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Reviewed, UniProtKB/Swiss-Prot Q00663 (CARP_CANTR)

Last modified September 22, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
    EC=3.4.23.24
Alternative name(s):
    Aspartate protease
    ACP
    Secreted aspartic proteinase
      Short name=SAPT
Gene names
Name: SAPT1
OrganismCandida tropicalis (Yeast)
Taxonomic identifier5482 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length394 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.

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 – 2323 Potential
Propeptide24 – 6037Activation peptide
PRO_0000025867
Chain61 – 394334Candidapepsin
PRO_0000025868

Sites

Active site921
Active site2781

Amino acid modifications

Glycosylation501N-linked (GlcNAc...) Potential
Disulfide bond107 ↔ 119
Disulfide bond314 ↔ 347

Experimental info

Sequence conflict1911V → D Ref.2
Sequence conflict1991S → D Ref.2
Sequence conflict2181C → L Ref.2
Sequence conflict2191D → Y Ref.2
Sequence conflict3221V → F Ref.2

Secondary structure

1 ................................................................... 394
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q00663-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 80E071BE1B58CC25

FASTA39442,559
        10         20         30         40         50         60 
MATIFLFTKN VFIALAFALF AQGLTIPDGI EKRTDKVVSL DFTVIRKPFN ATAHRLIQKR 

        70         80         90        100        110        120 
SDVPTTLINE GPSYAADIVV GSNQQKQTVV IDTGSSDLWV VDTDAECQVT YSGQTNNFCK 

       130        140        150        160        170        180 
QEGTFDPSSS SSAQNLNQDF SIEYGDLTSS QGSFYKDTVG FGGISIKNQQ FADVTTTSVD 

       190        200        210        220        230        240 
QGIMGIGFTA VEAGYNLYSN VPVTLKKQGI INKNAYSCDL NSEDASTGKI IFGGVDNAKY 

       250        260        270        280        290        300 
TGTLTALPVT SSVELRVHLG SINFDGTSVS TNADVVLDSG TTITYFSQST ADKFARIVGA 

       310        320        330        340        350        360 
TWDSRNEIYR LPSCDLSGDA VVNFDQGVKI TVPLSELILK DSDSSICYFG ISRNDANILG 

       370        380        390 
DNFLRRAYIV YDLDDKTISL AQVKYTSSSD ISAL

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References

[1]"Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalis."
Togni G., Sanglard D., Falchetto R., Monod M.
FEBS Lett. 286:181-185(1991) [PubMed: 1864366] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 61-88.
Strain: ATCC 750 / CBS 94 / DSM 11953 / JCM 1541.
[2]"High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast."
Symersky J., Monod M., Foundling S.I.
Biochemistry 36:12700-12710(1997) [PubMed: 9335526] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 61-394 IN COMPLEX WITH SUBSTRATE PEPTIDE.
Strain: ATCC 750 / CBS 94 / DSM 11953 / JCM 1541.

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Cross-references

Sequence databases

X61438 Genomic DNA. Translation: CAA43678.1.
PIRS16971.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1J71X-ray1.80A61-394[»]
ModBaseSearch...

Protein family/group databases

MEROPSA01.037.

Enzyme and pathway databases

BRENDA3.4.23.24. 1242.

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-CutDBQ00663.

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Entry information

Entry nameCARP_CANTR
AccessionPrimary (citable) accession number: Q00663
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: September 22, 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

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