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Protein

Candidapepsin

Gene

SAPT1

Organism
Candida tropicalis (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 sitei92 – 921
Active sitei278 – 2781

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.24. 1146.

Protein family/group databases

MEROPSiA01.037.

Names & Taxonomyi

Protein namesi
Recommended name:
Candidapepsin (EC:3.4.23.24)
Alternative name(s):
ACP
Aspartate protease
Secreted aspartic proteinase
Short name:
SAPT
Gene namesi
Name:SAPT1
OrganismiCandida tropicalis (Yeast)
Taxonomic identifieri5482 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Propeptidei24 – 6037Activation peptide1 PublicationPRO_0000025867Add
BLAST
Chaini61 – 394334CandidapepsinPRO_0000025868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence analysis
Disulfide bondi107 ↔ 119
Disulfide bondi314 ↔ 347

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

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

Miscellaneous databases

PMAP-CutDBQ00663.

Interactioni

Protein-protein interaction databases

STRINGi294747.XP_002548135.1.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi63 – 697Combined sources
Beta strandi71 – 8010Combined sources
Turni81 – 844Combined sources
Beta strandi85 – 928Combined sources
Beta strandi98 – 10710Combined sources
Helixi118 – 1203Combined sources
Helixi127 – 1293Combined sources
Beta strandi134 – 14411Combined sources
Beta strandi149 – 16113Combined sources
Beta strandi164 – 18118Combined sources
Beta strandi183 – 1853Combined sources
Helixi189 – 1913Combined sources
Helixi201 – 2077Combined sources
Beta strandi212 – 2198Combined sources
Beta strandi226 – 2327Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi239 – 24810Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi256 – 2649Combined sources
Beta strandi267 – 27711Combined sources
Beta strandi282 – 2865Combined sources
Helixi288 – 29811Combined sources
Beta strandi301 – 3033Combined sources
Turni304 – 3074Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi318 – 3258Combined sources
Beta strandi329 – 3335Combined sources
Helixi334 – 3374Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi342 – 3454Combined sources
Beta strandi347 – 3537Combined sources
Helixi361 – 3644Combined sources
Beta strandi367 – 3726Combined sources
Turni373 – 3764Combined sources
Beta strandi377 – 3837Combined sources
Beta strandi391 – 3933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J71X-ray1.80A61-394[»]
ProteinModelPortaliQ00663.
SMRiQ00663. Positions 61-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00663.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 381308Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.

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.

Q00663-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATIFLFTKN VFIALAFALF AQGLTIPDGI EKRTDKVVSL DFTVIRKPFN
60 70 80 90 100
ATAHRLIQKR SDVPTTLINE GPSYAADIVV GSNQQKQTVV IDTGSSDLWV
110 120 130 140 150
VDTDAECQVT YSGQTNNFCK QEGTFDPSSS SSAQNLNQDF SIEYGDLTSS
160 170 180 190 200
QGSFYKDTVG FGGISIKNQQ FADVTTTSVD QGIMGIGFTA VEAGYNLYSN
210 220 230 240 250
VPVTLKKQGI INKNAYSCDL NSEDASTGKI IFGGVDNAKY TGTLTALPVT
260 270 280 290 300
SSVELRVHLG SINFDGTSVS TNADVVLDSG TTITYFSQST ADKFARIVGA
310 320 330 340 350
TWDSRNEIYR LPSCDLSGDA VVNFDQGVKI TVPLSELILK DSDSSICYFG
360 370 380 390
ISRNDANILG DNFLRRAYIV YDLDDKTISL AQVKYTSSSD ISAL
Length:394
Mass (Da):42,559
Last modified:December 1, 1992 - v1
Checksum:i80E071BE1B58CC25
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911V → D (PubMed:9335526).Curated
Sequence conflicti199 – 1991S → D (PubMed:9335526).Curated
Sequence conflicti218 – 2181C → L (PubMed:9335526).Curated
Sequence conflicti219 – 2191D → Y (PubMed:9335526).Curated
Sequence conflicti322 – 3221V → F (PubMed:9335526).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61438 Genomic DNA. Translation: CAA43678.1.
PIRiS16971.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61438 Genomic DNA. Translation: CAA43678.1.
PIRiS16971.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J71X-ray1.80A61-394[»]
ProteinModelPortaliQ00663.
SMRiQ00663. Positions 61-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi294747.XP_002548135.1.

Protein family/group databases

MEROPSiA01.037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.

Enzyme and pathway databases

BRENDAi3.4.23.24. 1146.

Miscellaneous databases

EvolutionaryTraceiQ00663.
PMAP-CutDBQ00663.

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. "Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalis."
    Togni G., Sanglard D., Falchetto R., Monod M.
    FEBS Lett. 286:181-185(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 61-88.
    Strain: ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400.
  2. "High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast."
    Symersky J., Monod M., Foundling S.I.
    Biochemistry 36:12700-12710(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 61-394 IN COMPLEX WITH SUBSTRATE PEPTIDE.
    Strain: ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400.

Entry informationi

Entry nameiCARP_CANTR
AccessioniPrimary (citable) accession number: Q00663
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 13, 2016
This is version 94 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.