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P0CY27 (CARP1_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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Names and origin

Protein namesRecommended name:
Candidapepsin-1
EC=3.4.23.24
Alternative name(s):
ACP 1
Aspartate protease 1
Secreted aspartic protease 1
Gene names
Name:SAP1
Synonyms:PRA10, PRA3
ORF Names:CaO19.13137, CaO19.5714
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 length391 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.

Sequence similarities

Belongs to the peptidase A1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 5032Activation peptide By similarity
PRO_0000413044
Chain51 – 391341Candidapepsin-1
PRO_0000413045

Sites

Active site821
Active site2671

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Disulfide bond97 ↔ 109
Disulfide bond305 ↔ 343

Secondary structure

1 ...................................................................... 391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0CY27 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: CF88C56943BCCCA9

FASTA39141,602
        10         20         30         40         50         60 
MFLKNIFIAL AIALLVDASP AKRSPGFVTL DFDVIKTPVN ATGQEGKVKR QAIPVTLNNE 

        70         80         90        100        110        120 
HVSYAADITI GSNKQKFNVI VDTGSSDLWV PDASVTCDKP RPGQSADFCK GKGIYTPKSS 

       130        140        150        160        170        180 
TTSQNLGTPF YIGYGDGSSS QGTLYKDTVG FGGASITKQV FADITKTSIP QGILGIGYKT 

       190        200        210        220        230        240 
NEAAGDYDNV PVTLKNQGVI AKNAYSLYLN SPNAATGQII FGGVDKAKYS GSLIAVPVTS 

       250        260        270        280        290        300 
DRELRITLNS LKAVGKNING NIDVLLDSGT TITYLQQDVA QDIIDAFQAE LKSDGQGHTF 

       310        320        330        340        350        360 
YVTDCQTSGT VDFNFDNNAK ISVPASEFTA PLSYANGQPY PKCQLLLGIS DANILGDNFL 

       370        380        390 
RSAYLVYDLD DDKISLAQVK YTSASNIAAL T

« 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]"X-ray structures of Sap1 and Sap5: structural comparison of the secreted aspartic proteinases from Candida albicans."
Borelli C., Ruge E., Lee J.H., Schaller M., Vogelsang A., Monod M., Korting H.C., Huber R., Maskos K.
Proteins 72:1308-1319(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 51-391.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACQ01000047 Genomic DNA. Translation: EAK99043.1.
AACQ01000046 Genomic DNA. Translation: EAK99117.1.
RefSeqXP_717987.1. XM_712894.1.
XP_718053.1. XM_712960.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QZWX-ray2.05A/B51-391[»]
ProteinModelPortalP0CY27.
SMRP0CY27. Positions 51-391.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3640256.
3640364.
KEGGcal:CaO19.13137.
cal:CaO19.5714.

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

EvolutionaryTraceP0CY27.

Entry information

Entry nameCARP1_CANAL
AccessionPrimary (citable) accession number: P0CY27
Secondary accession number(s): P28872, Q5A8N4
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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