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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)DescriptionActionsGraphical viewLength
Active sitei88PROSITE-ProRule annotation1
Active sitei274PROSITE-ProRule annotation1

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 databases

ChEMBLiCHEMBL6021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002585019 – 56Activation peptide3 PublicationsAdd BLAST38
ChainiPRO_000002585157 – 398Candidapepsin-2Add BLAST342

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi103 ↔ 115By similarity
Disulfide bondi312 ↔ 350By similarity
Glycosylationi313N-linked (GlcNAc...)Sequence analysis1
Glycosylationi321N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

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

Interactioni

Subunit structurei

Monomer.1 Publication

Chemistry databases

BindingDBiP0CS83.

Structurei

Secondary structure

1398
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi59 – 65Combined sources7
Beta strandi67 – 76Combined sources10
Turni77 – 80Combined sources4
Beta strandi81 – 88Combined sources8
Beta strandi94 – 103Combined sources10
Helixi114 – 116Combined sources3
Helixi123 – 125Combined sources3
Beta strandi130 – 139Combined sources10
Beta strandi141 – 143Combined sources3
Beta strandi145 – 157Combined sources13
Beta strandi160 – 177Combined sources18
Beta strandi179 – 181Combined sources3
Helixi185 – 187Combined sources3
Helixi196 – 202Combined sources7
Beta strandi205 – 214Combined sources10
Beta strandi221 – 227Combined sources7
Beta strandi229 – 231Combined sources3
Beta strandi234 – 237Combined sources4
Beta strandi240 – 243Combined sources4
Beta strandi247 – 249Combined sources3
Beta strandi251 – 259Combined sources9
Beta strandi262 – 273Combined sources12
Beta strandi278 – 282Combined sources5
Helixi284 – 293Combined sources10
Beta strandi297 – 300Combined sources4
Beta strandi302 – 305Combined sources4
Beta strandi306 – 310Combined sources5
Beta strandi316 – 323Combined sources8
Beta strandi327 – 331Combined sources5
Helixi332 – 335Combined sources4
Beta strandi336 – 338Combined sources3
Turni339 – 343Combined sources5
Beta strandi350 – 356Combined sources7
Helixi364 – 367Combined sources4
Beta strandi370 – 375Combined sources6
Turni376 – 379Combined sources4
Beta strandi380 – 386Combined sources7
Beta strandi394 – 396Combined sources3

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini70 – 384Peptidase A1PROSITE-ProRule annotationAdd BLAST315

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni88 – 90Inhibitor bindingBy similarity3
Regioni141 – 142Inhibitor bindingBy similarity2
Regioni274 – 278Inhibitor bindingBy similarity5

Sequence similaritiesi

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

Keywords - Domaini

Signal

Family and domain databases

CDDicd05474. SAP_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR033876. SAP-like.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti43F → S in CAA44178 (PubMed:1491622).Curated1
Sequence conflicti214 – 236YLNSP…NAKYS → ILILQMSPRDKSFSVGLIML NIV in CAA44178 (PubMed:1491622).CuratedAdd BLAST23
Sequence conflicti370 – 396AYIVY…SSISA → LILFMIWMIMKFLWLKSNIL LFQYFS in CAA44178 (PubMed:1491622).CuratedAdd BLAST27

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti9A → G in strain: TIMM 2726. 1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EAGX-ray2.10A57-398[»]
1ZAPX-ray2.50A57-398[»]
3PVKX-ray1.27A57-398[»]
3Q70X-ray1.40A57-398[»]
ProteinModelPortaliP0CS83.
SMRiP0CS83.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP0CS83.
ChEMBLiCHEMBL6021.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.23.24. 1096.

Family and domain databases

CDDicd05474. SAP_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR033876. SAP-like.
[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...

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: November 30, 2016
This is version 27 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.