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Protein

Candidapepsin-2

Gene

SAP2

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881PROSITE-ProRule annotation
Active sitei274 – 2741PROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.24. 1096.

Names & Taxonomyi

Protein namesi
Recommended name:
Candidapepsin-2 (EC:3.4.23.24)
Alternative name(s):
ACP 2
Aspartate protease 2
Secreted aspartic protease 2
Gene namesi
Name:SAP2
Synonyms:PRA11, PRA2
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL6021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 5638Activation peptide3 PublicationsPRO_0000025850Add
BLAST
Chaini57 – 398342Candidapepsin-2PRO_0000025851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi103 ↔ 115By similarity
Disulfide bondi312 ↔ 350By similarity
Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Interactioni

Subunit structurei

Monomer.1 Publication

Chemistry

BindingDBiP0CS83.

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi59 – 657Combined sources
Beta strandi67 – 7610Combined sources
Turni77 – 804Combined sources
Beta strandi81 – 888Combined sources
Beta strandi94 – 10310Combined sources
Helixi114 – 1163Combined sources
Helixi123 – 1253Combined sources
Beta strandi130 – 13910Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi145 – 15713Combined sources
Beta strandi160 – 17718Combined sources
Beta strandi179 – 1813Combined sources
Helixi185 – 1873Combined sources
Helixi196 – 2027Combined sources
Beta strandi205 – 21410Combined sources
Beta strandi221 – 2277Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi251 – 2599Combined sources
Beta strandi262 – 27312Combined sources
Beta strandi278 – 2825Combined sources
Helixi284 – 29310Combined sources
Beta strandi297 – 3004Combined sources
Beta strandi302 – 3054Combined sources
Beta strandi306 – 3105Combined sources
Beta strandi316 – 3238Combined sources
Beta strandi327 – 3315Combined sources
Helixi332 – 3354Combined sources
Beta strandi336 – 3383Combined sources
Turni339 – 3435Combined sources
Beta strandi350 – 3567Combined sources
Helixi364 – 3674Combined sources
Beta strandi370 – 3756Combined sources
Turni376 – 3794Combined sources
Beta strandi380 – 3867Combined sources
Beta strandi394 – 3963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EAGX-ray2.10A57-398[»]
1ZAPX-ray2.50A57-398[»]
3PVKX-ray1.27A57-398[»]
3Q70X-ray1.40A57-398[»]
ProteinModelPortaliP0CS83.
SMRiP0CS83. Positions 57-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 384315Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 903Inhibitor bindingBy similarity
Regioni141 – 1422Inhibitor bindingBy similarity
Regioni274 – 2785Inhibitor bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CS83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLKNIFIAL AIALLVDATP TTTKRSAGFV ALDFSVVKTP KAFPVTNGQE
60 70 80 90 100
GKTSKRQAVP VTLHNEQVTY AADITVGSNN QKLNVIVDTG SSDLWVPDVN
110 120 130 140 150
VDCQVTYSDQ TADFCKQKGT YDPSGSSASQ DLNTPFKIGY GDGSSSQGTL
160 170 180 190 200
YKDTVGFGGV SIKNQVLADV DSTSIDQGIL GVGYKTNEAG GSYDNVPVTL
210 220 230 240 250
KKQGVIAKNA YSLYLNSPDA ATGQIIFGGV DNAKYSGSLI ALPVTSDREL
260 270 280 290 300
RISLGSVEVS GKTINTDNVD VLLDSGTTIT YLQQDLADQI IKAFNGKLTQ
310 320 330 340 350
DSNGNSFYEV DCNLSGDVVF NFSKNAKISV PASEFAASLQ GDDGQPYDKC
360 370 380 390
QLLFDVNDAN ILGDNFLRSA YIVYDLDDNE ISLAQVKYTS ASSISALT
Length:398
Mass (Da):42,330
Last modified:February 22, 2012 - v1
Checksum:i53F2AF0F3DB04DB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431F → S in CAA44178 (PubMed:1491622).Curated
Sequence conflicti214 – 23623YLNSP…NAKYS → ILILQMSPRDKSFSVGLIML NIV in CAA44178 (PubMed:1491622).CuratedAdd
BLAST
Sequence conflicti370 – 39627AYIVY…SSISA → LILFMIWMIMKFLWLKSNIL LFQYFS in CAA44178 (PubMed:1491622).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91A → G in strain: TIMM 2726.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83663 Genomic DNA. Translation: AAA34332.1.
X62289 mRNA. Translation: CAA44178.1.
PIRiA45280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83663 Genomic DNA. Translation: AAA34332.1.
X62289 mRNA. Translation: CAA44178.1.
PIRiA45280.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EAGX-ray2.10A57-398[»]
1ZAPX-ray2.50A57-398[»]
3PVKX-ray1.27A57-398[»]
3Q70X-ray1.40A57-398[»]
ProteinModelPortaliP0CS83.
SMRiP0CS83. Positions 57-398.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP0CS83.
ChEMBLiCHEMBL6021.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.23.24. 1096.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION.
    Strain: ATCC 10261 / CBS 2718 / NBRC 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-71.
    Strain: 3153A and SS.
  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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC 10231 / CBS 6431 / DSM 1386 / NBRC 1594.
  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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 57-398.
    Strain: ATCC 10261 / CBS 2718 / NBRC 1061.
  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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 57-398 IN COMPLEX WITH A70450, PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION, SUBUNIT.
    Strain: Val-1.

Entry informationi

Entry nameiCARP2_CANAX
AccessioniPrimary (citable) accession number: P0CS83
Secondary accession number(s): P28871
, P43097, Q59MV8, Q8NKF0, Q8NKF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 22, 2012
Last modified: April 13, 2016
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.