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Protein

Candidapepsin-2

Gene

SAP2

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 squash aspartic peptidase inhibitor (SQAPI).1 Publication

pH dependencei

Optimum pH is 4.0.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881
Active sitei274 – 2741

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: CGD
  • drug binding Source: CGD

GO - Biological processi

  • adhesion of symbiont to host Source: CGD
  • cellular protein catabolic process Source: CGD
  • induction by symbiont of defense-related host calcium ion flux Source: CGD
  • induction by symbiont of host defense 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-2 (EC:3.4.23.24)
Alternative name(s):
ACP 2
Aspartate protease 2
Secreted aspartic protease 2
Gene namesi
Name:SAP2
Synonyms:PEP11, PRA11, PRA2
ORF Names:CaO19.11193, CaO19.3708
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000196689. SAP2.

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 – 5638Activation peptide1 PublicationPRO_0000413048Add
BLAST
Chaini57 – 398342Candidapepsin-2PRO_0000413049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi103 ↔ 115
Disulfide bondi312 ↔ 350
Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence analysis

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 and true hyphae. Expressed in greater amounts in the mature biofilms compared to early biofilms during inflammatory disorder of the palatal mucosa among denture wearers. Induced by fluconazole.3 Publications

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP0DJ06.
SMRiP0DJ06. Positions 57-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0DJ06.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 384315Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 903Inhibitor binding
Regioni141 – 1422Inhibitor binding
Regioni274 – 2785Inhibitor binding

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiP0DJ06.
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.

P0DJ06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLKNIFIAL AIALLVDATP TTTKRSAGFV ALDFSVVKTP KAFPVTNGQE
60 70 80 90 100
GKTSKRQAVP VTLHNEQVTY AADITVGSNN QKLNVIVDTG SSDLWVPDVN
110 120 130 140 150
VDCQVTYSDQ TADFCKQKGT YDPSGSSASQ DLNTPFKIGY GDGSSSQGTL
160 170 180 190 200
YKDTVGFGGV SIKNQVLADV DSTSIDQGIL GVGYKTNEAG GSYDNVPVTL
210 220 230 240 250
KKQGVIAKNA YSLYLNSPDA ATGQIIFGGV DNAKYSGSLI ALPVTSDREL
260 270 280 290 300
RISLGSVEVS GKTINTDNVD VLVDSGTTIT YLQQDLADQI IKAFNGKLTQ
310 320 330 340 350
DSNGNSFYEV DCNLSGDVVF NFSKNAKISV PASEFAASLQ GDDGQPYDKC
360 370 380 390
QLLFDVNDAN ILGDNFLRSA YIVYDLDDNE ISLAQVKYTS ASSISALT
Length:398
Mass (Da):42,316
Last modified:October 19, 2011 - v1
Checksum:i53F2AF1ADDBFADAA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91A → G in allele SAP2-1. 1 Publication
Natural varianti273 – 2731V → L in allele SAP2-1. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF481100 Genomic DNA. Translation: AAM21050.1.
AF481101 Genomic DNA. Translation: AAM21051.1.
AACQ01000217 Genomic DNA. Translation: EAK91808.1.
AACQ01000216 Genomic DNA. Translation: EAK91822.1.
PIRiA45280.
RefSeqiXP_711047.1. XM_705955.1.
XP_711061.1. XM_705969.1.

Genome annotation databases

EnsemblFungiiEAK91808; EAK91808; CaO19.3708.
EAK91822; EAK91822; CaO19.11193.
GeneIDi3647333.
3647354.
KEGGical:CaO19.11193.
cal:CaO19.3708.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF481100 Genomic DNA. Translation: AAM21050.1.
AF481101 Genomic DNA. Translation: AAM21051.1.
AACQ01000217 Genomic DNA. Translation: EAK91808.1.
AACQ01000216 Genomic DNA. Translation: EAK91822.1.
PIRiA45280.
RefSeqiXP_711047.1. XM_705955.1.
XP_711061.1. XM_705969.1.

3D structure databases

ProteinModelPortaliP0DJ06.
SMRiP0DJ06. Positions 57-398.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAK91808; EAK91808; CaO19.3708.
EAK91822; EAK91822; CaO19.11193.
GeneIDi3647333.
3647354.
KEGGical:CaO19.11193.
cal:CaO19.3708.

Organism-specific databases

CGDiCAL0000196689. SAP2.

Phylogenomic databases

InParanoidiP0DJ06.
KOiK06005.
OrthoDBiEOG092C3KPP.

Enzyme and pathway databases

BRENDAi3.4.23.24. 1096.

Miscellaneous databases

EvolutionaryTraceiP0DJ06.

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 nameiCARP2_CANAL
AccessioniPrimary (citable) accession number: P0DJ06
Secondary accession number(s): P28871
, P43097, Q59MV8, Q8NKF0, Q8NKF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: September 7, 2016
This is version 30 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.