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P0CY29 (CARP3_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Candidapepsin-3
EC=3.4.23.24
Alternative name(s):
ACP 3
Aspartate protease 3
Secreted aspartic protease 3
Gene names
Name:SAP3
ORF Names:CaO19.13422, CaO19.6001
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida ›

Protein attributes

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 5840Activation peptide By similarity
PRO_0000413052
Chain59 – 398340Candidapepsin-3
PRO_0000413053

Regions

Region90 – 923Inhibitor binding
Region140 – 1434Inhibitor binding
Region274 – 2785Inhibitor binding

Sites

Active site901
Active site2741

Amino acid modifications

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0CY29 [UniParc].

Last modified October 19, 2011. 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

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[2]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[3]"The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A."
Borelli C., Ruge E., Schaller M., Monod M., Korting H.C., Huber R., Maskos K.
Proteins 68:738-748(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 59-396 IN COMPLEX WITH ZINC AND PEPSTATIN A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACQ01000004 Genomic DNA. Translation: EAL04349.1.
AACQ01000003 Genomic DNA. Translation: EAL04504.1.
RefSeqXP_723063.1. XM_717970.1.
XP_723210.1. XM_718117.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H6SX-ray2.20A59-398[»]
2H6TX-ray1.90A59-396[»]
ProteinModelPortalP0CY29.
SMRP0CY29. Positions 59-398.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CGDCAL0005017. SAP3.

Phylogenomic databases

KOK06005.

Enzyme and pathway databases

BRENDA3.4.23.24. 1124.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0CY29.

Entry information

Entry nameCARP3_CANAL
AccessionPrimary (citable) accession number: P0CY29
Secondary accession number(s): P43092, Q5ANA2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 19, 2011
Last modified: May 1, 2013
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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