UniProtKB - Q5A8N2 (CARP4_CANAL)
Candidapepsin-4
SAP4
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. Activates host systemic immunity. 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.
4 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.1 Publication EC:3.4.23.24
Activity regulationi
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 107 | PROSITE-ProRule annotation | 1 | |
Active sitei | 293 | PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- aspartic-type endopeptidase activity Source: CGD
GO - Biological processi
- activation of immune response Source: CGD
- evasion of host immune response Source: CGD
- fungal-type cell wall organization Source: GO_Central
- proteolysis 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 | A01.062 |
Names & Taxonomyi
Protein namesi | Recommended name: Candidapepsin-4 (EC:3.4.23.24)Alternative name(s): ACP 4 Aspartate protease 4 Secreted aspartic protease 4 |
Gene namesi | Name:SAP4 Ordered Locus Names:CAALFM_C603500CA ORF Names:CaO19.13139, CaO19.5716 |
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 | CAL0000194858, SAP4 |
VEuPathDBi | FungiDB:C6_03500C_A |
Subcellular locationi
Extracellular region or secreted
- Secreted By similarity
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_0000424296 | 19 – 75 | Activation peptideBy similarityAdd BLAST | 57 | |
ChainiPRO_0000424297 | 76 – 417 | Candidapepsin-4Add BLAST | 342 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 122 ↔ 134 | By similarity | ||
Glycosylationi | 137 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 331 ↔ 369 | By similarity |
Post-translational modificationi
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, ZymogenExpressioni
Inductioni
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 89 – 403 | Peptidase A1PROSITE-ProRule annotationAdd BLAST | 315 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 107 – 109 | Inhibitor bindingBy similarity | 3 | |
Regioni | 160 – 161 | Inhibitor bindingBy similarity | 2 | |
Regioni | 293 – 297 | Inhibitor bindingBy similarity | 5 |
Sequence similaritiesi
Keywords - Domaini
Repeat, SignalPhylogenomic databases
eggNOGi | KOG1339, Eukaryota |
HOGENOMi | CLU_013253_9_1_1 |
InParanoidi | Q5A8N2 |
OMAi | NEAYVAD |
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
MFLQNILSVL AFALLIDAAP VKRSTGFVTL DFNVKRSLVD PKDPTVEVKR
60 70 80 90 100
SPLFLDIEPT EIPVDDTGRN DVGKRGPVAV KLDNEIITYS ADITIGSNNQ
110 120 130 140 150
KLSVIVDTGS SDLWVPDSNA VCIPKWPGDR GDFCKNNGSY SPAASSTSKN
160 170 180 190 200
LNTPFEIKYA DGSVAQGNLY QDTVGIGGVS VRDQLFANVR STSAHKGILG
210 220 230 240 250
IGFQSNEATR TPYDNLPITL KKQGIISKNA YSLFLNSPEA SSGQIIFGGI
260 270 280 290 300
DKAKYSGSLV DLPITSDRTL SVGLRSVNVM GQNVNVNAGV LLDSGTTISY
310 320 330 340 350
FTPNIARSII YALGGQVHYD SSGNEAYVAD CKTSGTVDFQ FDRNLKISVP
360 370 380 390 400
ASEFLYQLYY TNGEPYPKCE IRVRESEDNI LGDNFMRSAY IVYDLDDRKI
410
SMAQVKYTSQ SNIVAIN
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP017628 Genomic DNA Translation: AOW30280.1 |
RefSeqi | XP_718054.1, XM_712961.1 |
Genome annotation databases
GeneIDi | 3640257 |
KEGGi | cal:CAALFM_C603500CA |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP017628 Genomic DNA Translation: AOW30280.1 |
RefSeqi | XP_718054.1, XM_712961.1 |
3D structure databases
AlphaFoldDBi | Q5A8N2 |
SMRi | Q5A8N2 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 237561.Q5A8N2 |
Protein family/group databases
MEROPSi | A01.062 |
Genome annotation databases
GeneIDi | 3640257 |
KEGGi | cal:CAALFM_C603500CA |
Organism-specific databases
CGDi | CAL0000194858, SAP4 |
VEuPathDBi | FungiDB:C6_03500C_A |
Phylogenomic databases
eggNOGi | KOG1339, Eukaryota |
HOGENOMi | CLU_013253_9_1_1 |
InParanoidi | Q5A8N2 |
OMAi | NEAYVAD |
OrthoDBi | 753343at2759 |
Enzyme and pathway databases
BRENDAi | 3.4.23.24, 1096 |
Miscellaneous databases
PHI-basei | PHI:6786 PHI:6792 PHI:6807 PHI:6814 |
PROi | PR:Q5A8N2 |
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 | CARP4_CANAL | |
Accessioni | Q5A8N2Primary (citable) accession number: Q5A8N2 Secondary accession number(s): A0A1D8PQ73 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 13, 2013 |
Last sequence update: | April 26, 2005 | |
Last modified: | May 25, 2022 | |
This is version 115 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
Reference proteomeDocuments
- Candida albicans
Candida albicans: entries and gene names - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families