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Reviewed, UniProtKB/Swiss-Prot P43092 (CARP3_CANAL)

Last modified November 3, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Candidapepsin-3
    EC=3.4.23.24
Alternative name(s):
    Aspartate protease 3
    ACP 3
    Secreted aspartic protease 3
Gene names
Name: SAP3
ORF Names: CaO19.6001, CaO19.13422
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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.

Subcellular location

Secreted.

Post-translational modification

O-glycosylated By similarity.

Miscellaneous

Expressed exclusively in O (opaque) cells and not in W (white) cells of strain WO-1.

Sequence similarities

Belongs to the peptidase A1 family.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 5840Activation peptide
PRO_0000025852
Chain59 – 398340Candidapepsin-3
PRO_0000025853

Sites

Active site901 By similarity
Active site2741 By similarity

Amino acid modifications

Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Potential
Disulfide bond105 ↔ 116 By similarity
Disulfide bond312 ↔ 350 By similarity

Secondary structure

1 ....................................................... 398
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P43092-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D9A8687FBAD4C448

FASTA39842,806
        10         20         30         40         50         60 
MFLKNIFIAL AIALLADATP TTFNNSPGFV ALNFDVIKTH KNVTGPQGEI NTNVNVKRQT 

        70         80         90        100        110        120 
VPVKLINEQV SYASDITVGS NKQKLTVVID TGSSDLWVPD SQVSCQAGQG QDPNFCKNEG 

       130        140        150        160        170        180 
TYSPSSSSSS QNLNSPFSIE YGDGTTSQGT WYKDTIGFGG ISITKQQFAD VTSTSVDQGI 

       190        200        210        220        230        240 
LGIGYKTHEA EGNYDNVPVT LKNQGIISKN AYSLYLNSRQ ATSGQIIFGG VDNAKYSGTL 

       250        260        270        280        290        300 
IALPVTSDNE LRIHLNTVKV AGQSINADVD VLLDSGTTIT YLQQGVADQV ISAFNGQETY 

       310        320        330        340        350        360 
DANGNLFYLV DCNLSGSVDF AFDKNAKISV PASEFTAPLY TEDGQVYDQC QLLFGTSDYN 

       370        380        390 
ILGDNFLRSA YIVYDLDDNE ISLAQVKYTT ASNIAALT

« Hide

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References

« Hide 'large scale' references
[1]"Three distinct secreted aspartyl proteinases in Candida albicans."
White T.C., Miyasaki S.H., Agabian N.
J. Bacteriol. 175:6126-6133(1993) [PubMed: 8407785] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 59-73.
Strain: SS.
[2]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314.
[3]"Analysis of secreted aspartic proteinases from Candida albicans: purification and characterization of individual Sap1, Sap2 and Sap3 isoenzymes."
Smolenski G., Sullivan P.A., Cutfield S.M., Cutfield J.F.
Microbiology 143:349-356(1997) [PubMed: 9043112] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L22358 Genomic DNA. Translation: AAA34372.1.
AACQ01000004 Genomic DNA. Translation: EAL04349.1.
AACQ01000003 Genomic DNA. Translation: EAL04504.1.
PIRA36926.
RefSeqXP_723063.1.
XP_723210.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2H6SX-ray2.20A59-396[»]
2H6TX-ray1.90A59-396[»]
ModBaseSearch...

Protein family/group databases

MEROPSA01.061.

Genome annotation databases

GeneID3635197.
3635386.
KEGGcal:CaO19.13422.
cal:CaO19.6001.

Organism-specific databases

CGDCAL0005017. SAP3.

Phylogenomic databases

OMAVEMINEV.

Enzyme and pathway databases

BRENDA3.4.23.24. 1124.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

PMAP-CutDBP43092.

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Entry information

Entry nameCARP3_CANAL
AccessionPrimary (citable) accession number: P43092
Secondary accession number(s): Q5ANA2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Candida albicans

Candida albicans: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents