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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)DescriptionActionsGraphical viewLength
Active sitei921
Active sitei2781

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000002586724 – 60Activation peptide1 PublicationAdd BLAST37
ChainiPRO_000002586861 – 394CandidapepsinAdd BLAST334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi50N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi107 ↔ 119
Disulfide bondi314 ↔ 347

Post-translational modificationi

O-glycosylated.

Keywords - PTMi

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

Proteomic databases

PRIDEiQ00663.

Miscellaneous databases

PMAP-CutDBQ00663.

Interactioni

Protein-protein interaction databases

STRINGi294747.XP_002548135.1.

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi63 – 69Combined sources7
Beta strandi71 – 80Combined sources10
Turni81 – 84Combined sources4
Beta strandi85 – 92Combined sources8
Beta strandi98 – 107Combined sources10
Helixi118 – 120Combined sources3
Helixi127 – 129Combined sources3
Beta strandi134 – 144Combined sources11
Beta strandi149 – 161Combined sources13
Beta strandi164 – 181Combined sources18
Beta strandi183 – 185Combined sources3
Helixi189 – 191Combined sources3
Helixi201 – 207Combined sources7
Beta strandi212 – 219Combined sources8
Beta strandi226 – 232Combined sources7
Beta strandi234 – 236Combined sources3
Beta strandi239 – 248Combined sources10
Beta strandi252 – 254Combined sources3
Beta strandi256 – 264Combined sources9
Beta strandi267 – 277Combined sources11
Beta strandi282 – 286Combined sources5
Helixi288 – 298Combined sources11
Beta strandi301 – 303Combined sources3
Turni304 – 307Combined sources4
Beta strandi308 – 310Combined sources3
Beta strandi312 – 314Combined sources3
Beta strandi318 – 325Combined sources8
Beta strandi329 – 333Combined sources5
Helixi334 – 337Combined sources4
Beta strandi338 – 340Combined sources3
Beta strandi342 – 345Combined sources4
Beta strandi347 – 353Combined sources7
Helixi361 – 364Combined sources4
Beta strandi367 – 372Combined sources6
Turni373 – 376Combined sources4
Beta strandi377 – 383Combined sources7
Beta strandi391 – 393Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ00663.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini74 – 381Peptidase A1PROSITE-ProRule annotationAdd BLAST308

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

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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti191V → D (PubMed:9335526).Curated1
Sequence conflicti199S → D (PubMed:9335526).Curated1
Sequence conflicti218C → L (PubMed:9335526).Curated1
Sequence conflicti219D → Y (PubMed:9335526).Curated1
Sequence conflicti322V → F (PubMed:9335526).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J71X-ray1.80A61-394[»]
ProteinModelPortaliQ00663.
SMRiQ00663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi294747.XP_002548135.1.

Protein family/group databases

MEROPSiA01.037.

Proteomic databases

PRIDEiQ00663.

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

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 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: November 30, 2016
This is version 97 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.