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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)DescriptionActionsGraphical viewLength
Active sitei901
Active sitei2741

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000041305219 – 58Activation peptideBy similarityAdd BLAST40
ChainiPRO_000041305359 – 398Candidapepsin-3Add BLAST340

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi42N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi105 ↔ 116
Disulfide bondi312 ↔ 350
Glycosylationi313N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

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

Proteomic databases

PRIDEiP0CY29.

Expressioni

Inductioni

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

Structurei

Secondary structure

1398
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 67Combined sources7
Beta strandi69 – 78Combined sources10
Turni79 – 82Combined sources4
Beta strandi83 – 90Combined sources8
Beta strandi96 – 105Combined sources10
Helixi115 – 117Combined sources3
Helixi124 – 126Combined sources3
Beta strandi131 – 140Combined sources10
Beta strandi146 – 158Combined sources13
Beta strandi161 – 174Combined sources14
Beta strandi176 – 178Combined sources3
Beta strandi180 – 182Combined sources3
Helixi190 – 192Combined sources3
Helixi197 – 203Combined sources7
Beta strandi206 – 215Combined sources10
Beta strandi222 – 228Combined sources7
Beta strandi230 – 232Combined sources3
Beta strandi235 – 244Combined sources10
Beta strandi248 – 250Combined sources3
Beta strandi252 – 260Combined sources9
Beta strandi263 – 273Combined sources11
Beta strandi278 – 282Combined sources5
Helixi284 – 293Combined sources10
Beta strandi297 – 300Combined sources4
Beta strandi306 – 310Combined sources5
Beta strandi316 – 323Combined sources8
Beta strandi327 – 331Combined sources5
Helixi332 – 335Combined sources4
Beta strandi336 – 340Combined sources5
Beta strandi346 – 356Combined sources11
Helixi364 – 367Combined sources4
Beta strandi370 – 375Combined sources6
Turni376 – 379Combined sources4
Beta strandi380 – 386Combined sources7
Beta strandi394 – 396Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0CY29.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 384Peptidase A1PROSITE-ProRule annotationAdd BLAST313

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni90 – 92Inhibitor binding3
Regioni140 – 143Inhibitor binding4
Regioni274 – 278Inhibitor binding5

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

CDDicd05474. SAP_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR033876. SAP-like.
[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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H6SX-ray2.20A59-398[»]
2H6TX-ray1.90A59-398[»]
ProteinModelPortaliP0CY29.
SMRiP0CY29.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP0CY29.

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

CDDicd05474. SAP_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR033876. SAP-like.
[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: November 30, 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.