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Protein

Candidapepsin-3

Gene

SAP3

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.4 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.1 Publication

pH dependencei

Optimum pH is 3.0.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901
Active sitei274 – 2741

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
  • 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-3 (EC:3.4.23.24)
Alternative name(s):
ACP 3
Aspartate protease 3
Secreted aspartic protease 3
Gene namesi
Name:SAP3
ORF Names:CaO19.13422, CaO19.6001
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000201569. SAP3.

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 – 5840Activation peptideBy similarityPRO_0000413052Add
BLAST
Chaini59 – 398340Candidapepsin-3PRO_0000413053Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi105 ↔ 116
Disulfide bondi312 ↔ 350
Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

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

Expressioni

Inductioni

Expressed during development of germ tubes, pseudohyphae and true hyphae.1 Publication

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 677Combined sources
Beta strandi69 – 7810Combined sources
Turni79 – 824Combined sources
Beta strandi83 – 908Combined sources
Beta strandi96 – 10510Combined sources
Helixi115 – 1173Combined sources
Helixi124 – 1263Combined sources
Beta strandi131 – 14010Combined sources
Beta strandi146 – 15813Combined sources
Beta strandi161 – 17414Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi180 – 1823Combined sources
Helixi190 – 1923Combined sources
Helixi197 – 2037Combined sources
Beta strandi206 – 21510Combined sources
Beta strandi222 – 2287Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi235 – 24410Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi252 – 2609Combined sources
Beta strandi263 – 27311Combined sources
Beta strandi278 – 2825Combined sources
Helixi284 – 29310Combined sources
Beta strandi297 – 3004Combined sources
Beta strandi306 – 3105Combined sources
Beta strandi316 – 3238Combined sources
Beta strandi327 – 3315Combined sources
Helixi332 – 3354Combined sources
Beta strandi336 – 3405Combined sources
Beta strandi346 – 35611Combined sources
Helixi364 – 3674Combined sources
Beta strandi370 – 3756Combined sources
Turni376 – 3794Combined sources
Beta strandi380 – 3867Combined sources
Beta strandi394 – 3963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H6SX-ray2.20A59-398[»]
2H6TX-ray1.90A59-398[»]
ProteinModelPortaliP0CY29.
SMRiP0CY29. Positions 59-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CY29.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 384313Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni90 – 923Inhibitor binding
Regioni140 – 1434Inhibitor 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

InParanoidiP0CY29.
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.

P0CY29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLKNIFIAL AIALLADATP TTFNNSPGFV ALNFDVIKTH KNVTGPQGEI
60 70 80 90 100
NTNVNVKRQT VPVKLINEQV SYASDITVGS NKQKLTVVID TGSSDLWVPD
110 120 130 140 150
SQVSCQAGQG QDPNFCKNEG TYSPSSSSSS QNLNSPFSIE YGDGTTSQGT
160 170 180 190 200
WYKDTIGFGG ISITKQQFAD VTSTSVDQGI LGIGYKTHEA EGNYDNVPVT
210 220 230 240 250
LKNQGIISKN AYSLYLNSRQ ATSGQIIFGG VDNAKYSGTL IALPVTSDNE
260 270 280 290 300
LRIHLNTVKV AGQSINADVD VLLDSGTTIT YLQQGVADQV ISAFNGQETY
310 320 330 340 350
DANGNLFYLV DCNLSGSVDF AFDKNAKISV PASEFTAPLY TEDGQVYDQC
360 370 380 390
QLLFGTSDYN ILGDNFLRSA YIVYDLDDNE ISLAQVKYTT ASNIAALT
Length:398
Mass (Da):42,806
Last modified:October 19, 2011 - v1
Checksum:iD9A8687FBAD4C448
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000004 Genomic DNA. Translation: EAL04349.1.
AACQ01000003 Genomic DNA. Translation: EAL04504.1.
RefSeqiXP_723063.1. XM_717970.1.
XP_723210.1. XM_718117.1.

Genome annotation databases

EnsemblFungiiEAL04349; EAL04349; CaO19.13422.
EAL04504; EAL04504; CaO19.6001.
GeneIDi3635197.
3635386.
KEGGical:CaO19.13422.
cal:CaO19.6001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000004 Genomic DNA. Translation: EAL04349.1.
AACQ01000003 Genomic DNA. Translation: EAL04504.1.
RefSeqiXP_723063.1. XM_717970.1.
XP_723210.1. XM_718117.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H6SX-ray2.20A59-398[»]
2H6TX-ray1.90A59-398[»]
ProteinModelPortaliP0CY29.
SMRiP0CY29. Positions 59-398.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAL04349; EAL04349; CaO19.13422.
EAL04504; EAL04504; CaO19.6001.
GeneIDi3635197.
3635386.
KEGGical:CaO19.13422.
cal:CaO19.6001.

Organism-specific databases

CGDiCAL0000201569. SAP3.

Phylogenomic databases

InParanoidiP0CY29.
KOiK06005.
OrthoDBiEOG092C3KPP.

Enzyme and pathway databases

BRENDAi3.4.23.24. 1096.

Miscellaneous databases

EvolutionaryTraceiP0CY29.

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 nameiCARP3_CANAL
AccessioniPrimary (citable) accession number: P0CY29
Secondary accession number(s): P43092, Q5ANA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: September 7, 2016
This is version 31 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.