Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O42778 (CARP8_CANAL)

Last modified June 16, 2009. Version 48. 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-8
    EC=3.4.23.24
Alternative name(s):
    Aspartate protease 8
    ACP 8
    Secreted aspartic protease 8
Gene names
Name: SAP8
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length405 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
   PTMDisulfide bond
Glycoprotein
Zymogen
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – ?Activation peptide PotentialPRO_0000025862
Chain? – 405Candidapepsin-8PRO_0000025863

Regions

Compositional bias59 – 7012Poly-Gln

Sites

Active site1071 By similarity
Active site2921 By similarity

Amino acid modifications

Glycosylation501N-linked (GlcNAc...) Potential
Disulfide bond122 ↔ 134 By similarity
Disulfide bond327 ↔ 358 By similarity

Sequences

Sequence LengthMass (Da)Tools
O42778-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 912FC91979FE39C0

FASTA40543,051
        10         20         30         40         50         60 
MVSIITFTKN VLVTLAFALL AQGLAIPEDI DKRAEKVVSL DFTVTRKPFN ATAHGQHHQS 

        70         80         90        100        110        120 
QQQQQQQQQQ PAQKRGTVQT SLINEGPSYA ATITVGSNKQ QQTVIVDTGS SDLWVVDSAA 

       130        140        150        160        170        180 
VCQVTYPGQS PTFCKQDGTY KPSSSTTSQN LGKAFSIRYE DGSSSQGTVY KDTIGLGGAS 

       190        200        210        220        230        240 
ITNQQFADVT TTSVDQGILG IGFTGDESSP TYDNVPVTLK KQGIINKNAY SLYLNSASAS 

       250        260        270        280        290        300 
SGTIIFGGVD NAKYTGSLTA LPITSSNELR VQLSTINIAG TTVSASTTPV LDSGTTLTYF 

       310        320        330        340        350        360 
SQTIADKLAA AVGAKWNSYY QLYTSSCNLA GNIVFNFAKG VTISVPLSEF VLQDGNSCYF 

       370        380        390        400 
GVSRDSATIL GDNFLRRAYA VYDLDGNTIS LAQVKYTTSS SISTL 

« 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

AF043330 Genomic DNA. Translation: AAC69995.1.

3D structure databases

HSSPHSSP built from PDB template 1J71 based on UniProtKB Q00663.
ModBaseSearch...

Protein family/group databases

MEROPSA01.066.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

PMAP-CutDBO42778.

Entry information

Entry nameCARP8_CANAL
AccessionPrimary (citable) accession number: O42778
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 1, 1998
Last modified: June 16, 2009
This is version 48 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