifieri | 237561 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Candida/Lodderomyces clade › Candida › |
Proteomesi |
|
Organism-specific databases
CGDi | CAL0000189556, SAP1 |
VEuPathDBi | FungiDB:C6_03490C_A |
Subcellular locationi
Extracellular region or secreted
- Secreted 2 Publications
Cell Wall
- fungal-type cell wall Source: GO_Central
Extracellular region or secreted
- extracellular region Source: CGD
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 18 | Sequence analysisAdd BLAST | 18 | |
PropeptideiPRO_0000413044 | 19 – 50 | Activation peptideBy similarityAdd BLAST | 32 | |
ChainiPRO_0000413045 | 51 – 391 | Candidapepsin-1Add BLAST | 341 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 40 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 97 ↔ 109 | |||
Disulfide bondi | 305 ↔ 343 |
Post-translational modificationi
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, ZymogenExpressioni
Inductioni
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P0CY27 |
SMRi | P0CY27 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0CY27 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 64 – 377 | Peptidase A1PROSITE-ProRule annotationAdd BLAST | 314 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 82 – 84 | Inhibitor bindingBy similarity | 3 | |
Regioni | 135 – 136 | Inhibitor bindingBy similarity | 2 | |
Regioni | 267 – 271 | Inhibitor bindingBy similarity | 5 |
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG1339, Eukaryota |
HOGENOMi | CLU_013253_9_1_1 |
InParanoidi | P0CY27 |
OMAi | GIGYKTN |
OrthoDBi | 753343at2759 |
Family and domain databases
CDDi | cd05474, SAP_like, 1 hit |
Gene3Di | 2.40.70.10, 2 hits |
InterProi | View protein in InterPro IPR001461, Aspartic_peptidase_A1 IPR001969, Aspartic_peptidase_AS IPR033121, PEPTIDASE_A1 IPR021109, Peptidase_aspartic_dom_sf IPR033876, SAP-like |
PANTHERi | PTHR47965, PTHR47965, 1 hit |
Pfami | View protein in Pfam PF00026, Asp, 1 hit |
PRINTSi | PR00792, PEPSIN |
SUPFAMi | SSF50630, SSF50630, 1 hit |
PROSITEi | View protein in PROSITE PS00141, ASP_PROTEASE, 2 hits PS51767, PEPTIDASE_A1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP017628 Genomic DNA Translation: AOW30279.1 |
RefSeqi | XP_718053.2, XM_712960.2 |
Genome annotation databases
GeneIDi | 3640256 |
KEGGi | cal:CAALFM_C603490CA |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP017628 Genomic DNA Translation: AOW30279.1 |
RefSeqi | XP_718053.2, XM_712960.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2QZW | X-ray | 2.05 | A/B | 51-391 | [»] | |
AlphaFoldDBi | P0CY27 | |||||
SMRi | P0CY27 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 237561.P0CY27 |
Protein family/group databases
MEROPSi | A01.014 |
Genome annotation databases
GeneIDi | 3640256 |
KEGGi | cal:CAALFM_C603490CA |
Organism-specific databases
CGDi | CAL0000189556, SAP1 |
VEuPathDBi | FungiDB:C6_03490C_A |
Phylogenomic databases
eggNOGi | KOG1339, Eukaryota |
HOGENOMi | CLU_013253_9_1_1 |
InParanoidi | P0CY27 |
OMAi | GIGYKTN |
OrthoDBi | 753343at2759 |
Enzyme and pathway databases
BRENDAi | 3.4.23.24, 1096 |
Miscellaneous databases
EvolutionaryTracei | P0CY27 |
PHI-basei | PHI:6783 PHI:6789 PHI:6811 |
PROi | PR:P0CY27 |
Family and domain databases
CDDi | cd05474, SAP_like, 1 hit |
Gene3Di | 2.40.70.10, 2 hits |
InterProi | View protein in InterPro IPR001461, Aspartic_peptidase_A1 IPR001969, Aspartic_peptidase_AS IPR033121, PEPTIDASE_A1 IPR021109, Peptidase_aspartic_dom_sf IPR033876, SAP-like |
PANTHERi | PTHR47965, PTHR47965, 1 hit |
Pfami | View protein in Pfam PF00026, Asp, 1 hit |
PRINTSi | PR00792, PEPSIN |
SUPFAMi | SSF50630, SSF50630, 1 hit |
PROSITEi | View protein in PROSITE PS00141, ASP_PROTEASE, 2 hits PS51767, PEPTIDASE_A1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CARP1_CANAL | |
Accessioni | P0CY27Primary (citable) accession number: P0CY27 Secondary accession number(s): A0A1D8PQ68, P28872, Q5A8N4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 19, 2011 |
Last sequence update: | October 19, 2011 | |
Last modified: | May 25, 2022 | |
This is version 67 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Candida albicans
Candida albicans: entries and gene names - Peptidase families
Classification of peptidase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families