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UniProtKB - Q00663 (CARP_CANTR)
Protein
Candidapepsin
Gene
SAPT1
Organism
Candida tropicalis (Yeast)
Status
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. EC:3.4.23.24
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 92 | 1 | ||
Active sitei | 278 | 1 |
GO - Molecular functioni
- aspartic-type endopeptidase activity Source: UniProtKB-KW
Keywordsi
Molecular function | Aspartyl protease, Hydrolase, Protease |
Enzyme and pathway databases
BRENDAi | 3.4.23.24, 1146 |
Protein family/group databases
MEROPSi | A01.037 |
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 |
Organismi | Candida tropicalis (Yeast) |
Taxonomic identifieri | 5482 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Candida/Lodderomyces clade › Candida |
Organism-specific databases
VEuPathDBi | FungiDB:CTRG_02432 |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 23 | Sequence analysisAdd BLAST | 23 | |
PropeptideiPRO_0000025867 | 24 – 60 | Activation peptide1 PublicationAdd BLAST | 37 | |
ChainiPRO_0000025868 | 61 – 394 | CandidapepsinAdd BLAST | 334 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 50 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 107 ↔ 119 | |||
Disulfide bondi | 314 ↔ 347 |
Post-translational modificationi
O-glycosylated.
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, ZymogenStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q00663 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q00663 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 74 – 381 | Peptidase A1PROSITE-ProRule annotationAdd BLAST | 308 |
Sequence similaritiesi
Belongs to the peptidase A1 family.Curated
Keywords - Domaini
SignalFamily and domain databases
CDDi | cd05474, SAP_like, 1 hit |
Gene3Di | 2.40.70.10, 2 hits |
InterProi | View protein in InterPro IPR001461, Aspartic_peptidase_A1 IPR001969, Aspartic_peptidase_AS IPR033121, PEPTIDASE_A1 IPR021109, Peptidase_aspartic_dom_sf IPR033876, SAP-like |
PANTHERi | PTHR47965, PTHR47965, 1 hit |
Pfami | View protein in Pfam PF00026, Asp, 1 hit |
PRINTSi | PR00792, PEPSIN |
SUPFAMi | SSF50630, SSF50630, 1 hit |
PROSITEi | View protein in PROSITE PS00141, ASP_PROTEASE, 2 hits PS51767, PEPTIDASE_A1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q00663-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 191 | V → D (PubMed:9335526).Curated | 1 | |
Sequence conflicti | 199 | S → D (PubMed:9335526).Curated | 1 | |
Sequence conflicti | 218 | C → L (PubMed:9335526).Curated | 1 | |
Sequence conflicti | 219 | D → Y (PubMed:9335526).Curated | 1 | |
Sequence conflicti | 322 | V → F (PubMed:9335526).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X61438 Genomic DNA Translation: CAA43678.1 |
PIRi | S16971 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X61438 Genomic DNA Translation: CAA43678.1 |
PIRi | S16971 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1J71 | X-ray | 1.80 | A | 61-394 | [»] | |
SMRi | Q00663 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | A01.037 |
Organism-specific databases
VEuPathDBi | FungiDB:CTRG_02432 |
Enzyme and pathway databases
BRENDAi | 3.4.23.24, 1146 |
Miscellaneous databases
EvolutionaryTracei | Q00663 |
PHI-basei | PHI:17 |
Family and domain databases
CDDi | cd05474, SAP_like, 1 hit |
Gene3Di | 2.40.70.10, 2 hits |
InterProi | View protein in InterPro IPR001461, Aspartic_peptidase_A1 IPR001969, Aspartic_peptidase_AS IPR033121, PEPTIDASE_A1 IPR021109, Peptidase_aspartic_dom_sf IPR033876, SAP-like |
PANTHERi | PTHR47965, PTHR47965, 1 hit |
Pfami | View protein in Pfam PF00026, Asp, 1 hit |
PRINTSi | PR00792, PEPSIN |
SUPFAMi | SSF50630, SSF50630, 1 hit |
PROSITEi | View protein in PROSITE PS00141, ASP_PROTEASE, 2 hits PS51767, PEPTIDASE_A1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CARP_CANTR | |
Accessioni | Q00663Primary (citable) accession number: Q00663 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 1992 |
Last sequence update: | December 1, 1992 | |
Last modified: | September 29, 2021 | |
This is version 112 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- Peptidase families
Classification of peptidase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families