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UniProtKB - O42778 (CARP8_CANAX)
Protein
Candidapepsin-8
Gene
SAP8
Organism
Candida albicans (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 | 107 | PROSITE-ProRule annotation | 1 | |
Active sitei | 292 | PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- aspartic-type endopeptidase activity Source: UniProtKB-KW
Keywordsi
Molecular function | Aspartyl protease, Hydrolase, Protease |
Protein family/group databases
MEROPSi | A01.066 |
Names & Taxonomyi
Protein namesi | Recommended name: Candidapepsin-8 (EC:3.4.23.24)Alternative name(s): ACP 8 Aspartate protease 8 Secreted aspartic protease 8 |
Gene namesi | Name:SAP8 |
Organismi | Candida albicans (Yeast) |
Taxonomic identifieri | 5476 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Candida/Lodderomyces clade › Candida |
Organism-specific databases
VEuPathDBi | FungiDB:C3_02510C_A FungiDB:CAWG_02575 |
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 – 25 | Sequence analysisAdd BLAST | 25 | |
PropeptideiPRO_0000025862 | 26 – ? | Activation peptideSequence analysis | ||
ChainiPRO_0000025863 | ? – 405 | Candidapepsin-8 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 50 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 122 ↔ 134 | By similarity | ||
Disulfide bondi | 327 ↔ 358 | By similarity |
Post-translational modificationi
O-glycosylated.By similarity
Keywords - PTMi
Disulfide bond, Glycoprotein, ZymogenFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 89 – 392 | Peptidase A1PROSITE-ProRule annotationAdd BLAST | 304 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 52 – 78 | DisorderedSequence analysisAdd BLAST | 27 |
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, 1 hit PS51767, PEPTIDASE_A1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O42778-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MVSIITFTKN VLVTLAFALL AQGLAIPEDI DKRAEKVVSL DFTVTRKPFN
60 70 80 90 100
ATAHGQHHQS QQQQQQQQQQ PAQKRGTVQT SLINEGPSYA ATITVGSNKQ
110 120 130 140 150
QQTVIVDTGS SDLWVVDSAA VCQVTYPGQS PTFCKQDGTY KPSSSTTSQN
160 170 180 190 200
LGKAFSIRYE DGSSSQGTVY KDTIGLGGAS ITNQQFADVT TTSVDQGILG
210 220 230 240 250
IGFTGDESSP TYDNVPVTLK KQGIINKNAY SLYLNSASAS SGTIIFGGVD
260 270 280 290 300
NAKYTGSLTA LPITSSNELR VQLSTINIAG TTVSASTTPV LDSGTTLTYF
310 320 330 340 350
SQTIADKLAA AVGAKWNSYY QLYTSSCNLA GNIVFNFAKG VTISVPLSEF
360 370 380 390 400
VLQDGNSCYF GVSRDSATIL GDNFLRRAYA VYDLDGNTIS LAQVKYTTSS
SISTL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF043330 Genomic DNA Translation: AAC69995.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF043330 Genomic DNA Translation: AAC69995.1 |
3D structure databases
SMRi | O42778 |
ModBasei | Search... |
Chemistry databases
ChEMBLi | CHEMBL6050 |
Protein family/group databases
MEROPSi | A01.066 |
Organism-specific databases
VEuPathDBi | FungiDB:C3_02510C_A FungiDB:CAWG_02575 |
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, 1 hit PS51767, PEPTIDASE_A1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CARP8_CANAX | |
Accessioni | O42778Primary (citable) accession number: O42778 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | June 1, 1998 | |
Last modified: | September 29, 2021 | |
This is version 90 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
Documents
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families