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Reviewed, UniProtKB/Swiss-Prot P28871 (CARP2_CANAL)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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-2
    EC=3.4.23.24
Alternative name(s):
    Aspartate protease 2
    ACP 2
    Secreted aspartic protease 2
Gene names
Name: SAP2
Synonyms: PRA11, PRA2
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length398 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.

Subunit structure

Monomer. Ref.6

Subcellular location

Secreted. Ref.6 Ref.1

Post-translational modification

O-glycosylated.

Miscellaneous

Expressed both in W (white) and in O (opaque) cells of strain WO-1.

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 – 1818 Potential
Propeptide19 – 5638Activation peptide
PRO_0000025850
Chain57 – 398342Candidapepsin-2
PRO_0000025851

Regions

Region88 – 903Inhibitor binding
Region141 – 1422Inhibitor binding
Region274 – 2785Inhibitor binding

Sites

Active site881
Active site2741

Amino acid modifications

Glycosylation3131N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Disulfide bond103 ↔ 115
Disulfide bond312 ↔ 350

Experimental info

Sequence conflict91A → G in CAA44178. Ref.2
Sequence conflict431F → S in CAA44178. Ref.2
Sequence conflict216 – 23621NSPDA…NAKYS → ILQMSPRDKSFSVGLIMLNI V Ref.2
Sequence conflict370 – 39627AYIVY…SSISA → LILFMIWMIMKFLWLKSNIL LFQYFS in CAA44178. Ref.2

Secondary structure

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

Details...

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Sequences

Sequence LengthMass (Da)Tools
P28871-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 53F2AF0F3DB04DB0

FASTA39842,330
        10         20         30         40         50         60 
MFLKNIFIAL AIALLVDATP TTTKRSAGFV ALDFSVVKTP KAFPVTNGQE GKTSKRQAVP 

        70         80         90        100        110        120 
VTLHNEQVTY AADITVGSNN QKLNVIVDTG SSDLWVPDVN VDCQVTYSDQ TADFCKQKGT 

       130        140        150        160        170        180 
YDPSGSSASQ DLNTPFKIGY GDGSSSQGTL YKDTVGFGGV SIKNQVLADV DSTSIDQGIL 

       190        200        210        220        230        240 
GVGYKTNEAG GSYDNVPVTL KKQGVIAKNA YSLYLNSPDA ATGQIIFGGV DNAKYSGSLI 

       250        260        270        280        290        300 
ALPVTSDREL RISLGSVEVS GKTINTDNVD VLLDSGTTIT YLQQDLADQI IKAFNGKLTQ 

       310        320        330        340        350        360 
DSNGNSFYEV DCNLSGDVVF NFSKNAKISV PASEFAASLQ GDDGQPYDKC QLLFDVNDAN 

       370        380        390 
ILGDNFLRSA YIVYDLDDNE ISLAQVKYTS ASSISALT

« Hide

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References

[1]"A second gene for a secreted aspartate proteinase in Candida albicans."
Wright R.J., Carne A., Hieber A.D., Lamont I.L., Emerson G.W., Sullivan P.A.
J. Bacteriol. 174:7848-7853(1992) [PubMed: 1447155] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], N-TERMINAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
Strain: ATCC 10261 / CBS 2718 / IFO 1061.
[2]"cDNA cloning of an aspartic proteinase secreted by Candida albicans."
Mukai H., Takeda O., Asada K., Kato I., Murayama S.Y., Yamaguchi H.
Microbiol. Immunol. 36:1207-1216(1992) [PubMed: 1491622] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: TIMM 2726 / 114 / Serotype A.
[3]"Three distinct secreted aspartyl proteinases in Candida albicans."
White T.C., Miyasaki S.H., Agabian N.
J. Bacteriol. 175:6126-6133(1993) [PubMed: 8407785] [Abstract]
Cited for: PROTEIN SEQUENCE OF 57-65.
Strain: SS and WO-1.
[4]"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: 9043112] [Abstract]
Cited for: CHARACTERIZATION.
[5]"The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors."
Cutfield S.M., Dodson E.J., Anderson B.F., Moody P.C.E., Marshall C.J., Sullivan P.A., Cutfield J.F.
Structure 3:1261-1271(1995) [PubMed: 8591036] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[6]"Structure of a secreted aspartic protease from C. albicans complexed with a potent inhibitor: implications for the design of antifungal agents."
Abad-Zapatero C., Goldman R., Muchmore S.W., Hutchins C., Stewart K., Navaza J., Payne C.D., Ray T.L.
Protein Sci. 5:640-652(1996) [PubMed: 8845753] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 57-398 IN COMPLEX WITH A70450, N-TERMINAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, SUBUNIT.

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Cross-references

Sequence databases

M83663 Genomic DNA. Translation: AAA34332.1.
X62289 mRNA. Translation: CAA44178.1.
PIRA45280.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EAGX-ray2.10A57-398[»]
1ZAPX-ray2.50A57-398[»]
ModBaseSearch...

Protein family/group databases

MEROPSA01.060.

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. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCARP2_CANAL
AccessionPrimary (citable) accession number: P28871
Secondary accession number(s): P43097
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 74 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

Candida albicans

Candida albicans: entries and gene names

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