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Reviewed, UniProtKB/Swiss-Prot O42779 (CARP9_CANAL)

Last modified July 22, 2008. Version 46. 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

Names and origin

Protein namesRecommended name:
    Candidapepsin-9
    EC=3.4.23.24
Alternative name(s):
    Aspartate protease 9
    ACP 9
    Secreted aspartic protease 9
Gene names
Name: SAP9
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords

   Cellular componentSecreted
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMGlycoprotein
Zymogen

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – ?Activation peptide Potential
Chain? – 544Candidapepsin-9

Sites

Active site1671 By similarity
Active site3711 By similarity

Amino acid modifications

Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Potential
Glycosylation4991N-linked (GlcNAc...) Potential
Disulfide bond406 ↔ 441 By similarity

Sequences

Sequence LengthMass (Da)Tools
O42779-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: E6D755A46040A486

FASTA54458,625
        10         20         30         40         50         60 
MRLNSVALLS LVATALAAKA PFKIDFEVRR GESKDDLSPE DDSNPRFVKR DGSLDMTLTN 

        70         80         90        100        110        120 
KQTFYMATLK IGSNEDENRV LEDTGSSDLW VMSHDLKCVS APISKRNERS FGHGTGVKLN 

       130        140        150        160        170        180 
ERELMQKRKN LYQPSRTIET DEEKEASEKI HNKLFGFGSI YSTVYITEGP GAYSTFSPLV 

       190        200        210        220        230        240 
GTEGGSGGSG GSNTCRSYGS FNTENSDTFK KNNTNDFEIQ YADDTSAIGI WGYDDVTISN 

       250        260        270        280        290        300 
VTVKDLSFAI ANETSSDVGV LGIGLPGLEV TTQLRYTYQN LPLKLKADGI IAKSLYSLYL 

       310        320        330        340        350        360 
NTADAKAGSI LFGAIDHAKY QGDLVTVKMM RTYSQISYPV RIQVPVLKID VESSSGSTTN 

       370        380        390        400        410        420 
ILSGTTGVVL DTGSTLSYVF SDTLQSLGKA LNGQYSNSVG AYVVNCNLAD SSRTVDIEFG 

       430        440        450        460        470        480 
GNKTIKVPIS DLVLQASKST CILGVMQQSS SSSYMLFGDN ILRSAYIVYD LDDYEVSLAQ 

       490        500        510        520        530        540 
VSYTNKESIE VIGASGITNS SGSGTTSSSG TSTSTSTRHS AGSIISNPVY GLLLSLLISY 


YVLV 

« Hide

References

[1]"Differential regulation of SAP8 and SAP9, which encode two new members of the secreted aspartic proteinase family in Candida albicans."
Monod M., Hube B., Hess D., Sanglard D.
Microbiology 144:2731-2737(1998) [PubMed: 9802014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C74.

Cross-references

Sequence databases

AF043331 Genomic DNA. Translation: AAC69996.1.

3D structure databases

HSSPHSSP built from PDB template 1EAG based on UniProtKB P28871.
ModBaseSearch...

Protein family/group databases

MEROPSA01.067.

Family and domain databases

InterProIPR001969. Pept_Asp_AS.
IPR009007. Pept_Aspartc_cat.
IPR001461. Peptidase_A1.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 1 hit.
[Graphical view]
ProDomO42779.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameCARP9_CANAL
AccessionPrimary (citable) accession number: O42779
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 1, 1998
Last modified: July 22, 2008
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Candida albicans

Candida albicans: entries and gene names

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